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Low-density lipoprotein receptor (LDL receptor)

 LDLR_HUMAN              Reviewed;         860 AA.
P01130; B4DII3; B4DJZ8; B4DR00; B4DTQ3; C0JYY8; H0YLU8; H0YNT7;
Q53ZD9; Q59FQ1; Q9UDH7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 223.
RecName: Full=Low-density lipoprotein receptor;
Short=LDL receptor;
Flags: Precursor;
Name=LDLR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=6091915; DOI=10.1016/0092-8674(84)90188-0;
Yamamoto T., Davis C.G., Brown M.S., Schneider W.J., Casey M.L.,
Goldstein J.L., Russell D.W.;
"The human LDL receptor: a cysteine-rich protein with multiple Alu
sequences in its mRNA.";
Cell 39:27-38(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2988123; DOI=10.1126/science.2988123;
Suedhof T.C., Goldstein J.L., Brown M.S., Russell D.W.;
"The LDL receptor gene: a mosaic of exons shared with different
proteins.";
Science 228:815-822(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Jia S., Lv L., Sun H., Wang Q., Wang H., Zhan L., Yang Z.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6).
TISSUE=Hippocampus, Placenta, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D.,
Toth E.J., Krauss R.M., Nickerson D.A.;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 186-210; 394-405; 441-449; 472-495; 521-541 AND
605-617.
TISSUE=Cervix carcinoma;
PubMed=8127891; DOI=10.1073/pnas.91.5.1839;
Hofer F., Gruenberger M., Kowalski H., Machat H., Huettinger M.,
Kuechler E., Blaas D.;
"Members of the low density lipoprotein receptor family mediate cell
entry of a minor-group common cold virus.";
Proc. Natl. Acad. Sci. U.S.A. 91:1839-1842(1994).
[13]
FUNCTION, AND GLYCOSYLATION.
PubMed=3005267;
Davis C.G., Elhammer A., Russell D.W., Schneider W.J., Kornfeld S.,
Brown M.S., Goldstein J.L.;
"Deletion of clustered O-linked carbohydrates does not impair function
of low density lipoprotein receptor in transfected fibroblasts.";
J. Biol. Chem. 261:2828-2838(1986).
[14]
MUTAGENESIS OF CYTOPLASMIC DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=3104336;
Davis C.G., van Driel I.R., Russell D.W., Brown M.S., Goldstein J.L.;
"The low density lipoprotein receptor. Identification of amino acids
in cytoplasmic domain required for rapid endocytosis.";
J. Biol. Chem. 262:4075-4082(1987).
[15]
FUNCTION (MICROBIAL INFECTION) AS RECEPTOR OF HEPATITIS C VIRUS.
PubMed=10535997; DOI=10.1073/pnas.96.22.12766;
Agnello V., Abel G., Elfahal M., Knight G.B., Zhang Q.X.;
"Hepatitis C virus and other flaviviridae viruses enter cells via low
density lipoprotein receptor.";
Proc. Natl. Acad. Sci. U.S.A. 96:12766-12771(1999).
[16]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 TAT.
PubMed=11100124; DOI=10.1038/82199;
Liu Y., Jones M., Hingtgen C.M., Bu G., Laribee N., Tanzi R.E.,
Moir R.D., Nath A., He J.J.;
"Uptake of HIV-1 tat protein mediated by low-density lipoprotein
receptor-related protein disrupts the neuronal metabolic balance of
the receptor ligands.";
Nat. Med. 6:1380-1387(2000).
[17]
INTERACTION WITH LDLRAP1.
PubMed=12221107; DOI=10.1074/jbc.M208539200;
He G., Gupta S., Yi M., Michaely P., Hobbs H.H., Cohen J.C.;
"ARH is a modular adaptor protein that interacts with the LDL
receptor, clathrin, and AP-2.";
J. Biol. Chem. 277:44044-44049(2002).
[18]
INTERACTION WITH ARRB1, AND MUTAGENESIS OF TYR-828 AND SER-854.
PubMed=12944399; DOI=10.1074/jbc.M309450200;
Wu J.-H., Peppel K., Nelson C.D., Lin F.-T., Kohout T.A., Miller W.E.,
Exum S.T., Freedman N.J.;
"The adaptor protein beta-arrestin2 enhances endocytosis of the low
density lipoprotein receptor.";
J. Biol. Chem. 278:44238-44245(2003).
[19]
GLYCOSYLATION AT ASN-657.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[20]
FUNCTION (MICROBIAL INFECTION) AS RECEPTOR OF HEPATITIS C VIRUS.
PubMed=12615904; DOI=10.1084/jem.20021756;
Bartosch B., Dubuisson J., Cosset F.-L.;
"Infectious hepatitis C virus pseudo-particles containing functional
E1-E2 envelope protein complexes.";
J. Exp. Med. 197:633-642(2003).
[21]
INTERACTION WITH SNX17.
PubMed=14739284; DOI=10.1074/jbc.M313689200;
Burden J.J., Sun X.-M., Garcia Garcia A.B., Soutar A.K.;
"Sorting motifs in the intracellular domain of the low density
lipoprotein receptor interact with a novel domain of sorting nexin-
17.";
J. Biol. Chem. 279:16237-16245(2004).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[24]
SUBCELLULAR LOCATION, AND INTERACTION WITH PCSK9.
PubMed=17461796; DOI=10.1111/j.1600-0854.2007.00562.x;
Nassoury N., Blasiole D.A., Tebon Oler A., Benjannet S., Hamelin J.,
Poupon V., McPherson P.S., Attie A.D., Prat A., Seidah N.G.;
"The cellular trafficking of the secretory proprotein convertase PCSK9
and its dependence on the LDLR.";
Traffic 8:718-732(2007).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[26]
SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANT SAINT
OMER ASP-546, MUTAGENESIS OF LYS-811; LYS-816; LYS-830 AND CYS-839,
UBIQUITINATION, AND REGION.
PubMed=19520913; DOI=10.1126/science.1168974;
Zelcer N., Hong C., Boyadjian R., Tontonoz P.;
"LXR regulates cholesterol uptake through Idol-dependent
ubiquitination of the LDL receptor.";
Science 325:100-104(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
INTERACTION WITH PCSK9.
PubMed=21149300; DOI=10.1074/jbc.M110.199042;
Yamamoto T., Lu C., Ryan R.O.;
"A two-step binding model of PCSK9 interaction with the low density
lipoprotein receptor.";
J. Biol. Chem. 286:5464-5470(2011).
[29]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VESICULAR
STOMATITIS VIRUS GLYCOPROTEIN.
PubMed=23589850; DOI=10.1073/pnas.1214441110;
Finkelshtein D., Werman A., Novick D., Barak S., Rubinstein M.;
"LDL receptor and its family members serve as the cellular receptors
for vesicular stomatitis virus.";
Proc. Natl. Acad. Sci. U.S.A. 110:7306-7311(2013).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
STRUCTURE BY NMR OF 20-67.
PubMed=7603991; DOI=10.1073/pnas.92.14.6334;
Daly N.L., Scanlon M.J., Djordjevic J.T., Kroon P.A., Smith R.;
"Three-dimensional structure of a cysteine-rich repeat from the low-
density lipoprotein receptor.";
Proc. Natl. Acad. Sci. U.S.A. 92:6334-6338(1995).
[33]
STRUCTURE BY NMR OF 65-104.
PubMed=7578052; DOI=10.1021/bi00044a025;
Daly N.L., Djordjevic J.T., Kroon P.A., Smith R.;
"Three-dimensional structure of the second cysteine-rich repeat from
the human low-density lipoprotein receptor.";
Biochemistry 34:14474-14481(1995).
[34]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 196-232.
PubMed=9262405; DOI=10.1038/41798;
Fass D., Blacklow S.C., Kim P.S., Berger J.M.;
"Molecular basis of familial hypercholesterolaemia from structure of
LDL receptor module.";
Nature 388:691-693(1997).
[35]
STRUCTURE BY NMR OF 20-104, AND DISULFIDE BONDS.
PubMed=10933493; DOI=10.1110/ps.9.7.1282;
Kurniawan N.D., Atkins A.R., Bieri S., Brown C.J., Brereton I.M.,
Kroon P.A., Smith R.;
"NMR structure of a concatemer of the first and second ligand-binding
modules of the human low-density lipoprotein receptor.";
Protein Sci. 9:1282-1293(2000).
[36]
X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 22-720, AND DISULFIDE BONDS.
PubMed=12459547; DOI=10.1126/science.1078124;
Rudenko G., Henry L., Henderson K., Ichtchenko K., Brown M.S.,
Goldstein J.L., Deisenhofer J.;
"Structure of the LDL receptor extracellular domain at endosomal pH.";
Science 298:2353-2358(2002).
[37]
X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 819-832 IN COMPLEX WITH
LDLRAP1, INTERACTION WITH LDLRAP1, CHARACTERIZATION OF VARIANT FH
CYS-828, MUTAGENESIS OF ILE-821 AND GLN-829, TOPOLOGY, AND MOTIF.
PubMed=22509010; DOI=10.1073/pnas.1114128109;
Dvir H., Shah M., Girardi E., Guo L., Farquhar M.G., Zajonc D.M.;
"Atomic structure of the autosomal recessive hypercholesterolemia
phosphotyrosine-binding domain in complex with the LDL-receptor
tail.";
Proc. Natl. Acad. Sci. U.S.A. 109:6916-6921(2012).
[38]
REVIEW ON FH VARIANTS.
PubMed=1301956; DOI=10.1002/humu.1380010602;
Hobbs H.H., Brown M.S., Goldstein J.L.;
"Molecular genetics of the LDL receptor gene in familial
hypercholesterolemia.";
Hum. Mutat. 1:445-466(1992).
[39]
REVIEW ON FH VARIANTS.
PubMed=9016531; DOI=10.1093/nar/25.1.172;
Varret M., Rabes J.-P., Collod-Beroud G., Junien J., Boileau C.,
Beroud C.;
"Software and database for the analysis of mutations in the human LDL
receptor gene.";
Nucleic Acids Res. 25:172-180(1997).
[40]
VARIANT FH 47-ASP-GLY-48 DEL.
PubMed=3263645; DOI=10.1073/pnas.85.21.7912;
Leitersdorf E., Hobbs H.H., Fourie A.M., Jacobs M.,
van der Westhuyzen D.R., Coetzee G.A.;
"Deletion in the first cysteine-rich repeat of low density lipoprotein
receptor impairs its transport but not lipoprotein binding in
fibroblasts from a subject with familial hypercholesterolemia.";
Proc. Natl. Acad. Sci. U.S.A. 85:7912-7916(1988).
[41]
VARIANTS FH ASN-175; GLU-227 AND MET-429.
PubMed=2569482; DOI=10.1172/JCI114258;
Leitersdorf E., van der Westhuyzen D.R., Coetzee G.A., Hobbs H.H.;
"Two common low density lipoprotein receptor gene mutations cause
familial hypercholesterolemia in Afrikaners.";
J. Clin. Invest. 84:954-961(1989).
[42]
VARIANT FH CYS-828.
PubMed=3955657; DOI=10.1016/0092-8674(86)90533-7;
Davis C.G., Lehrman M.A., Russell D.W., Anderson R.G.W., Brown M.S.,
Goldstein J.L.;
"The J.D. mutation in familial hypercholesterolemia: amino acid
substitution in cytoplasmic domain impedes internalization of LDL
receptors.";
Cell 45:15-24(1986).
[43]
VARIANTS FH TYR-90 AND LYS-140.
PubMed=8347689; DOI=10.1016/0925-4439(93)90156-U;
Rubinsztein D.C., Jialal I., Leitersdorf E., Coetzee G.A.,
van der Westhuyzen D.R.;
"Identification of two new LDL-receptor mutations causing homozygous
familial hypercholesterolemia in a South African of Indian origin.";
Biochim. Biophys. Acta 1182:75-82(1993).
[44]
VARIANTS FH GLY-87; LYS-228 AND TYR-667.
PubMed=2318961; DOI=10.1172/JCI114531;
Leitersdorf E., Tobin E.J., Davignon J., Hobbs H.H.;
"Common low-density lipoprotein receptor mutations in the French
Canadian population.";
J. Clin. Invest. 85:1014-1023(1990).
[45]
VARIANT FH HIS-433.
PubMed=1446662; DOI=10.1111/j.1432-1033.1992.tb17383.x;
Miyake Y., Tajima S., Funahashi T., Yamamura T., Yamamoto A.;
"A point mutation of low-density-lipoprotein receptor causing rapid
degradation of the receptor.";
Eur. J. Biochem. 210:1-7(1992).
[46]
VARIANT FH GLY-218 DEL.
PubMed=1867200;
Meiner V., Landsberger D., Berkman N., Reshef A., Segal P.,
Seftel H.C., van der Westhuyzen D.R., Jeenah M.S., Coetzee G.A.,
Leitersdorf E.;
"A common Lithuanian mutation causing familial hypercholesterolemia in
Ashkenazi Jews.";
Am. J. Hum. Genet. 49:443-449(1991).
[47]
VARIANT FH HIS-168.
PubMed=8462973; DOI=10.1007/BF00222714;
Leitersdorf E., Reshef A., Meiner V., Dann E.J., Beigel Y.,
van Roggen F.G., van der Westhuyzen D.R., Coetzee G.A.;
"A missense mutation in the low density lipoprotein receptor gene
causes familial hypercholesterolemia in Sephardic Jews.";
Hum. Genet. 91:141-147(1993).
[48]
VARIANT FH PHE-318.
PubMed=8168830; DOI=10.1007/BF00202819;
Lelli N., Garuti R., Pedrazzi P., Ghisellini M., Simone M.L.,
Tiozzo R., Cattin L., Valenti M., Rolleri M., Bertolini S.,
Stefanutti C., Calandra S.;
"A new missense mutation (Cys297-->Phe) of the low density lipoprotein
receptor in Italian patients with familial hypercholesterolemia
(FHTrieste).";
Hum. Genet. 93:538-540(1994).
[49]
VARIANT FH LEU-685.
PubMed=2726768; DOI=10.1073/pnas.86.11.4166;
Soutar A.K., Knight B.L., Patel D.D.;
"Identification of a point mutation in growth factor repeat C of the
low density lipoprotein-receptor gene in a patient with homozygous
familial hypercholesterolemia that affects ligand binding and
intracellular movement of receptors.";
Proc. Natl. Acad. Sci. U.S.A. 86:4166-4170(1989).
[50]
VARIANT FH LEU-685.
PubMed=1464748;
Rubinsztein D.C., Coetzee G.A., Marais A.D., Leitersdorf E.,
Seftel H.C., van der Westhuyzen D.R.;
"Identification and properties of the proline664-leucine mutant LDL
receptor in South Africans of Indian origin.";
J. Lipid Res. 33:1647-1655(1992).
[51]
VARIANTS FH PORI HIS-401 AND TURKU ASP-844.
PubMed=7573037;
Koivisto U.-M., Viikari J.S., Kontula K.;
"Molecular characterization of minor gene rearrangements in Finnish
patients with heterozygous familial hypercholesterolemia:
identification of two common missense mutations (Gly823-->Asp and
Leu380-->His) and eight rare mutations of the LDL receptor gene.";
Am. J. Hum. Genet. 57:789-797(1995).
[52]
VARIANTS FH LYS-140; SER-338 AND LEU-685.
PubMed=7583548; DOI=10.1161/01.ATV.15.10.1713;
Maruyama T., Miyake Y., Tajima S., Harada-Shiba M., Yamamura T.,
Tsushima M., Kishino B., Horiguchi Y., Funahashi T., Matsuzawa Y.,
Yamamoto A.;
"Common mutations in the low-density-lipoprotein-receptor gene causing
familial hypercholesterolemia in the Japanese population.";
Arterioscler. Thromb. Vasc. Biol. 15:1713-1718(1995).
[53]
VARIANT FH FRENCH HIS-564.
PubMed=7550239; DOI=10.1002/humu.1380060117;
Tricot-Guerber F., Saint-Jore B., Valenti K., Foulon T., Bost M.,
Hadjian A.J.;
"Identification of a mutation, N543H, in exon 11 of the low-density
lipoprotein receptor gene in a French family with familial
hypercholesterolemia.";
Hum. Mutat. 6:87-88(1995).
[54]
VARIANTS FH LYS-277; THR-423 AND ASN-579.
PubMed=7635461; DOI=10.1007/BF00207370;
Ekstroem U., Abrahamson M., Sveger T., Lombardi P., Nilsson-Ehle P.;
"An efficient screening procedure detecting six novel mutations in the
LDL receptor gene in Swedish children with hypercholesterolemia.";
Hum. Genet. 96:147-150(1995).
[55]
VARIANT FH NORWEGIAN ASN-487 DEL.
PubMed=7635482; DOI=10.1007/BF00207391;
Leren T.P., Solberg K., Rodningen O.K., Tonstad S., Ose L.;
"Two novel point mutations in the EGF precursor homology domain of the
LDL receptor gene causing familial hypercholesterolemia.";
Hum. Genet. 96:241-242(1995).
[56]
VARIANTS FH COLOGNE GLY-221; TYR-221 AND VAL-224.
PubMed=7649546;
Geisel J., Holzem G., Oette K.;
"Screening for mutations in exon 4 of the LDL receptor gene in a
German population with severe hypercholesterolemia.";
Hum. Genet. 96:301-304(1995).
[57]
VARIANTS FH LA HABANA LYS-277; MET-429 AND MET-797.
PubMed=7649549; DOI=10.1007/BF00210415;
Pereira E., Ferreira R., Hermelin B., Thomas G., Bernard C.,
Bertrand V., Nassiff H., Mendez del Castillo D., Bereziat G.,
Benlian P.;
"Recurrent and novel LDL receptor gene mutations causing heterozygous
familial hypercholesterolemia in La Habana.";
Hum. Genet. 96:319-322(1995).
[58]
VARIANTS FH TYR-168 AND ARG-366.
PubMed=8740918;
Gundersen K.E., Solberg K., Rodningen O.K., Tonstad S., Ose L.,
Berg K., Leren T.P.;
"Two novel missense mutations in the LDL receptor gene causing
familial hypercholesterolemia.";
Clin. Genet. 49:85-87(1996).
[59]
VARIANT FH GLY-231.
PubMed=8664907;
DOI=10.1002/(SICI)1098-1004(1996)7:1<70::AID-HUMU12>3.3.CO;2-G;
Sundvold H., Solberg K., Tonstad S., Rodningen O.K., Ose L., Berg K.,
Leren T.P.;
"A common missense mutation (C210G) in the LDL receptor gene among
Norwegian familial hypercholesterolemia subjects.";
Hum. Mutat. 7:70-71(1996).
[60]
VARIANTS FH ARG-197; TYR-248; ALA-301; TRP-302 AND PRO-350.
PubMed=9026534;
Webb J.C., Sun X.-M., McCarthy S.N., Neuwirth C., Thompson G.R.,
Knigh B., Soutar A.K.;
"Characterization of mutations in the low density lipoprotein (LDL)-
receptor gene in patients with homozygous familial
hypercholesterolemia, and frequency of these mutations in FH patients
in the United Kingdom.";
J. Lipid Res. 37:368-381(1996).
[61]
VARIANT FH LEU-685.
PubMed=9254862; DOI=10.1007/s004390050503;
Peeters A.V., van Gaal L.F., du Plessis L., Lombardi M.P.R.,
Havekes L.M., Kotze M.J.;
"Mutational and genetic origin of LDL receptor gene mutations detected
in both Belgian and Dutch familial hypercholesterolemics.";
Hum. Genet. 100:266-270(1997).
[62]
VARIANTS FH HIS-564 AND 799-LEU--PHE-801 DEL.
PubMed=9143924;
DOI=10.1002/(SICI)1098-1004(1997)9:5<437::AID-HUMU10>3.0.CO;2-3;
Jensen H.K., Jensen T.G., Faergeman O., Jensen L.G., Andresen B.S.,
Corydon M.J., Andreasen P.H., Hansen P.S., Heath F., Bolund L.,
Gregersen N.;
"Two mutations in the same low-density lipoprotein receptor allele act
in synergy to reduce receptor function in heterozygous familial
hypercholesterolemia.";
Hum. Mutat. 9:437-444(1997).
[63]
VARIANTS FH TRP-27; CYS-78; GLY-87; TYR-89; ASN-90; GLY-90; LYS-101;
TYR-160; ASN-168; LEU-177; GLY-221; GLU-227; ARG-286; TYR-313;
TYR-327; ASN-342; PRO-350; ASP-399; TRP-416; HIS-482; ARG-483;
SER-526; ASP-549; CYS-633; LEU-649 AND ILE-726.
PubMed=9259195;
DOI=10.1002/(SICI)1098-1004(1997)10:2<116::AID-HUMU4>3.3.CO;2-#;
Day I.N.M., Whittall R.A., O'Dell S.D., Haddad L., Bolla M.K.,
Gudnason V., Humphries S.E.;
"Spectrum of LDL receptor gene mutations in heterozygous familial
hypercholesterolemia.";
Hum. Mutat. 10:116-127(1997).
[64]
VARIANTS FH PRO-56; TYR-175; TYR-356; VAL-401 AND TRP-416.
PubMed=9104431; DOI=10.1046/j.1365-2796.1997.78119000.x;
Leren T.P., Tonstad S., Gundersen K.E., Bakken K.S., Rodningen O.K.,
Sundvold H., Ose L., Berg K.;
"Molecular genetics of familial hypercholesterolaemia in Norway.";
J. Intern. Med. 241:185-194(1997).
[65]
VARIANTS FH LEU-177; GLY-218 DEL; SER-564 AND GLU-592.
PubMed=9654205; DOI=10.1007/s004390050740;
Gorski B., Kubalska J., Naruszewicz M., Lubinski J.;
"LDL-R and Apo-B-100 gene mutations in Polish familial
hypercholesterolemias.";
Hum. Genet. 102:562-565(1998).
[66]
VARIANTS FH TRP-173 AND ARG-368.
PubMed=9452094;
Couture P., Vohl M.-C., Gagne C., Gaudet D., Torres A.L., Lupien P.J.,
Despres J.-P., Labrie F., Simard J., Moorjani S.;
"Identification of three mutations in the low-density lipoprotein
receptor gene causing familial hypercholesterolemia among French
Canadians.";
Hum. Mutat. Suppl. 1:S226-S231(1998).
[67]
VARIANTS FH GLN-416 AND MET-429.
PubMed=9452095;
Thiart R., Loubser O., de Villiers J.N.P., Marx M.P., Zaire R.,
Raal F.J., Kotze M.J.;
"Two novel and two known low-density lipoprotein receptor gene
mutations in German patients with familial hypercholesterolemia.";
Hum. Mutat. Suppl. 1:S232-S233(1998).
[68]
VARIANTS FH TYR-329; ARG-414 AND MET-429.
PubMed=9452118;
Mak Y.T., Zhang J., Chan Y.S., Mak T.W.L., Tomlinson B.,
Masarei J.R.L., Pang C.P.;
"Possible common mutations in the low density lipoprotein receptor
gene in Chinese.";
Hum. Mutat. Suppl. 1:S310-S313(1998).
[69]
VARIANTS FH GLU-92; GLY-95; ARG-116; LEU-177; GLY-221; TYR-221;
LYS-277; TYR-302; LYS-434; TYR-667 AND GLU-700.
PubMed=10206683;
DOI=10.1002/(SICI)1098-1004(1998)11:5<413::AID-HUMU17>3.3.CO;2-6;
Cenarro A., Jensen H.K., Casao E., Civeira F., Gonzalez-Bonillo J.,
Rodriguez-Rey J.C., Gregersen N., Pocovi M.;
"Identification of recurrent and novel mutations in the LDL receptor
gene in Spanish patients with familial hypercholesterolemia.";
Hum. Mutat. 11:413-413(1998).
[70]
VARIANT FH CHIETI-3 GLU-228 DELINS CYS-LYS.
PubMed=10660340;
Motti C., Bertolini S., Rampa P., Trovatello G., Liberatoscioli L.,
Calandra S., Federici G., Cortese C.;
"Two novel mutations consisting in minor gene rearrangements in the
human low density lipoprotein receptor gene in Italian patients
affected by familial hypercholesterolemia.";
Hum. Mutat. 12:290-290(1998).
[71]
VARIANT FH TYR-276.
Vergopoulos A., Bajari T., Jouma M., Aydin A., Boehring S., Luft F.C.,
Schuster H.;
"A novel single amino acid substitution in exon 6 of the low-density
lipoprotein receptor gene in a Syrian family.";
Hum. Mutat. 12:365-365(1998).
[72]
VARIANTS FH TYR-379 AND SER-608.
PubMed=9852677; DOI=10.1007/s100380050083;
Hirayama T., Yamaki E., Hata A., Tsuji M., Hashimoto K., Yamamoto M.,
Emi M.;
"Five familial hypercholesterolemic kindreds in Japan with novel
mutations of the LDL receptor gene.";
J. Hum. Genet. 43:250-254(1998).
[73]
VARIANT FH GLASCO TYR-184.
PubMed=9678702; DOI=10.1136/jmg.35.7.573;
Lee W.K., Haddad L., Macleod M.J., Dorrance A.M., Wilson D.J.,
Gaffney D., Dominiczak M.H., Packard C.J., Day I.N., Humphries S.E.,
Dominiczak A.F.;
"Identification of a common low density lipoprotein receptor mutation
(C163Y) in the west of Scotland.";
J. Med. Genet. 35:573-578(1998).
[74]
VARIANTS FH GLY-87; LYS-140; ASN-172; ARG-243; LEU-306; PRO-404;
HIS-564; SER-577; ASN-579; ILE-726 AND LYS-825.
PubMed=10532689; DOI=10.1016/S0021-9150(99)00158-6;
Jensen H.K., Jensen L.G., Meinertz H., Hansen P.S., Gregersen N.,
Faergeman O.;
"Spectrum of LDL receptor gene mutations in Denmark: implications for
molecular diagnostic strategy in heterozygous familial
hypercholesterolemia.";
Atherosclerosis 146:337-344(1999).
[75]
VARIANT FH PHE-261.
PubMed=10422803; DOI=10.1034/j.1399-0004.1999.550506.x;
Ekstroem U., Abrahamson M., Floren C.-H., Tollig H., Wettrell G.,
Nilsson G., Sun X.-M., Soutar A.K., Nilsson-Ehle P.;
"An individual with a healthy phenotype in spite of a pathogenic LDL
receptor mutation (C240F).";
Clin. Genet. 55:332-339(1999).
[76]
VARIANTS FH SER-50; ASN-221; LYS-288; VAL-432 AND HIS-564.
PubMed=10090484;
DOI=10.1002/(SICI)1098-1004(1999)13:3<257::AID-HUMU14>3.3.CO;2-4;
Ebhardt M., Schmidt H., Doerk T., Tietge U., Haas R., Manns M.-P.,
Schmidtke J., Stuhrmann M.;
"Mutation analysis in 46 German families with familial
hypercholesterolemia: identification of 8 new mutations.";
Hum. Mutat. 13:257-257(1999).
[77]
VARIANTS FH SER-338; LEU-403; THR-431; VAL-568 AND LYS-714.
PubMed=10447263;
DOI=10.1002/(SICI)1098-1004(1999)14:1<87::AID-HUMU13>3.3.CO;2-H;
Hattori H., Nagano M., Iwata F., Homma Y., Egashira T., Okada T.;
"Identification of recurrent and novel mutations in the LDL receptor
gene in Japanese familial hypercholesterolemia.";
Hum. Mutat. 14:87-87(1999).
[78]
VARIANTS ARG-2; ILE-468 AND GLN-814.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[79]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[80]
VARIANTS FH PHE-134; TRP-134; TYR-222; PRO-254; ARG-276; ARG-318;
THR-370; GLY-415 AND TYR-579.
PubMed=10978268; DOI=10.1161/01.ATV.20.9.e41;
Bertolini S., Cantafora A., Averna M., Cortese C., Motti C.,
Martini S., Pes G., Postiglione A., Stefanutti C., Blotta I.,
Pisciotta L., Rolleri M., Langheim S., Ghisellini M., Rabbone I.,
Calandra S.;
"Clinical expression of familial hypercholesterolemia in clusters of
mutations of the LDL receptor gene that cause a receptor-defective or
receptor-negative phenotype.";
Arterioscler. Thromb. Vasc. Biol. 20:E41-E52(2000).
[81]
VARIANT FH THR-451.
PubMed=10980548;
DOI=10.1002/1098-1004(200009)16:3<277::AID-HUMU24>3.0.CO;2-Y;
Miltiadous G., Elisaf M., Xenophontos S., Manoli P., Cariolou M.A.;
"Segregation of a novel LDLR gene mutation (I430T) with familial
hypercholesterolaemia in a Greek pedigree.";
Hum. Mutat. 16:277-277(2000).
[82]
VARIANT FH 47-ASP-GLY-48 DEL, AND VARIANTS HIS-172; TRP-253; GLN-406;
LYS-408; LEU-699 AND GLN-814.
PubMed=10882754; DOI=10.1136/jmg.37.7.514;
Thiart R., Scholtz C.L., Vergotine J., Hoogendijk C.F.,
de Villiers J.N.P., Nissen H., Brusgaard K., Gaffney D., Hoffs M.S.,
Vermaak W.J.H., Kotze M.J.;
"Predominance of a 6 bp deletion in exon 2 of the LDL receptor gene in
Africans with familial hypercholesterolaemia.";
J. Med. Genet. 37:514-519(2000).
[83]
VARIANT FH SER-46.
PubMed=11298688; DOI=10.1034/j.1399-0004.2001.590414.x;
Takahashi M., Ikeda U., Takahashi S., Hattori H., Iwasaki T.,
Ishihara M., Egashira T., Honma S., Asano Y., Shimada K.A.;
"A novel mutation in exon 2 of the low-density lipoprotein-receptor
gene in a patient with homozygous familial hypercholesterolemia.";
Clin. Genet. 59:290-292(2001).
[84]
INVOLVEMENT IN FH, VARIANTS FH ARG-143; TYR-148; TRP-184; CYS-574;
ASP-639 AND ASP-806, AND VARIANTS TRP-257 AND ILE-742.
PubMed=11462246; DOI=10.1002/humu.1171;
Nauck M.S., Koester W., Doerfer K., Eckes J., Scharnagl H.,
Gierens H., Nissen H., Nauck M.A., Wieland H., Maerz W.;
"Identification of recurrent and novel mutations in the LDL receptor
gene in German patients with familial hypercholesterolemia.";
Hum. Mutat. 18:165-166(2001).
[85]
VARIANTS FH TYR-89; LYS-101; GLY-218 DEL; GLY-221; ASN-221; TYR-358;
PRO-479; HIS-482; ARG-677 AND LEU-685, AND FUNCTION.
PubMed=17142622; DOI=10.1136/jmg.2006.038356;
Simon Broome familial hyperlipidemia register group and scientific steering committee;
Humphries S.E., Whittall R.A., Hubbart C.S., Maplebeck S.,
Cooper J.A., Soutar A.K., Naoumova R., Thompson G.R., Seed M.,
Durrington P.N., Miller J.P., Betteridge D.J.B., Neil H.A.W.;
"Genetic causes of familial hypercholesterolaemia in patients in the
UK: relation to plasma lipid levels and coronary heart disease risk.";
J. Med. Genet. 43:943-949(2006).
[86]
VARIANTS FH THR-50; LEU-211; GLY-221; GLU-266; LYS-277; ARG-286;
ARG-314; ARG-352; LYS-408; THR-431; HIS-442; MET-523; GLY-577; THR-585
AND LEU-685.
PubMed=17347910; DOI=10.1007/s10545-007-0563-5;
Widhalm K., Dirisamer A., Lindemayr A., Kostner G.;
"Diagnosis of families with familial hypercholesterolaemia and/or Apo
B-100 defect by means of DNA analysis of LDL-receptor gene
mutations.";
J. Inherit. Metab. Dis. 30:239-247(2007).
[87]
VARIANTS FH TYR-155; GLY-300; GLY-301; TRP-416 AND ASN-454.
PubMed=19318025; DOI=10.1016/j.clinbiochem.2009.01.017;
Alonso R., Defesche J.C., Tejedor D., Castillo S., Stef M., Mata N.,
Gomez-Enterria P., Martinez-Faedo C., Forga L., Mata P.;
"Genetic diagnosis of familial hypercholesterolemia using a DNA-array
based platform.";
Clin. Biochem. 42:899-903(2009).
[88]
VARIANTS FH PRO-254; TYR-356; TYR-358; THR-451 AND SER-826.
PubMed=19319977; DOI=10.1002/humu.21002;
Abifadel M., Rabes J.-P., Jambart S., Halaby G., Gannage-Yared M.-H.,
Sarkis A., Beaino G., Varret M., Salem N., Corbani S., Aydenian H.,
Junien C., Munnich A., Boileau C.;
"The molecular basis of familial hypercholesterolemia in Lebanon:
spectrum of LDLR mutations and role of PCSK9 as a modifier gene.";
Hum. Mutat. 30:E682-E691(2009).
[89]
VARIANTS HIS-139; LYS-201; SER-255; ASN-304 AND GLY-471.
PubMed=21418584; DOI=10.1186/1471-2350-12-40;
Al-Khateeb A., Zahri M.K., Mohamed M.S., Sasongko T.H., Ibrahim S.,
Yusof Z., Zilfalil B.A.;
"Analysis of sequence variations in low-density lipoprotein receptor
gene among Malaysian patients with familial hypercholesterolemia.";
BMC Med. Genet. 12:40-40(2011).
[90]
VARIANT FH PHE-329.
PubMed=22160468; DOI=10.1007/s11033-011-1314-0;
Walus-Miarka M., Sanak M., Idzior-Walus B., Miarka P., Witek P.,
Malecki M.T., Czarnecka D.;
"A novel mutation (Cys308Phe) of the LDL receptor gene in families
from the South-Eastern part of Poland.";
Mol. Biol. Rep. 39:5181-5186(2012).
[91]
VARIANTS FH TYR-160; ALA-168; LEU-177; TYR-184; GLY-221; GLN-228;
LYS-228; TRP-276; TYR-285; GLY-301; PHE-318; CYS-326; SER-343;
TYR-368; ASP-373; TRP-406; MET-429; ASN-492; ASP-549; HIS-564;
HIS-574; TRP-595; HIS-601; LEU-685; LEU-699; MET-797 AND GLN-814.
PubMed=24529145; DOI=10.1016/j.atherosclerosis.2013.12.028;
Santos P.C., Morgan A.C., Jannes C.E., Turolla L., Krieger J.E.,
Santos R.D., Pereira A.C.;
"Presence and type of low density lipoprotein receptor (LDLR) mutation
influences the lipid profile and response to lipid-lowering therapy in
Brazilian patients with heterozygous familial hypercholesterolemia.";
Atherosclerosis 233:206-210(2014).
[92]
CHARACTERIZATION OF VARIANTS FH ARG-116; ASN-168; ASN-172; GLY-300 AND
GLY-301, AND CHARACTERIZATION OF VARIANT TRP-257.
PubMed=25545329; DOI=10.1016/j.atherosclerosis.2014.12.026;
Etxebarria A., Benito-Vicente A., Stef M., Ostolaza H., Palacios L.,
Martin C.;
"Activity-associated effect of LDL receptor missense variants located
in the cysteine-rich repeats.";
Atherosclerosis 238:304-312(2015).
[93]
CHARACTERIZATION OF VARIANTS FH TYR-155; TRP-416; ASN-454; GLY-577 AND
LYS-825.
PubMed=25378237; DOI=10.1002/humu.22721;
Etxebarria A., Benito-Vicente A., Palacios L., Stef M., Cenarro A.,
Civeira F., Ostolaza H., Martin C.;
"Functional characterization and classification of frequent low-
density lipoprotein receptor variants.";
Hum. Mutat. 36:129-141(2015).
-!- FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of
plasma, and transports it into cells by endocytosis. In order to
be internalized, the receptor-ligand complexes must first cluster
into clathrin-coated pits. {ECO:0000269|PubMed:3005267,
ECO:0000269|PubMed:6091915}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
virus in hepatocytes, but not through a direct interaction with
viral proteins (PubMed:10535997, PubMed:12615904). Acts as a
receptor for vesicular stomatitis virus (PubMed:23589850). In case
of HIV-1 infection, may function as a receptor for extracellular
Tat in neurons, mediating its internalization in uninfected cells
(PubMed:11100124). {ECO:0000269|PubMed:10535997,
ECO:0000269|PubMed:11100124, ECO:0000269|PubMed:12615904,
ECO:0000269|PubMed:23589850}.
-!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain);
the interaction is impaired by tyrosine phosphorylation of the
NPXY motif (By similarity). Interacts (via NPXY motif) with
LDLRAP1 (via PID domain) (PubMed:12221107, PubMed:22509010).
Interacts with ARRB1 (PubMed:12944399). Interacts with SNX17
(PubMed:14739284). Interacts with the full-length immature form of
PCSK9 (via C-terminus) (PubMed:17461796, PubMed:21149300).
{ECO:0000250|UniProtKB:P35951, ECO:0000269|PubMed:12221107,
ECO:0000269|PubMed:12944399, ECO:0000269|PubMed:14739284,
ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:21149300,
ECO:0000269|PubMed:22509010}.
-!- SUBUNIT: (Microbial infection) Interacts with vesicular stomatitis
virus glycoprotein. {ECO:0000269|PubMed:23589850}.
-!- SUBUNIT: (Microbial infection) May interact with HIV-1 Tat.
{ECO:0000269|PubMed:11100124}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-988319, EBI-988319;
P04114:APOB; NbExp=4; IntAct=EBI-988319, EBI-3926040;
P02649:APOE; NbExp=2; IntAct=EBI-988319, EBI-1222467;
P02749:APOH; NbExp=3; IntAct=EBI-988319, EBI-2114682;
D3ZAR1:Ldlrap1 (xeno); NbExp=3; IntAct=EBI-988319, EBI-9250714;
Q8NBP7:PCSK9; NbExp=10; IntAct=EBI-988319, EBI-7539251;
Q8NBP7-1:PCSK9; NbExp=4; IntAct=EBI-988319, EBI-15656131;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17461796,
ECO:0000269|PubMed:19520913}; Single-pass type I membrane protein
{ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit
{ECO:0000303|PubMed:6091915}. Golgi apparatus
{ECO:0000269|PubMed:17461796}. Early endosome
{ECO:0000269|PubMed:17461796}. Late endosome
{ECO:0000269|PubMed:17461796}. Lysosome
{ECO:0000269|PubMed:17461796}. Note=Rapidly endocytosed upon
ligand binding. {ECO:0000269|PubMed:3104336}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=P01130-1; Sequence=Displayed;
Name=2;
IsoId=P01130-2; Sequence=VSP_043053, VSP_043054;
Note=No experimental confirmation available.;
Name=3;
IsoId=P01130-3; Sequence=VSP_055014, VSP_055015;
Note=No experimental confirmation available.;
Name=4;
IsoId=P01130-4; Sequence=VSP_043595;
Note=No experimental confirmation available.;
Name=5;
IsoId=P01130-5; Sequence=VSP_045525;
Note=No experimental confirmation available.;
Name=6;
IsoId=P01130-6; Sequence=VSP_047413;
Note=No experimental confirmation available.;
-!- DOMAIN: The NPXY motif mediates the interaction with the clathrin
adapter DAB2 and with LDLRAP1 which are involved in receptor
internalization. A few residues outside the motif also play a role
in the interaction. {ECO:0000269|PubMed:22509010}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:3005267}.
-!- PTM: Ubiquitinated by MYLIP leading to degradation.
{ECO:0000269|PubMed:19520913}.
-!- DISEASE: Familial hypercholesterolemia (FH) [MIM:143890]: Common
autosomal semi-dominant disease that affects about 1 in 500
individuals. The receptor defect impairs the catabolism of LDL,
and the resultant elevation in plasma LDL-cholesterol promotes
deposition of cholesterol in the skin (xanthelasma), tendons
(xanthomas), and coronary arteries (atherosclerosis).
{ECO:0000269|PubMed:10090484, ECO:0000269|PubMed:10206683,
ECO:0000269|PubMed:10422803, ECO:0000269|PubMed:10447263,
ECO:0000269|PubMed:10532689, ECO:0000269|PubMed:10660340,
ECO:0000269|PubMed:10882754, ECO:0000269|PubMed:10978268,
ECO:0000269|PubMed:10980548, ECO:0000269|PubMed:11298688,
ECO:0000269|PubMed:11462246, ECO:0000269|PubMed:1446662,
ECO:0000269|PubMed:1464748, ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:17347910, ECO:0000269|PubMed:1867200,
ECO:0000269|PubMed:19318025, ECO:0000269|PubMed:19319977,
ECO:0000269|PubMed:22160468, ECO:0000269|PubMed:22509010,
ECO:0000269|PubMed:2318961, ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:25378237, ECO:0000269|PubMed:25545329,
ECO:0000269|PubMed:2569482, ECO:0000269|PubMed:2726768,
ECO:0000269|PubMed:3263645, ECO:0000269|PubMed:3955657,
ECO:0000269|PubMed:7550239, ECO:0000269|PubMed:7573037,
ECO:0000269|PubMed:7583548, ECO:0000269|PubMed:7635461,
ECO:0000269|PubMed:7635482, ECO:0000269|PubMed:7649546,
ECO:0000269|PubMed:7649549, ECO:0000269|PubMed:8168830,
ECO:0000269|PubMed:8347689, ECO:0000269|PubMed:8462973,
ECO:0000269|PubMed:8664907, ECO:0000269|PubMed:8740918,
ECO:0000269|PubMed:9026534, ECO:0000269|PubMed:9104431,
ECO:0000269|PubMed:9143924, ECO:0000269|PubMed:9254862,
ECO:0000269|PubMed:9259195, ECO:0000269|PubMed:9452094,
ECO:0000269|PubMed:9452095, ECO:0000269|PubMed:9452118,
ECO:0000269|PubMed:9654205, ECO:0000269|PubMed:9678702,
ECO:0000269|PubMed:9852677, ECO:0000269|Ref.71}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92646.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=LDLR; Note=LDLR mutation database;
URL="http://www.ucl.ac.uk/fh/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=LDLR";
-----------------------------------------------------------------------
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EMBL; L00352; AAA56833.1; -; Genomic_DNA.
EMBL; L00336; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00337; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00338; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00339; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00340; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00341; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00343; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00344; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00345; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00346; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00347; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00348; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00349; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00350; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L00351; AAA56833.1; JOINED; Genomic_DNA.
EMBL; L29401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY114155; AAM56036.1; -; mRNA.
EMBL; AK295612; BAG58495.1; -; mRNA.
EMBL; AK296312; BAG59010.1; -; mRNA.
EMBL; AK299038; BAG61112.1; -; mRNA.
EMBL; AK300313; BAG62065.1; -; mRNA.
EMBL; BT007361; AAP36025.1; -; mRNA.
EMBL; AY324609; AAP72971.1; -; Genomic_DNA.
EMBL; AB209409; BAD92646.1; ALT_INIT; mRNA.
EMBL; FJ525879; ACN81317.1; -; Genomic_DNA.
EMBL; AC011485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84169.1; -; Genomic_DNA.
EMBL; BC014514; AAH14514.1; -; mRNA.
CCDS; CCDS12254.1; -. [P01130-1]
CCDS; CCDS56083.1; -. [P01130-2]
CCDS; CCDS56084.1; -. [P01130-3]
CCDS; CCDS56085.1; -. [P01130-4]
CCDS; CCDS58651.1; -. [P01130-5]
PIR; A01383; QRHULD.
RefSeq; NP_000518.1; NM_000527.4. [P01130-1]
RefSeq; NP_001182727.1; NM_001195798.1. [P01130-5]
RefSeq; NP_001182728.1; NM_001195799.1. [P01130-4]
RefSeq; NP_001182729.1; NM_001195800.1. [P01130-3]
RefSeq; NP_001182732.1; NM_001195803.1. [P01130-2]
UniGene; Hs.213289; -.
UniGene; Hs.713981; -.
PDB; 1AJJ; X-ray; 1.70 A; A=196-232.
PDB; 1D2J; NMR; -; A=233-272.
PDB; 1F5Y; NMR; -; A=22-104.
PDB; 1F8Z; NMR; -; A=234-272.
PDB; 1HJ7; NMR; -; A=314-393.
PDB; 1HZ8; NMR; -; A=314-395.
PDB; 1I0U; NMR; -; A=314-395.
PDB; 1IJQ; X-ray; 1.50 A; A/B=398-713.
PDB; 1LDL; NMR; -; A=20-67.
PDB; 1LDR; NMR; -; A=64-104.
PDB; 1LRX; Model; -; B=396-659.
PDB; 1N7D; X-ray; 3.70 A; A=22-720.
PDB; 1XFE; NMR; -; A=272-353.
PDB; 2FCW; X-ray; 1.26 A; B=107-186.
PDB; 2KRI; NMR; -; B=147-186.
PDB; 2LGP; NMR; -; A=144-235.
PDB; 2M7P; NMR; -; A=82-104.
PDB; 2MG9; NMR; -; A=314-339.
PDB; 2W2M; X-ray; 2.40 A; E=314-393.
PDB; 2W2N; X-ray; 2.30 A; E=314-393.
PDB; 2W2O; X-ray; 2.62 A; E=314-393.
PDB; 2W2P; X-ray; 2.62 A; E=314-393.
PDB; 2W2Q; X-ray; 2.33 A; E=314-393.
PDB; 3BPS; X-ray; 2.41 A; E=314-393.
PDB; 3GCW; X-ray; 2.70 A; E=314-393.
PDB; 3GCX; X-ray; 2.70 A; E=314-393.
PDB; 3M0C; X-ray; 7.01 A; C=4-788.
PDB; 3P5B; X-ray; 3.30 A; L=316-715.
PDB; 3P5C; X-ray; 4.20 A; L=276-715.
PDB; 3SO6; X-ray; 1.37 A; Q=819-832.
PDB; 4NE9; X-ray; 2.60 A; D=314-339.
PDBsum; 1AJJ; -.
PDBsum; 1D2J; -.
PDBsum; 1F5Y; -.
PDBsum; 1F8Z; -.
PDBsum; 1HJ7; -.
PDBsum; 1HZ8; -.
PDBsum; 1I0U; -.
PDBsum; 1IJQ; -.
PDBsum; 1LDL; -.
PDBsum; 1LDR; -.
PDBsum; 1LRX; -.
PDBsum; 1N7D; -.
PDBsum; 1XFE; -.
PDBsum; 2FCW; -.
PDBsum; 2KRI; -.
PDBsum; 2LGP; -.
PDBsum; 2M7P; -.
PDBsum; 2MG9; -.
PDBsum; 2W2M; -.
PDBsum; 2W2N; -.
PDBsum; 2W2O; -.
PDBsum; 2W2P; -.
PDBsum; 2W2Q; -.
PDBsum; 3BPS; -.
PDBsum; 3GCW; -.
PDBsum; 3GCX; -.
PDBsum; 3M0C; -.
PDBsum; 3P5B; -.
PDBsum; 3P5C; -.
PDBsum; 3SO6; -.
PDBsum; 4NE9; -.
ProteinModelPortal; P01130; -.
SMR; P01130; -.
BioGrid; 110141; 42.
DIP; DIP-29695N; -.
ELM; P01130; -.
IntAct; P01130; 16.
MINT; MINT-3003796; -.
STRING; 9606.ENSP00000454071; -.
BindingDB; P01130; -.
ChEMBL; CHEMBL3311; -.
DrugBank; DB00707; Porfimer.
iPTMnet; P01130; -.
PhosphoSitePlus; P01130; -.
UniCarbKB; P01130; -.
BioMuta; LDLR; -.
DMDM; 126073; -.
EPD; P01130; -.
MaxQB; P01130; -.
PaxDb; P01130; -.
PeptideAtlas; P01130; -.
PRIDE; P01130; -.
DNASU; 3949; -.
Ensembl; ENST00000455727; ENSP00000397829; ENSG00000130164. [P01130-3]
Ensembl; ENST00000535915; ENSP00000440520; ENSG00000130164. [P01130-4]
Ensembl; ENST00000545707; ENSP00000437639; ENSG00000130164. [P01130-2]
Ensembl; ENST00000558013; ENSP00000453346; ENSG00000130164. [P01130-5]
Ensembl; ENST00000558518; ENSP00000454071; ENSG00000130164. [P01130-1]
GeneID; 3949; -.
KEGG; hsa:3949; -.
UCSC; uc002mqk.5; human. [P01130-1]
CTD; 3949; -.
DisGeNET; 3949; -.
EuPathDB; HostDB:ENSG00000130164.11; -.
GeneCards; LDLR; -.
GeneReviews; LDLR; -.
HGNC; HGNC:6547; LDLR.
HPA; HPA009647; -.
HPA; HPA013159; -.
MalaCards; LDLR; -.
MIM; 143890; phenotype.
MIM; 606945; gene.
neXtProt; NX_P01130; -.
OpenTargets; ENSG00000130164; -.
Orphanet; 406; Heterozygous familial hypercholesterolemia.
Orphanet; 391665; Homozygous familial hypercholesterolemia.
PharmGKB; PA227; -.
eggNOG; ENOG410IPSW; Eukaryota.
eggNOG; ENOG410Z5FJ; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000115656; -.
HOVERGEN; HBG006250; -.
InParanoid; P01130; -.
KO; K12473; -.
PhylomeDB; P01130; -.
TreeFam; TF351700; -.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8964026; Chylomicron clearance.
Reactome; R-HSA-8964038; LDL clearance.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; P01130; -.
ChiTaRS; LDLR; human.
EvolutionaryTrace; P01130; -.
GeneWiki; LDL_receptor; -.
GenomeRNAi; 3949; -.
PRO; PR:P01130; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130164; -.
CleanEx; HS_LDLR; -.
ExpressionAtlas; P01130; baseline and differential.
Genevisible; P01130; HS.
GO; GO:0045177; C:apical part of cell; ISS:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; ISS:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005905; C:clathrin-coated pit; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; ISS:ARUK-UCL.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:1990666; C:PCSK9-LDLR complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0036477; C:somatodendritic compartment; IEA:Ensembl.
GO; GO:0097443; C:sorting endosome; IEA:Ensembl.
GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0032050; F:clathrin heavy chain binding; TAS:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030169; F:low-density lipoprotein particle binding; IMP:BHF-UCL.
GO; GO:0005041; F:low-density lipoprotein receptor activity; IDA:BHF-UCL.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:BHF-UCL.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IMP:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0070508; P:cholesterol import; IMP:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0030301; P:cholesterol transport; IMP:HGNC.
GO; GO:0034382; P:chylomicron remnant clearance; TAS:Reactome.
GO; GO:0006897; P:endocytosis; TAS:ProtInc.
GO; GO:0030299; P:intestinal cholesterol absorption; IMP:HGNC.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
GO; GO:0007616; P:long-term memory; IGI:ARUK-UCL.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISS:ARUK-UCL.
GO; GO:0061889; P:negative regulation of astrocyte activation; ISS:ARUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1903979; P:negative regulation of microglial cell activation; ISS:ARUK-UCL.
GO; GO:0051248; P:negative regulation of protein metabolic process; ISS:ARUK-UCL.
GO; GO:0015914; P:phospholipid transport; ISS:BHF-UCL.
GO; GO:0034381; P:plasma lipoprotein particle clearance; TAS:ARUK-UCL.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:0045807; P:positive regulation of endocytosis; ISS:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0010986; P:positive regulation of lipoprotein particle clearance; ISS:ARUK-UCL.
GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; ISS:ARUK-UCL.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IMP:BHF-UCL.
GO; GO:2000188; P:regulation of cholesterol homeostasis; IEA:Ensembl.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; ISS:BHF-UCL.
GO; GO:0051246; P:regulation of protein metabolic process; IGI:ARUK-UCL.
GO; GO:0061771; P:response to caloric restriction; IGI:ARUK-UCL.
CDD; cd00112; LDLa; 7.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 7.
Pfam; PF00058; Ldl_recept_b; 5.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 3.
SMART; SM00179; EGF_CA; 2.
SMART; SM00192; LDLa; 7.
SMART; SM00135; LY; 5.
SUPFAM; SSF57184; SSF57184; 2.
SUPFAM; SSF57424; SSF57424; 7.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01209; LDLRA_1; 7.
PROSITE; PS50068; LDLRA_2; 7.
PROSITE; PS51120; LDLRB; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane;
Cholesterol metabolism; Coated pit; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
EGF-like domain; Endocytosis; Endosome; Glycoprotein; Golgi apparatus;
Host cell receptor for virus entry; Host-virus interaction; LDL;
Lipid metabolism; Lipid transport; Lysosome; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Steroid metabolism; Sterol metabolism; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
SIGNAL 1 21 {ECO:0000250|UniProtKB:P01131}.
CHAIN 22 860 Low-density lipoprotein receptor.
/FTId=PRO_0000017312.
TOPO_DOM 22 788 Extracellular.
{ECO:0000250|UniProtKB:P01131}.
TRANSMEM 789 810 Helical. {ECO:0000255}.
TOPO_DOM 811 860 Cytoplasmic.
{ECO:0000269|PubMed:22509010}.
DOMAIN 25 65 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 66 106 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 107 145 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 146 186 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 195 233 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 234 272 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 274 313 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 314 353 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 354 393 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 397 438 LDL-receptor class B 1.
REPEAT 439 485 LDL-receptor class B 2.
REPEAT 486 528 LDL-receptor class B 3.
REPEAT 529 572 LDL-receptor class B 4.
REPEAT 573 615 LDL-receptor class B 5.
REPEAT 616 658 LDL-receptor class B 6.
DOMAIN 663 712 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 721 768 Clustered O-linked oligosaccharides.
REGION 811 860 Required for MYLIP-triggered down-
regulation of LDLR.
{ECO:0000269|PubMed:19520913}.
MOTIF 823 828 NPXY motif.
{ECO:0000269|PubMed:22509010}.
MOD_RES 724 724 Phosphothreonine.
{ECO:0000250|UniProtKB:P35952}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19520913}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19520913}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
DISULFID 27 39
DISULFID 34 52
DISULFID 46 63
DISULFID 68 82
DISULFID 75 95
DISULFID 89 104
DISULFID 109 121 {ECO:0000250}.
DISULFID 116 134
DISULFID 128 143
DISULFID 148 160
DISULFID 155 173
DISULFID 167 184
DISULFID 197 209
DISULFID 204 222
DISULFID 216 231
DISULFID 236 248
DISULFID 243 261
DISULFID 255 270
DISULFID 276 289
DISULFID 284 302
DISULFID 296 313
DISULFID 318 329
DISULFID 325 338
DISULFID 340 352
DISULFID 358 368
DISULFID 364 377
DISULFID 379 392
DISULFID 667 681
DISULFID 677 696
DISULFID 698 711
VAR_SEQ 35 155 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047413.
VAR_SEQ 64 105 LSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGC
P -> S (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043595.
VAR_SEQ 105 272 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055014.
VAR_SEQ 106 232 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043053.
VAR_SEQ 273 273 V -> L (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055015.
VAR_SEQ 663 713 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043054.
VAR_SEQ 850 851 Missing (in isoform 5).
{ECO:0000303|Ref.7}.
/FTId=VSP_045525.
VARIANT 2 2 G -> R (in dbSNP:rs5931).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_011862.
VARIANT 27 27 C -> W (in FH; San Francisco;
dbSNP:rs2228671).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005304.
VARIANT 46 46 C -> S (in FH; Japanese patient;
dbSNP:rs121908041).
{ECO:0000269|PubMed:11298688}.
/FTId=VAR_013949.
VARIANT 47 48 Missing (in FH; Cape Town-1; retards
receptor transport from the endoplasmic
reticulum to the cell surface).
{ECO:0000269|PubMed:10882754,
ECO:0000269|PubMed:3263645}.
/FTId=VAR_005305.
VARIANT 50 50 A -> S (in FH; German patient;
dbSNP:rs137853960).
{ECO:0000269|PubMed:10090484}.
/FTId=VAR_007979.
VARIANT 50 50 A -> T (in FH; unknown pathological
significance; dbSNP:rs137853960).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_072827.
VARIANT 52 52 C -> Y (in Paris-4; dbSNP:rs879254418).
/FTId=VAR_005306.
VARIANT 56 56 S -> P (in FH; dbSNP:rs878854026).
{ECO:0000269|PubMed:9104431}.
/FTId=VAR_007980.
VARIANT 78 78 R -> C (in FH; dbSNP:rs370860696).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005307.
VARIANT 87 87 W -> G (in FH; French Canadian-4;
dbSNP:rs121908025).
{ECO:0000269|PubMed:10532689,
ECO:0000269|PubMed:2318961,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005308.
VARIANT 89 89 C -> Y (in FH; dbSNP:rs875989894).
{ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005309.
VARIANT 90 90 D -> G (in FH; London-4;
dbSNP:rs771019366).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005310.
VARIANT 90 90 D -> N (in FH; dbSNP:rs749038326).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005311.
VARIANT 90 90 D -> Y (in FH; Durban-1;
dbSNP:rs749038326).
{ECO:0000269|PubMed:8347689}.
/FTId=VAR_005312.
VARIANT 92 92 Q -> E (in FH; Spanish patient;
dbSNP:rs774467219).
{ECO:0000269|PubMed:10206683}.
/FTId=VAR_005313.
VARIANT 95 95 C -> G (in FH; Spanish patient;
dbSNP:rs879254456).
{ECO:0000269|PubMed:10206683}.
/FTId=VAR_005314.
VARIANT 101 101 E -> K (in FH; Lancashire; 6% of American
English; dbSNP:rs144172724).
{ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005315.
VARIANT 105 105 P -> S (in dbSNP:rs13306510).
/FTId=VAR_059375.
VARIANT 109 109 C -> R (in Munster-1; dbSNP:rs140807148).
/FTId=VAR_005316.
VARIANT 116 116 C -> R (in FH; does not affect receptor
expression at the cell surface; results
in reduced LDL binding; results in
reduced LDL uptake and internalization;
dbSNP:rs879254482).
{ECO:0000269|PubMed:10206683,
ECO:0000269|PubMed:25545329}.
/FTId=VAR_005317.
VARIANT 134 134 C -> F (in FH; dbSNP:rs879254514).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062371.
VARIANT 134 134 C -> W (in FH; dbSNP:rs879254515).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062372.
VARIANT 139 139 D -> H (found in a patient with
hypercholesterolemia; dbSNP:rs879254517).
{ECO:0000269|PubMed:21418584}.
/FTId=VAR_065780.
VARIANT 140 140 E -> K (in FH; Philippines/Durban-2/
Japan; dbSNP:rs748944640).
{ECO:0000269|PubMed:10532689,
ECO:0000269|PubMed:7583548,
ECO:0000269|PubMed:8347689}.
/FTId=VAR_005318.
VARIANT 143 143 C -> R (in FH; dbSNP:rs875989901).
{ECO:0000269|PubMed:11462246}.
/FTId=VAR_072828.
VARIANT 148 148 C -> Y (in FH; dbSNP:rs879254526).
{ECO:0000269|PubMed:11462246}.
/FTId=VAR_072829.
VARIANT 155 155 C -> G (in Germany; dbSNP:rs879254535).
/FTId=VAR_005319.
VARIANT 155 155 C -> Y (in FH; results in defective LDL
binding; does not affect receptor
expression at the cell surface;
dbSNP:rs879254536).
{ECO:0000269|PubMed:19318025,
ECO:0000269|PubMed:25378237}.
/FTId=VAR_072830.
VARIANT 160 160 C -> Y (in FH; unknown pathological
significance; dbSNP:rs879254541).
{ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005320.
VARIANT 168 168 D -> A (in FH; unknown pathological
significance).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072831.
VARIANT 168 168 D -> H (in FH; Sephardic/Safed; 10% of
the Sephardic Jews; dbSNP:rs200727689).
{ECO:0000269|PubMed:8462973}.
/FTId=VAR_005321.
VARIANT 168 168 D -> N (in FH; does not affect receptor
expression at the cell surface; results
in reduced LDL binding; results in
reduced LDL uptake and internalization;
dbSNP:rs200727689).
{ECO:0000269|PubMed:25545329,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005322.
VARIANT 168 168 D -> Y (in FH; dbSNP:rs200727689).
{ECO:0000269|PubMed:8740918}.
/FTId=VAR_005323.
VARIANT 172 172 D -> H (may contribute to familial
hypercholesterolemia; dbSNP:rs879254554).
{ECO:0000269|PubMed:10882754}.
/FTId=VAR_013950.
VARIANT 172 172 D -> N (in FH; does not affect receptor
expression at the cell surface; results
in reduced LDL binding; results in
reduced LDL uptake and internalization;
dbSNP:rs879254554).
{ECO:0000269|PubMed:10532689,
ECO:0000269|PubMed:25545329}.
/FTId=VAR_072832.
VARIANT 173 173 C -> R (in Greece-1; dbSNP:rs879254558).
/FTId=VAR_005324.
VARIANT 173 173 C -> W (in FH; dbSNP:rs769318035).
{ECO:0000269|PubMed:9452094}.
/FTId=VAR_005325.
VARIANT 175 175 D -> N (in FH; Afrikaner-3; 5-10% of
Afrikaners; dbSNP:rs121908033).
{ECO:0000269|PubMed:2569482}.
/FTId=VAR_005326.
VARIANT 175 175 D -> Y (in FH; dbSNP:rs121908033).
{ECO:0000269|PubMed:9104431}.
/FTId=VAR_007981.
VARIANT 177 177 S -> L (in FH; Puerto Rico;
dbSNP:rs121908026).
{ECO:0000269|PubMed:10206683,
ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:9259195,
ECO:0000269|PubMed:9654205}.
/FTId=VAR_005327.
VARIANT 184 184 C -> W (in FH; dbSNP:rs879254571).
{ECO:0000269|PubMed:11462246}.
/FTId=VAR_072833.
VARIANT 184 184 C -> Y (in FH; Glasco;
dbSNP:rs121908039).
{ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:9678702}.
/FTId=VAR_013951.
VARIANT 197 197 C -> F (in Shreveport;
dbSNP:rs376459828).
/FTId=VAR_005328.
VARIANT 197 197 C -> R (in FH; British patient;
dbSNP:rs730882085).
{ECO:0000269|PubMed:9026534}.
/FTId=VAR_005330.
VARIANT 197 197 C -> Y (in El Salvador-1;
dbSNP:rs376459828).
/FTId=VAR_005329.
VARIANT 201 201 E -> K (found in a patient with
hypercholesterolemia; dbSNP:rs879254589).
{ECO:0000269|PubMed:21418584}.
/FTId=VAR_065781.
VARIANT 211 211 H -> L (in FH; unknown pathological
significance; dbSNP:rs879254603).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_072834.
VARIANT 218 218 Missing (in FH; Piscataway/Lithuania).
{ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:1867200,
ECO:0000269|PubMed:9654205}.
/FTId=VAR_005331.
VARIANT 221 221 D -> G (in FH; Padova;
dbSNP:rs373822756).
{ECO:0000269|PubMed:10206683,
ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:17347910,
ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:7649546,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005332.
VARIANT 221 221 D -> N (in FH; German patient;
dbSNP:rs875989906).
{ECO:0000269|PubMed:10090484,
ECO:0000269|PubMed:17142622}.
/FTId=VAR_007982.
VARIANT 221 221 D -> Y (in FH; Cologne patient;
dbSNP:rs875989906).
{ECO:0000269|PubMed:10206683,
ECO:0000269|PubMed:7649546}.
/FTId=VAR_005333.
VARIANT 222 222 C -> Y (in FH; dbSNP:rs730882086).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062373.
VARIANT 224 224 D -> G (in Italy-2; dbSNP:rs879254630).
/FTId=VAR_005335.
VARIANT 224 224 D -> N (in Portugal; dbSNP:rs387906303).
/FTId=VAR_005334.
VARIANT 224 224 D -> V (in FH; Cologne patient;
dbSNP:rs879254630).
{ECO:0000269|PubMed:7649546}.
/FTId=VAR_005336.
VARIANT 226 226 S -> P (in Miami-1; dbSNP:rs879254635).
/FTId=VAR_005337.
VARIANT 227 227 D -> E (in FH; Afrikaner-1/Maine; 65-70%
of Afrikaner Americans;
dbSNP:rs121908028).
{ECO:0000269|PubMed:2569482,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005338.
VARIANT 228 228 E -> CK (in Chieti-3).
{ECO:0000269|PubMed:10660340}.
/FTId=VAR_005339.
VARIANT 228 228 E -> K (in FH; French Canadian-3/Mexico;
2% of French Canadians;
dbSNP:rs121908029).
{ECO:0000269|PubMed:2318961,
ECO:0000269|PubMed:24529145}.
/FTId=VAR_005341.
VARIANT 228 228 E -> Q (in FH; Tulsa-2; unknown
pathological significance;
dbSNP:rs121908029).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_005340.
VARIANT 231 231 C -> G (in FH; Norwegian patient;
dbSNP:rs746091400).
{ECO:0000269|PubMed:8664907}.
/FTId=VAR_005342.
VARIANT 240 240 E -> K (in Charlotte; dbSNP:rs768563000).
/FTId=VAR_005343.
VARIANT 243 243 C -> R (in FH; unknown pathological
significance; dbSNP:rs879254659).
{ECO:0000269|PubMed:10532689}.
/FTId=VAR_072835.
VARIANT 248 248 C -> F (in Bretagne-1;
dbSNP:rs879254663).
/FTId=VAR_005344.
VARIANT 248 248 C -> Y (in FH; British patient;
dbSNP:rs879254663).
{ECO:0000269|PubMed:9026534}.
/FTId=VAR_005345.
VARIANT 253 253 R -> W (may contribute to familial
hypercholesterolemia; dbSNP:rs150673992).
{ECO:0000269|PubMed:10882754}.
/FTId=VAR_013952.
VARIANT 254 254 Q -> P (in FH; dbSNP:rs879254667).
{ECO:0000269|PubMed:10978268,
ECO:0000269|PubMed:19319977}.
/FTId=VAR_062374.
VARIANT 255 255 C -> S (found in a patient with
hypercholesterolemia; dbSNP:rs879254668).
{ECO:0000269|PubMed:21418584}.
/FTId=VAR_065782.
VARIANT 256 256 D -> G (in Nevers; dbSNP:rs879254670).
/FTId=VAR_005346.
VARIANT 257 257 R -> W (polymorphism; does not affect
receptor expression at the cell surface;
does not affect LDL binding; does not
affect LDL uptake and internalization;
dbSNP:rs200990725).
{ECO:0000269|PubMed:11462246,
ECO:0000269|PubMed:25545329}.
/FTId=VAR_072836.
VARIANT 261 261 C -> F (in FH; rare mutation; strongly
reduced receptor activity;
dbSNP:rs121908040).
{ECO:0000269|PubMed:10422803}.
/FTId=VAR_013953.
VARIANT 266 266 D -> E (in FH; Cincinnati-1; unknown
pathological significance;
dbSNP:rs139043155).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_005347.
VARIANT 270 270 C -> Y (in Miami-2; dbSNP:rs879254683).
/FTId=VAR_005348.
VARIANT 276 276 C -> R (in FH; dbSNP:rs879254692).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062375.
VARIANT 276 276 C -> W (in FH; unknown pathological
significance).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072837.
VARIANT 276 276 C -> Y (in FH; Syrian patient;
dbSNP:rs730882089). {ECO:0000269|Ref.71}.
/FTId=VAR_005349.
VARIANT 277 277 E -> K (in FH; patients from Sweden and
La Havana; unknown pathological
significance; dbSNP:rs148698650).
{ECO:0000269|PubMed:10206683,
ECO:0000269|PubMed:17347910,
ECO:0000269|PubMed:7635461,
ECO:0000269|PubMed:7649549}.
/FTId=VAR_005350.
VARIANT 285 285 H -> Y (in FH; unknown pathological
significance; dbSNP:rs730882091).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072838.
VARIANT 286 286 S -> R (in FH; Greece-2; unknown
pathological significance;
dbSNP:rs140241383).
{ECO:0000269|PubMed:17347910,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005351.
VARIANT 288 288 E -> K (in FH; German patient;
dbSNP:rs368657165).
{ECO:0000269|PubMed:10090484}.
/FTId=VAR_007983.
VARIANT 300 300 R -> G (in FH; does not affect receptor
expression at the cell surface; results
in reduced LDL binding; results in
reduced LDL uptake and internalization;
dbSNP:rs767618089).
{ECO:0000269|PubMed:19318025,
ECO:0000269|PubMed:25545329}.
/FTId=VAR_072839.
VARIANT 301 301 D -> A (in FH; Greek patient;
dbSNP:rs879254714).
{ECO:0000269|PubMed:9026534}.
/FTId=VAR_005352.
VARIANT 301 301 D -> G (in FH; does not affect receptor
expression at the cell surface; results
in reduced LDL binding; results in
reduced LDL uptake and internalization;
dbSNP:rs879254714).
{ECO:0000269|PubMed:19318025,
ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:25545329}.
/FTId=VAR_072840.
VARIANT 302 302 C -> W (in FH; Iraki patient;
dbSNP:rs879254716).
{ECO:0000269|PubMed:9026534}.
/FTId=VAR_005354.
VARIANT 302 302 C -> Y (in FH; Spanish patient;
dbSNP:rs879254715).
{ECO:0000269|PubMed:10206683}.
/FTId=VAR_005353.
VARIANT 304 304 D -> E (in Baltimore-1;
dbSNP:rs875989909).
/FTId=VAR_005356.
VARIANT 304 304 D -> N (in Denver-2; dbSNP:rs121908030).
{ECO:0000269|PubMed:21418584}.
/FTId=VAR_005355.
VARIANT 306 306 S -> L (in FH; Amsterdam; unknown
pathological significance;
dbSNP:rs11547917).
{ECO:0000269|PubMed:10532689}.
/FTId=VAR_005357.
VARIANT 313 313 C -> Y (in FH; dbSNP:rs875989911 and
dbSNP:rs875989910).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005358.
VARIANT 314 314 G -> R (in FH; unknown pathological
significance; dbSNP:rs72658858).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_072841.
VARIANT 318 318 C -> F (in FH; Trieste;
dbSNP:rs879254739).
{ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:8168830}.
/FTId=VAR_005360.
VARIANT 318 318 C -> R (in FH; dbSNP:rs879254738).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062376.
VARIANT 318 318 C -> Y (in Mexico-1; leads to a defect in
the intracellular transport of the
receptor; dbSNP:rs879254739).
/FTId=VAR_005359.
VARIANT 326 326 S -> C (in FH; unknown pathological
significance; dbSNP:rs879254747).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072842.
VARIANT 327 327 H -> Y (in FH; dbSNP:rs747507019).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005361.
VARIANT 329 329 C -> F (in FH).
{ECO:0000269|PubMed:22160468}.
/FTId=VAR_067196.
VARIANT 329 329 C -> Y (in FH; Chinese patient;
dbSNP:rs761954844).
{ECO:0000269|PubMed:9452118}.
/FTId=VAR_005362.
VARIANT 335 335 G -> S (in Paris-6; dbSNP:rs544453230).
/FTId=VAR_005363.
VARIANT 338 338 C -> S (in FH; Japanese patients;
dbSNP:rs879254753).
{ECO:0000269|PubMed:10447263,
ECO:0000269|PubMed:7583548}.
/FTId=VAR_005364.
VARIANT 342 342 D -> E (in New York-1).
/FTId=VAR_005365.
VARIANT 342 342 D -> N (in FH; unknown pathological
significance; dbSNP:rs139361635).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005366.
VARIANT 343 343 G -> S (in FH; Picardie; unknown
pathological significance;
dbSNP:rs730882096).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_005367.
VARIANT 350 350 R -> P (in FH; dbSNP:rs875989914).
{ECO:0000269|PubMed:9026534,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005368.
VARIANT 352 352 C -> R (in FH; unknown pathological
significance; dbSNP:rs879254769).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_072843.
VARIANT 352 352 C -> Y (in Mexico-2; dbSNP:rs193922566).
/FTId=VAR_005369.
VARIANT 354 354 D -> G (in Munster-2; dbSNP:rs755449669).
/FTId=VAR_005370.
VARIANT 354 354 D -> V (in Oklahoma).
/FTId=VAR_005371.
VARIANT 356 356 D -> Y (in FH).
{ECO:0000269|PubMed:19319977,
ECO:0000269|PubMed:9104431}.
/FTId=VAR_007984.
VARIANT 357 357 E -> K (in Paris-7; dbSNP:rs879254781).
/FTId=VAR_005372.
VARIANT 358 358 C -> Y (in FH; dbSNP:rs875989915).
{ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:19319977}.
/FTId=VAR_062377.
VARIANT 364 364 C -> R (in Mexico-3; dbSNP:rs879254787).
/FTId=VAR_005373.
VARIANT 366 366 Q -> R (in FH; dbSNP:rs746982741).
{ECO:0000269|PubMed:8740918}.
/FTId=VAR_007985.
VARIANT 368 368 C -> R (in FH; French Canadian patient).
{ECO:0000269|PubMed:9452094}.
/FTId=VAR_005374.
VARIANT 368 368 C -> Y (in FH; unknown pathological
significance; dbSNP:rs768430352).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072844.
VARIANT 370 370 N -> T (in FH; dbSNP:rs879254792).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062378.
VARIANT 373 373 G -> D (in FH; unknown pathological
significance; dbSNP:rs879254797).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072845.
VARIANT 379 379 C -> R (in Naples-1; dbSNP:rs879254803).
/FTId=VAR_005375.
VARIANT 379 379 C -> Y (in FH; dbSNP:rs879254804).
{ECO:0000269|PubMed:9852677}.
/FTId=VAR_007986.
VARIANT 391 391 A -> T (in dbSNP:rs11669576).
/FTId=VAR_024519.
VARIANT 399 399 A -> D (in FH; dbSNP:rs875989918).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005376.
VARIANT 401 401 L -> H (in Pori; dbSNP:rs121908038).
{ECO:0000269|PubMed:7573037}.
/FTId=VAR_005377.
VARIANT 401 401 L -> V (in FH; dbSNP:rs146200173).
{ECO:0000269|PubMed:9104431}.
/FTId=VAR_007987.
VARIANT 403 403 F -> L (in FH; Japanese patient;
dbSNP:rs879254831).
{ECO:0000269|PubMed:10447263}.
/FTId=VAR_008995.
VARIANT 404 404 T -> P (in FH; unknown pathological
significance; dbSNP:rs879254834).
{ECO:0000269|PubMed:10532689}.
/FTId=VAR_072846.
VARIANT 406 406 R -> Q (may contribute to familial
hypercholesterolemia; dbSNP:rs552422789).
{ECO:0000269|PubMed:10882754}.
/FTId=VAR_013954.
VARIANT 406 406 R -> W (in FH; unknown pathological
significance; dbSNP:rs121908043).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072847.
VARIANT 408 408 E -> K (in FH; Algeria-1; unknown
pathological significance;
dbSNP:rs137943601).
{ECO:0000269|PubMed:10882754,
ECO:0000269|PubMed:17347910}.
/FTId=VAR_005378.
VARIANT 414 414 L -> R (in FH; Chinese patient;
dbSNP:rs748554592).
{ECO:0000269|PubMed:9452118}.
/FTId=VAR_005379.
VARIANT 415 415 D -> G (in FH; dbSNP:rs879254845).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062379.
VARIANT 416 416 R -> Q (in FH; German patient;
dbSNP:rs773658037).
{ECO:0000269|PubMed:9452095}.
/FTId=VAR_005380.
VARIANT 416 416 R -> W (in FH; results in reduced
receptor expression at the cell surface
due to defective receptor recycling;
dbSNP:rs570942190).
{ECO:0000269|PubMed:19318025,
ECO:0000269|PubMed:25378237,
ECO:0000269|PubMed:9104431,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005381.
VARIANT 423 423 I -> T (in FH; Swedish patient;
dbSNP:rs879254849).
{ECO:0000269|PubMed:7635461}.
/FTId=VAR_005382.
VARIANT 429 429 V -> M (in FH; Afrikaner-2; 20-30% of
Afrikaners and 2% of FH Dutch;
dbSNP:rs28942078).
{ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:2569482,
ECO:0000269|PubMed:7649549,
ECO:0000269|PubMed:9452095,
ECO:0000269|PubMed:9452118}.
/FTId=VAR_005383.
VARIANT 431 431 A -> T (in FH; Algeria-2; unknown
pathological significance;
dbSNP:rs28942079).
{ECO:0000269|PubMed:10447263,
ECO:0000269|PubMed:17347910}.
/FTId=VAR_005384.
VARIANT 432 432 L -> V (in FH; German patient;
dbSNP:rs730882100).
{ECO:0000269|PubMed:10090484}.
/FTId=VAR_007988.
VARIANT 433 433 D -> H (in FH; Osaka-3;
dbSNP:rs121908036).
{ECO:0000269|PubMed:1446662}.
/FTId=VAR_005385.
VARIANT 434 434 T -> K (in FH; Algeria-3; unknown
pathological significance).
{ECO:0000269|PubMed:10206683}.
/FTId=VAR_005386.
VARIANT 441 441 I -> M (in Rouen).
/FTId=VAR_005388.
VARIANT 441 441 I -> N (in Russia-1; dbSNP:rs879254862).
/FTId=VAR_005387.
VARIANT 442 442 Y -> H (in FH; unknown pathological
significance; dbSNP:rs879254863).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_072848.
VARIANT 443 443 W -> C (in North Platt;
dbSNP:rs879254867).
/FTId=VAR_005389.
VARIANT 451 451 I -> T (in FH; dbSNP:rs879254874).
{ECO:0000269|PubMed:10980548,
ECO:0000269|PubMed:19319977}.
/FTId=VAR_062380.
VARIANT 454 454 T -> N (in FH; results in reduced
receptor expression at the cell surface
due to defective receptor recycling;
dbSNP:rs879254879).
{ECO:0000269|PubMed:19318025,
ECO:0000269|PubMed:25378237}.
/FTId=VAR_072849.
VARIANT 468 468 V -> I (in dbSNP:rs5932).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_011863.
VARIANT 471 471 R -> G (found in a patient with
hypercholesterolemia; dbSNP:rs879254891).
{ECO:0000269|PubMed:21418584}.
/FTId=VAR_065783.
VARIANT 478 478 G -> R (in New York-2;
dbSNP:rs144614838).
/FTId=VAR_005390.
VARIANT 479 479 L -> P (in FH; dbSNP:rs879254900).
{ECO:0000269|PubMed:17142622}.
/FTId=VAR_062381.
VARIANT 482 482 D -> H (in FH).
{ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005391.
VARIANT 483 483 W -> R (in FH; dbSNP:rs879254905).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005392.
VARIANT 485 485 H -> R (in Milan; dbSNP:rs879254906).
/FTId=VAR_005394.
VARIANT 487 487 Missing (in FH; Norwegian patient).
{ECO:0000269|PubMed:7635482}.
/FTId=VAR_005393.
VARIANT 492 492 D -> N (in FH; unknown pathological
significance; dbSNP:rs373646964).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072850.
VARIANT 523 523 V -> M (in FH; Kuwait; dbSNP:rs28942080).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_005395.
VARIANT 526 526 P -> S (in FH; Cincinnati-3; unknown
pathological significance;
dbSNP:rs730882106).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005396.
VARIANT 546 546 G -> D (in Saint Omer; retention in the
ER; dbSNP:rs28942081).
{ECO:0000269|PubMed:19520913}.
/FTId=VAR_005397.
VARIANT 549 549 G -> D (in FH; Genoa; dbSNP:rs28941776).
{ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005398.
VARIANT 564 564 N -> H (in FH; dbSNP:rs397509365).
{ECO:0000269|PubMed:10090484,
ECO:0000269|PubMed:10532689,
ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:7550239,
ECO:0000269|PubMed:9143924}.
/FTId=VAR_005399.
VARIANT 564 564 N -> S (in FH; Sicily;
dbSNP:rs758194385).
{ECO:0000269|PubMed:9654205}.
/FTId=VAR_005400.
VARIANT 565 565 G -> V (in Naples-2; dbSNP:rs28942082).
/FTId=VAR_005401.
VARIANT 568 568 L -> V (in FH; Japanese patient).
{ECO:0000269|PubMed:10447263}.
/FTId=VAR_008996.
VARIANT 574 574 R -> C (in FH; dbSNP:rs185098634).
{ECO:0000269|PubMed:11462246}.
/FTId=VAR_072851.
VARIANT 574 574 R -> H (in FH; unknown pathological
significance; dbSNP:rs777188764).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072852.
VARIANT 577 577 W -> G (in FH; results in loss of
receptor expression at the cell surface;
dbSNP:rs879255000).
{ECO:0000269|PubMed:17347910,
ECO:0000269|PubMed:25378237}.
/FTId=VAR_072853.
VARIANT 577 577 W -> S (in FH; unknown pathological
significance; dbSNP:rs138947766).
{ECO:0000269|PubMed:10532689}.
/FTId=VAR_072854.
VARIANT 579 579 D -> N (in FH; Cincinnati-4; less than 2%
receptor activity).
{ECO:0000269|PubMed:10532689,
ECO:0000269|PubMed:7635461}.
/FTId=VAR_005402.
VARIANT 579 579 D -> Y (in FH; dbSNP:rs875989929).
{ECO:0000269|PubMed:10978268}.
/FTId=VAR_062382.
VARIANT 585 585 I -> T (in FH; unknown pathological
significance; dbSNP:rs879255012).
{ECO:0000269|PubMed:17347910}.
/FTId=VAR_072855.
VARIANT 592 592 G -> E (in FH; Sicily;
dbSNP:rs137929307).
{ECO:0000269|PubMed:9654205}.
/FTId=VAR_005403.
VARIANT 595 595 R -> W (in FH; unknown pathological
significance; dbSNP:rs373371572).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072856.
VARIANT 599 599 L -> S (in London-5; dbSNP:rs879255025).
/FTId=VAR_005404.
VARIANT 601 601 D -> H (in FH; unknown pathological
significance).
{ECO:0000269|PubMed:24529145}.
/FTId=VAR_072857.
VARIANT 608 608 P -> S (in FH; dbSNP:rs879255034).
{ECO:0000269|PubMed:9852677}.
/FTId=VAR_007989.
VARIANT 633 633 R -> C (in FH; dbSNP:rs746118995).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005405.
VARIANT 639 639 V -> D (in FH; dbSNP:rs794728584).
{ECO:0000269|PubMed:11462246}.
/FTId=VAR_072858.
VARIANT 649 649 P -> L (in FH; dbSNP:rs879255081).
{ECO:0000269|PubMed:9259195}.
/FTId=VAR_005406.
VARIANT 667 667 C -> Y (in FH; French Canadian-2; 5% of
French Canadians; dbSNP:rs28942083).
{ECO:0000269|PubMed:10206683,
ECO:0000269|PubMed:2318961}.
/FTId=VAR_005407.
VARIANT 677 677 C -> R (in FH; New York-3;
dbSNP:rs775092314).
{ECO:0000269|PubMed:17142622}.
/FTId=VAR_005408.
VARIANT 682 682 L -> P (in Issoire; dbSNP:rs879255119).
/FTId=VAR_005409.
VARIANT 685 685 P -> L (in FH; Gujerat/Zambia/Belgian/
Dutch/Sweden/Japan; dbSNP:rs28942084).
{ECO:0000269|PubMed:1464748,
ECO:0000269|PubMed:17142622,
ECO:0000269|PubMed:17347910,
ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:2726768,
ECO:0000269|PubMed:7583548,
ECO:0000269|PubMed:9254862}.
/FTId=VAR_005410.
VARIANT 699 699 P -> L (in FH; unknown pathological
significance; dbSNP:rs201573863).
{ECO:0000269|PubMed:10882754,
ECO:0000269|PubMed:24529145}.
/FTId=VAR_013955.
VARIANT 700 700 D -> E (in FH; Spanish patient;
dbSNP:rs759858813).
{ECO:0000269|PubMed:10206683}.
/FTId=VAR_005412.
VARIANT 714 714 E -> K (in FH; Japanese patient;
dbSNP:rs869320652).
{ECO:0000269|PubMed:10447263}.
/FTId=VAR_008997.
VARIANT 726 726 T -> I (in FH; Paris-9; unknown
pathological significance;
dbSNP:rs45508991).
{ECO:0000269|PubMed:10532689,
ECO:0000269|PubMed:9259195}.
/FTId=VAR_005413.
VARIANT 742 742 T -> I (in dbSNP:rs767546791).
{ECO:0000269|PubMed:11462246}.
/FTId=VAR_072859.
VARIANT 792 792 I -> F (in Russia-2).
/FTId=VAR_005414.
VARIANT 797 797 V -> M (in FH; La Havana patient;
dbSNP:rs750518671).
{ECO:0000269|PubMed:24529145,
ECO:0000269|PubMed:7649549}.
/FTId=VAR_005415.
VARIANT 799 801 Missing (in FH; Danish patient).
{ECO:0000269|PubMed:9143924}.
/FTId=VAR_005416.
VARIANT 806 806 V -> D (in FH; unknown pathological
significance; dbSNP:rs879255208).
{ECO:0000269|PubMed:11462246}.
/FTId=VAR_072860.
VARIANT 814 814 R -> Q (in FH; unknown pathological
significance; dbSNP:rs5928).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10882754,
ECO:0000269|PubMed:24529145}.
/FTId=VAR_011864.
VARIANT 820 822 Missing (in FH).
/FTId=VAR_005417.
VARIANT 825 825 N -> K (in FH; does not affect receptor
expression at the cell surface; does not
affect LDL binding; results in impaired
LDL uptake and internalization;
dbSNP:rs374045590).
{ECO:0000269|PubMed:10532689,
ECO:0000269|PubMed:25378237}.
/FTId=VAR_072861.
VARIANT 826 826 P -> S (in FH).
{ECO:0000269|PubMed:19319977}.
/FTId=VAR_062383.
VARIANT 827 827 V -> I (in New York-5;
dbSNP:rs137853964).
/FTId=VAR_005418.
VARIANT 828 828 Y -> C (in FH; J.D.Bari/Syria; 2-fold
decreased affinity for LDLRAP1;
dbSNP:rs28942085).
{ECO:0000269|PubMed:22509010,
ECO:0000269|PubMed:3955657}.
/FTId=VAR_005419.
VARIANT 844 844 G -> D (in Turku; dbSNP:rs121908037).
{ECO:0000269|PubMed:7573037}.
/FTId=VAR_005420.
MUTAGEN 811 811 K->R: No change. No change; when
associated with R-816 and R-830.
Insensitive to MYLIP-triggered
degradation; when associated with R-816;
R-830 and A-839.
{ECO:0000269|PubMed:19520913}.
MUTAGEN 816 816 K->R: No change. No change; when
associated with R-830. No change; when
associated with R-811 and R-830.
Insensitive to MYLIP-triggered
degradation; when associated with R-830
and A-839. Insensitive to MYLIP-triggered
degradation; when associated with R-811;
R-830 and A-839.
{ECO:0000269|PubMed:19520913}.
MUTAGEN 821 821 I->A: 3-fold decreased affinity for
LDLRAP1. {ECO:0000269|PubMed:22509010}.
MUTAGEN 821 821 I->R: 10-fold decreased affinity for
LDLRAP1. {ECO:0000269|PubMed:22509010}.
MUTAGEN 828 828 Y->A: Abolishes interaction with ARRB2.
{ECO:0000269|PubMed:12944399}.
MUTAGEN 829 829 Q->A: Decreased affinity for LDLRAP1.
{ECO:0000269|PubMed:22509010}.
MUTAGEN 830 830 K->R: No change. No change; when
associated with R-816. No change; when
associated with R-811 and R-816.
Insensitive to MYLIP-triggered
degradation; when associated with A-839.
Insensitive to MYLIP-triggered
degradation; when associated with R-816
and A-839. Insensitive to MYLIP-triggered
degradation; when associated with R-811;
R-816 and A-839.
{ECO:0000269|PubMed:19520913}.
MUTAGEN 839 839 C->A: No change. Insensitive to MYLIP-
triggered degradation; when associated
with R-830. Insensitive to MYLIP-
triggered degradation; when associated
with R-816 and R-830. Insensitive to
MYLIP-triggered degradation; when
associated with R-811; R-816 and R-830.
{ECO:0000269|PubMed:19520913}.
MUTAGEN 854 854 S->A: No effect on receptor
internalization.
{ECO:0000269|PubMed:12944399}.
MUTAGEN 854 854 S->D: Enhances interaction with ARRB2 and
receptor internalization.
{ECO:0000269|PubMed:12944399}.
CONFLICT 31 31 E -> D (in Ref. 4; BAG58495).
{ECO:0000305}.
STRAND 29 33 {ECO:0000244|PDB:1F5Y}.
STRAND 35 37 {ECO:0000244|PDB:1F5Y}.
STRAND 39 41 {ECO:0000244|PDB:1LDL}.
TURN 42 46 {ECO:0000244|PDB:1F5Y}.
STRAND 47 49 {ECO:0000244|PDB:1F5Y}.
STRAND 51 55 {ECO:0000244|PDB:1F5Y}.
HELIX 56 58 {ECO:0000244|PDB:1F5Y}.
TURN 60 62 {ECO:0000244|PDB:1LDL}.
TURN 63 67 {ECO:0000244|PDB:1F5Y}.
STRAND 70 72 {ECO:0000244|PDB:1LDR}.
STRAND 75 77 {ECO:0000244|PDB:1LDR}.
STRAND 79 81 {ECO:0000244|PDB:1LDR}.
HELIX 85 87 {ECO:0000244|PDB:1F5Y}.
STRAND 88 90 {ECO:0000244|PDB:1LDR}.
STRAND 95 97 {ECO:0000244|PDB:1F5Y}.
TURN 99 103 {ECO:0000244|PDB:1F5Y}.
STRAND 113 115 {ECO:0000244|PDB:2FCW}.
STRAND 121 123 {ECO:0000244|PDB:2FCW}.
HELIX 124 126 {ECO:0000244|PDB:2FCW}.
STRAND 129 131 {ECO:0000244|PDB:2FCW}.
TURN 138 142 {ECO:0000244|PDB:2FCW}.
HELIX 143 147 {ECO:0000244|PDB:2FCW}.
STRAND 148 151 {ECO:0000244|PDB:2LGP}.
STRAND 152 154 {ECO:0000244|PDB:2FCW}.
TURN 156 158 {ECO:0000244|PDB:2LGP}.
STRAND 160 162 {ECO:0000244|PDB:2FCW}.
HELIX 163 165 {ECO:0000244|PDB:2FCW}.
STRAND 168 170 {ECO:0000244|PDB:2FCW}.
STRAND 173 176 {ECO:0000244|PDB:2LGP}.
HELIX 177 179 {ECO:0000244|PDB:2FCW}.
HELIX 181 183 {ECO:0000244|PDB:2FCW}.
TURN 189 191 {ECO:0000244|PDB:2LGP}.
STRAND 201 204 {ECO:0000244|PDB:2LGP}.
TURN 205 207 {ECO:0000244|PDB:2LGP}.
STRAND 208 211 {ECO:0000244|PDB:2LGP}.
HELIX 212 214 {ECO:0000244|PDB:1AJJ}.
STRAND 217 219 {ECO:0000244|PDB:1AJJ}.
STRAND 222 224 {ECO:0000244|PDB:2LGP}.
HELIX 226 228 {ECO:0000244|PDB:1AJJ}.
STRAND 241 243 {ECO:0000244|PDB:1D2J}.
TURN 244 246 {ECO:0000244|PDB:1D2J}.
STRAND 247 249 {ECO:0000244|PDB:1D2J}.
HELIX 251 253 {ECO:0000244|PDB:1D2J}.
STRAND 254 258 {ECO:0000244|PDB:1D2J}.
STRAND 260 264 {ECO:0000244|PDB:1D2J}.
HELIX 265 267 {ECO:0000244|PDB:1F8Z}.
STRAND 268 270 {ECO:0000244|PDB:1F8Z}.
STRAND 281 283 {ECO:0000244|PDB:1XFE}.
STRAND 289 292 {ECO:0000244|PDB:1XFE}.
TURN 293 296 {ECO:0000244|PDB:1XFE}.
STRAND 306 308 {ECO:0000244|PDB:1XFE}.
TURN 310 312 {ECO:0000244|PDB:1XFE}.
HELIX 317 319 {ECO:0000244|PDB:2W2N}.
HELIX 321 324 {ECO:0000244|PDB:2W2N}.
STRAND 326 330 {ECO:0000244|PDB:2W2N}.
STRAND 333 335 {ECO:0000244|PDB:2W2N}.
STRAND 337 339 {ECO:0000244|PDB:2W2N}.
STRAND 341 343 {ECO:0000244|PDB:1HZ8}.
STRAND 345 347 {ECO:0000244|PDB:2W2N}.
TURN 348 350 {ECO:0000244|PDB:2W2N}.
STRAND 351 353 {ECO:0000244|PDB:2W2N}.
HELIX 357 359 {ECO:0000244|PDB:1HJ7}.
STRAND 363 369 {ECO:0000244|PDB:1HJ7}.
STRAND 372 374 {ECO:0000244|PDB:3P5B}.
STRAND 376 378 {ECO:0000244|PDB:1HJ7}.
STRAND 381 385 {ECO:0000244|PDB:1HZ8}.
TURN 387 389 {ECO:0000244|PDB:3P5B}.
STRAND 392 394 {ECO:0000244|PDB:1HZ8}.
STRAND 400 404 {ECO:0000244|PDB:1IJQ}.
STRAND 406 413 {ECO:0000244|PDB:1IJQ}.
STRAND 420 423 {ECO:0000244|PDB:1IJQ}.
STRAND 427 435 {ECO:0000244|PDB:1IJQ}.
TURN 436 439 {ECO:0000244|PDB:1IJQ}.
STRAND 440 445 {ECO:0000244|PDB:1IJQ}.
TURN 446 449 {ECO:0000244|PDB:1IJQ}.
STRAND 450 455 {ECO:0000244|PDB:1IJQ}.
STRAND 466 469 {ECO:0000244|PDB:1IJQ}.
STRAND 478 482 {ECO:0000244|PDB:1IJQ}.
TURN 483 486 {ECO:0000244|PDB:1IJQ}.
STRAND 487 492 {ECO:0000244|PDB:1IJQ}.
TURN 493 496 {ECO:0000244|PDB:1IJQ}.
STRAND 497 502 {ECO:0000244|PDB:1IJQ}.
STRAND 505 513 {ECO:0000244|PDB:1IJQ}.
STRAND 519 525 {ECO:0000244|PDB:1IJQ}.
TURN 526 529 {ECO:0000244|PDB:1IJQ}.
STRAND 530 535 {ECO:0000244|PDB:1IJQ}.
STRAND 537 539 {ECO:0000244|PDB:1IJQ}.
STRAND 541 546 {ECO:0000244|PDB:1IJQ}.
STRAND 552 556 {ECO:0000244|PDB:1IJQ}.
STRAND 563 569 {ECO:0000244|PDB:1IJQ}.
TURN 570 573 {ECO:0000244|PDB:1IJQ}.
STRAND 574 579 {ECO:0000244|PDB:1IJQ}.
TURN 580 583 {ECO:0000244|PDB:1IJQ}.
STRAND 584 589 {ECO:0000244|PDB:1IJQ}.
STRAND 596 600 {ECO:0000244|PDB:1IJQ}.
TURN 602 605 {ECO:0000244|PDB:1IJQ}.
STRAND 606 614 {ECO:0000244|PDB:1IJQ}.
STRAND 617 622 {ECO:0000244|PDB:1IJQ}.
TURN 623 626 {ECO:0000244|PDB:1IJQ}.
STRAND 627 632 {ECO:0000244|PDB:1IJQ}.
TURN 633 635 {ECO:0000244|PDB:1IJQ}.
STRAND 640 643 {ECO:0000244|PDB:1IJQ}.
STRAND 652 656 {ECO:0000244|PDB:1IJQ}.
HELIX 657 659 {ECO:0000244|PDB:1IJQ}.
STRAND 668 672 {ECO:0000244|PDB:1IJQ}.
HELIX 673 676 {ECO:0000244|PDB:1IJQ}.
STRAND 678 683 {ECO:0000244|PDB:1IJQ}.
STRAND 693 697 {ECO:0000244|PDB:1IJQ}.
STRAND 708 713 {ECO:0000244|PDB:3P5B}.
STRAND 821 824 {ECO:0000244|PDB:3SO6}.
TURN 826 829 {ECO:0000244|PDB:3SO6}.
SEQUENCE 860 AA; 95376 MW; A4C28E9B8BADAD5E CRC64;
MGPWGWKLRW TVALLLAAAG TAVGDRCERN EFQCQDGKCI SYKWVCDGSA ECQDGSDESQ
ETCLSVTCKS GDFSCGGRVN RCIPQFWRCD GQVDCDNGSD EQGCPPKTCS QDEFRCHDGK
CISRQFVCDS DRDCLDGSDE ASCPVLTCGP ASFQCNSSTC IPQLWACDND PDCEDGSDEW
PQRCRGLYVF QGDSSPCSAF EFHCLSGECI HSSWRCDGGP DCKDKSDEEN CAVATCRPDE
FQCSDGNCIH GSRQCDREYD CKDMSDEVGC VNVTLCEGPN KFKCHSGECI TLDKVCNMAR
DCRDWSDEPI KECGTNECLD NNGGCSHVCN DLKIGYECLC PDGFQLVAQR RCEDIDECQD
PDTCSQLCVN LEGGYKCQCE EGFQLDPHTK ACKAVGSIAY LFFTNRHEVR KMTLDRSEYT
SLIPNLRNVV ALDTEVASNR IYWSDLSQRM ICSTQLDRAH GVSSYDTVIS RDIQAPDGLA
VDWIHSNIYW TDSVLGTVSV ADTKGVKRKT LFRENGSKPR AIVVDPVHGF MYWTDWGTPA
KIKKGGLNGV DIYSLVTENI QWPNGITLDL LSGRLYWVDS KLHSISSIDV NGGNRKTILE
DEKRLAHPFS LAVFEDKVFW TDIINEAIFS ANRLTGSDVN LLAENLLSPE DMVLFHNLTQ
PRGVNWCERT TLSNGGCQYL CLPAPQINPH SPKFTCACPD GMLLARDMRS CLTEAEAAVA
TQETSTVRLK VSSTAVRTQH TTTRPVPDTS RLPGATPGLT TVEIVTMSHQ ALGDVAGRGN
EKKPSSVRAL SIVLPIVLLV FLCLGVFLLW KNWRLKNINS INFDNPVYQK TTEDEVHICH
NQDGYSYPSR QMVSLEDDVA


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