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Low density lipoprotein receptor, isoform CRA_a (Low-density lipoprotein receptor)

 G3V7A5_RAT              Unreviewed;       879 AA.
G3V7A5;
16-NOV-2011, integrated into UniProtKB/TrEMBL.
16-NOV-2011, sequence version 1.
05-DEC-2018, entry version 71.
SubName: Full=Low density lipoprotein receptor, isoform CRA_a {ECO:0000313|EMBL:EDL78274.1};
SubName: Full=Low-density lipoprotein receptor {ECO:0000313|Ensembl:ENSRNOP00000013496};
Name=Ldlr {ECO:0000313|EMBL:EDL78274.1,
ECO:0000313|Ensembl:ENSRNOP00000013496, ECO:0000313|RGD:2998};
ORFNames=rCG_31837 {ECO:0000313|EMBL:EDL78274.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000013496, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000013496, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000013496,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDL78274.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL78274.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDL78274.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL78274.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000213|PubMed:16641100}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[5] {ECO:0000313|Ensembl:ENSRNOP00000013496}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000013496};
Ensembl;
Submitted (SEP-2011) to UniProtKB.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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EMBL; AC119556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473993; EDL78274.1; -; Genomic_DNA.
Ensembl; ENSRNOT00000013496; ENSRNOP00000013496; ENSRNOG00000009946.
RGD; 2998; Ldlr.
eggNOG; ENOG410KD0U; Eukaryota.
eggNOG; ENOG410Z5FJ; LUCA.
GeneTree; ENSGT00940000161046; -.
OMA; INVTLCE; -.
OrthoDB; EOG091G01MX; -.
TreeFam; TF351700; -.
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
Reactome; R-RNO-8964026; Chylomicron clearance.
Reactome; R-RNO-8964038; LDL clearance.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000009946; Expressed in 10 organ(s), highest expression level in liver.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:1990666; C:PCSK9-LDLR complex; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IEA:Ensembl.
GO; GO:0097242; P:amyloid-beta clearance; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0030299; P:intestinal cholesterol absorption; IEA:Ensembl.
GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
GO; GO:0061889; P:negative regulation of astrocyte activation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1903979; P:negative regulation of microglial cell activation; IEA:Ensembl.
GO; GO:0015914; P:phospholipid transport; IEA:Ensembl.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IEA:Ensembl.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; IEA:Ensembl.
GO; GO:0061771; P:response to caloric restriction; IEA:Ensembl.
CDD; cd00112; LDLa; 6.
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; 4.
SMART; SM00179; EGF_CA; 2.
SMART; SM00192; LDLa; 7.
SMART; SM00135; LY; 5.
SUPFAM; SSF57184; SSF57184; 1.
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; 4.
PROSITE; PS50068; LDLRA_2; 7.
PROSITE; PS51120; LDLRB; 5.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00124,
ECO:0000256|SAAS:SAAS00601599};
EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
ECO:0000256|SAAS:SAAS00032677};
Lipoprotein {ECO:0000313|EMBL:EDL78274.1};
Membrane {ECO:0000256|SAAS:SAAS00492819, ECO:0000256|SAM:Phobius};
Proteomics identification {ECO:0000213|PeptideAtlas:G3V7A5};
Receptor {ECO:0000313|EMBL:EDL78274.1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Repeat {ECO:0000256|SAAS:SAAS00594563};
Signal {ECO:0000256|SAM:SignalP};
Transmembrane {ECO:0000256|SAAS:SAAS00492819,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00492819,
ECO:0000256|SAM:Phobius}.
SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
CHAIN 24 879 {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5015091674.
TRANSMEM 806 829 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 315 354 EGF-like. {ECO:0000259|PROSITE:PS50026}.
DOMAIN 355 394 EGF-like. {ECO:0000259|PROSITE:PS50026}.
REPEAT 440 485 LDL-receptor class B.
{ECO:0000256|PROSITE-ProRule:PRU00461}.
REPEAT 486 528 LDL-receptor class B.
{ECO:0000256|PROSITE-ProRule:PRU00461}.
REPEAT 529 572 LDL-receptor class B.
{ECO:0000256|PROSITE-ProRule:PRU00461}.
REPEAT 573 617 LDL-receptor class B.
{ECO:0000256|PROSITE-ProRule:PRU00461}.
REPEAT 618 658 LDL-receptor class B.
{ECO:0000256|PROSITE-ProRule:PRU00461}.
DISULFID 27 39 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 34 52 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 89 104 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 109 121 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 116 134 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 128 143 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 148 160 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 155 173 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 198 210 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 205 223 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 217 232 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 237 249 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 244 262 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 256 271 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 285 303 {ECO:0000256|PROSITE-ProRule:PRU00124}.
DISULFID 359 369 {ECO:0000256|PROSITE-ProRule:PRU00076}.
SEQUENCE 879 AA; 96649 MW; F7026AAB0C9FF4BD CRC64;
MSTADLMLRW AIALLLAAAG VAAEDSCGKN EFQCRDGKCI VSKWVCDGSR ECPDGSDESP
ETCMSVTCRS GEFSCGGRVS RCIPDSWRCD GRTDCENGSD ELDCSPKTCS LDEFRCQDGK
CISRQFVCDQ DWDCLDGSDE AHCAATTCGP AHFRCNSSSC IPSLWACDGD RDCDDGSDEW
PQNCGGRDTA AEVVSSPCSS LEFHCGSSEC IHRSWVCDGA ADCKDKSDEE NCAVTTCRPD
EFQCADGSCI HGSRQCDREH DCKDMSDELG CINVTQCDGP NKFKCHSGEC ISLDKVCNSA
RDCRDWSDEP IKECKTNECL DNNGGCSHIC KDLKIGYECL CPSGFRLVDG HQCEDIDECQ
EPDTCSQLCV NLEGSFKCEC RAGFHMDPHT RVCKAVGSIG FLLFTNRHEV RKMTLDRSEY
TSLIPNLKNV VALDTEVANN RIYWSDLSQR KIYSAVMDQG TSLSYDAIIS GDLHAPDGLA
VDWIHGNIYW TDSVPGTVSV ADTKGVRRRT LFREKGSRPR AIVVDPVHGF MYWTDWGTPA
KIKKGGLNGV DIYSLVTEDI QWPNGITLDL PSGRLYWVDS KLHSISSIDV NGGGRKTILE
DEKQLAHPFS LAIYEDKVYW TDVLNEAIFS ANRLTGSDVN LVAKNLMSPE DIVLFHNVTQ
PRGVNWCEAT VLPNGGCQYM CLPAPQISAH SPKFTCACPD GMLLAKDMRS CLPEVDTVPT
TQGTSTIGPV VTTSAAVSLK RKEDPSATRH KEDPSATRHK EDPSATSTSR QPGDTPELST
VESVTVSSQV QGDMAGRGDE VQRHGVGFLS IFLPIALVAL LVFGAILLWR NWRLRNINSI
NFDNPVYQKT TEDEIHICRS QDGYTYPSRQ MVSLEDDVA


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