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Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (Apolipoprotein E receptor) (APOER) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]

 LRP1_HUMAN              Reviewed;        4544 AA.
Q07954; Q2PP12; Q86SW0; Q8IVG8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
07-APR-2021, entry version 225.
RecName: Full=Prolow-density lipoprotein receptor-related protein 1 {ECO:0000305};
Short=LRP-1;
AltName: Full=Alpha-2-macroglobulin receptor {ECO:0000303|PubMed:26142438};
Short=A2MR;
AltName: Full=Apolipoprotein E receptor;
Short=APOER;
AltName: CD_antigen=CD91;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 85 kDa subunit;
Short=LRP-85;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 515 kDa subunit;
Short=LRP-515;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 intracellular domain;
Short=LRPICD;
Flags: Precursor;
Name=LRP1 {ECO:0000312|HGNC:HGNC:6692}; Synonyms=A2MR, APR;
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), AND VARIANT PRO-2900.
TISSUE=Liver;
PubMed=3266596; DOI=10.1002/j.1460-2075.1988.tb03306.x;
Herz J., Hamann U., Rogne S., Myklebost O., Gausepohl H., Stanley K.K.;
"Surface location and high affinity for calcium of a 500-kd liver membrane
protein closely related to the LDL-receptor suggest a physiological role as
lipoprotein receptor.";
EMBO J. 7:4119-4127(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7534747; DOI=10.1006/geno.1994.1584;
Van Leuven F., Stas L., Hilliker C., Lorent K., Umans L., Serneels L.,
Overbergh L., Torrekens S., Moechars D., De Strooper B., Van den Berghe H.;
"Structure of the gene (LRP1) coding for the human alpha 2-macroglobulin
receptor lipoprotein receptor-related protein.";
Genomics 24:78-89(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-2900.
PubMed=9782078; DOI=10.1006/geno.1998.5408;
Van Leuven F., Stas L., Thiry E., Nelissen B., Miyake Y.;
"Strategy to sequence the 89 exons of the human LRP1 gene coding for the
lipoprotein receptor related protein: identification of one expressed
mutation among 48 polymorphisms.";
Genomics 52:138-144(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-2900.
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=2597675; DOI=10.1016/0167-4781(89)90107-3;
Kutt H., Herz J., Stanley K.K.;
"Structure of the low-density lipoprotein receptor-related protein (LRP)
promoter.";
Biochim. Biophys. Acta 1009:229-236(1989).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
TISSUE=Blood;
Glaeser C.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 150-166; 234-252; 685-695; 902-916; 1096-1109;
1743-1756; 2863-2874; 2949-2960; 3023-3039 AND 3277-3291.
TISSUE=Placenta;
PubMed=1698775;
Strickland D.K., Ashcom J.D., Williams S., Burgess W.H., Migliorini M.,
Argraves W.S.;
"Sequence identity between the alpha 2-macroglobulin receptor and low
density lipoprotein receptor-related protein suggests that this molecule is
a multifunctional receptor.";
J. Biol. Chem. 265:17401-17404(1990).
[10]
PROTEOLYTIC PROCESSING.
PubMed=2112085; DOI=10.1002/j.1460-2075.1990.tb08301.x;
Herz J., Kowal R.C., Goldstein J.L., Brown M.S.;
"Proteolytic processing of the 600 kd low density lipoprotein receptor-
related protein (LRP) occurs in a trans-Golgi compartment.";
EMBO J. 9:1769-1776(1990).
[11]
FUNCTION.
PubMed=1702392; DOI=10.1016/0014-5793(90)80530-v;
Kristensen T., Moestrup S.K., Gliemann J., Bendtsen L., Sand O.,
Sottrup-Jensen L.;
"Evidence that the newly cloned low-density-lipoprotein receptor related
protein (LRP) is the alpha 2-macroglobulin receptor.";
FEBS Lett. 276:151-155(1990).
[12]
FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
PubMed=1618748;
Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K.,
Saelinger C.B.;
"The alpha 2-macroglobulin receptor/low density lipoprotein receptor-
related protein binds and internalizes Pseudomonas exotoxin A.";
J. Biol. Chem. 267:12420-12423(1992).
[13]
INTERACTION WITH MDK.
PubMed=10772929; DOI=10.1006/bbrc.2000.2549;
Muramatsu H., Zou K., Sakaguchi N., Ikematsu S., Sakuma S., Muramatsu T.;
"LDL receptor-related protein as a component of the midkine receptor.";
Biochem. Biophys. Res. Commun. 270:936-941(2000).
[14]
INTERACTION WITH GULP1, AND MUTAGENESIS OF ASN-4470 AND ASN-4504.
PubMed=11729193; DOI=10.1074/jbc.m109336200;
Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G.,
Henson P.M., Ravichandran K.S.;
"Interaction of CED-6/GULP, an adapter protein involved in engulfment of
apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-
related protein (LRP).";
J. Biol. Chem. 277:11772-11779(2002).
[15]
PHOSPHORYLATION AT TYR-4507, MUTAGENESIS OF 4470-ASN--TYR-4473 AND
4504-ASN--TYR-4507, AND INTERACTION WITH PDGF.
PubMed=11854294; DOI=10.1074/jbc.m200427200;
Loukinova E., Ranganathan S., Kuznetsov S., Gorlatova N., Migliorini M.M.,
Loukinov D., Ulery P.G., Mikhailenko I., Lawrence D.A., Strickland D.K.;
"Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of
the low density lipoprotein receptor-related protein (LRP). Evidence for
integrated co-receptor function between LRP and the PDGF.";
J. Biol. Chem. 277:15499-15506(2002).
[16]
FUNCTION, AND PROTEOLYTIC PROCESSING.
PubMed=11907044; DOI=10.1074/jbc.m201979200;
May P., Reddy Y.K., Herz J.;
"Proteolytic processing of low density lipoprotein receptor-related protein
mediates regulated release of its intracellular domain.";
J. Biol. Chem. 277:18736-18743(2002).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12888553; DOI=10.1074/jbc.m306403200;
Kinoshita A., Shah T., Tangredi M.M., Strickland D.K., Hyman B.T.;
"The intracellular domain of the low density lipoprotein receptor-related
protein modulates transactivation mediated by amyloid precursor protein and
Fe65.";
J. Biol. Chem. 278:41182-41188(2003).
[18]
FUNCTION.
PubMed=12713657; DOI=10.1034/j.1600-0854.2003.00086_4_5.x;
May P., Herz J.;
"LDL receptor-related proteins in neurodevelopment.";
Traffic 4:291-301(2003).
[19]
INTERACTION WITH LRPAP1; PDGFB; PLAU AND SERPINE1.
PubMed=15053742; DOI=10.1042/bj20040149;
Gliemann J., Hermey G., Nykjaer A., Petersen C.M., Jacobsen C.,
Andreasen P.A.;
"The mosaic receptor sorLA/LR11 binds components of the plasminogen-
activating system and platelet-derived growth factor-BB similarly to LRP1
(low-density lipoprotein receptor-related protein), but mediates slow
internalization of bound ligand.";
Biochem. J. 381:203-212(2004).
[20]
INTERACTION WITH PLAUR.
PubMed=14764453; DOI=10.1161/01.res.0000120862.79154.0f;
Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S., Kanaki T.,
Shibasaki M., Takahashi K., Schneider W.J., Saito Y.;
"LR11, an LDL receptor gene family member, is a novel regulator of smooth
muscle cell migration.";
Circ. Res. 94:752-758(2004).
[21]
PHOSPHORYLATION AT THR-4460; SER-4517; SER-4520 AND SER-4523, MUTAGENESIS
OF THR-4460; THR-4472; SER-4517; SER-4520 AND SER-4523, AND INTERACTION
WITH SHC1; GULP1 AND DAB1.
PubMed=15272003; DOI=10.1074/jbc.m407592200;
Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D.,
Mikhailenko I., Hyman B.T., Strickland D.K.;
"Serine and threonine phosphorylation of the low density lipoprotein
receptor-related protein by protein kinase Calpha regulates endocytosis and
association with adaptor molecules.";
J. Biol. Chem. 279:40536-40544(2004).
[22]
INTERACTION WITH SNX17.
PubMed=15769472; DOI=10.1016/j.jmb.2005.02.004;
Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V.,
Schreckenberger S., Hahn H., Bohnensack R.;
"Functions of sorting nexin 17 domains and recognition motif for P-selectin
trafficking.";
J. Mol. Biol. 347:813-825(2005).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-2127 AND
ASN-3048.
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).
[24]
IDENTIFICATION IN A COMPLEX WITH CUBN AND PID1, AND INTERACTION WITH CUBN
AND PID1.
PubMed=17124247; DOI=10.1074/mcp.m600289-mcp200;
Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C.,
Scaloni A., Napolitano M., Russo T., Zambrano N.;
"Identification of the ligands of protein interaction domains through a
functional approach.";
Mol. Cell. Proteomics 6:333-345(2007).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-1511;
ASN-1575; ASN-1616; ASN-1645; ASN-1763; ASN-2127; ASN-2815; ASN-3048;
ASN-3089; ASN-3488; ASN-3788; ASN-3953; ASN-4075 AND ASN-4125.
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]
GLYCOSYLATION AT ASN-729 AND ASN-1511.
PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core fucosylated
glycoproteins.";
Mol. Cell. Proteomics 8:913-923(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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4520, AND 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).
[29]
FUNCTION, AND INTERACTION WITH LRPAP1 AND MAPT1.
PubMed=32296178; DOI=10.1038/s41586-020-2156-5;
Rauch J.N., Luna G., Guzman E., Challis C., Sibih Y.E., Leshuk C.,
Hernandez I., Wegmann S., Hyman B.T., Gradinaru V., Kampmann M.,
Kosik K.S.;
"LRP1 is a master regulator of tau uptake and spread.";
Nature 0:0-0(2020).
[30]
STRUCTURE BY NMR OF 1059-1100 IN COMPLEX WITH CALCIUM IONS, AND DISULFIDE
BONDS.
PubMed=10318830; DOI=10.1074/jbc.274.20.14130;
Huang W., Dolmer K., Gettins P.G.W.;
"NMR solution structure of complement-like repeat CR8 from the low density
lipoprotein receptor-related protein.";
J. Biol. Chem. 274:14130-14136(1999).
[31]
STRUCTURE BY NMR OF 851-893 IN COMPLEX WITH CALCIUM IONS, AND DISULFIDE
BONDS.
PubMed=10652313; DOI=10.1074/jbc.275.5.3264;
Dolmer K., Huang W., Gettins P.G.W.;
"NMR solution structure of complement-like repeat CR3 from the low density
lipoprotein receptor-related protein. Evidence for specific binding to the
receptor binding domain of human alpha(2)-macroglobulin.";
J. Biol. Chem. 275:3264-3269(2000).
[32]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1012-1054 IN COMPLEX WITH CALCIUM
IONS, AND DISULFIDE BONDS.
PubMed=11735395; DOI=10.1021/bi015688m;
Simonovic M., Dolmer K., Huang W., Strickland D.K., Volz K., Gettins P.G.;
"Calcium coordination and pH dependence of the calcium affinity of ligand-
binding repeat CR7 from the LRP. Comparison with related domains from the
LRP and the LDL receptor.";
Biochemistry 40:15127-15134(2001).
[33]
STRUCTURE BY NMR OF 932-1013 IN COMPLEX WITH LRPAP1 AND CALCIUM IONS, AND
DISULFIDE BONDS.
PubMed=16938309; DOI=10.1016/j.jmb.2006.07.013;
Jensen G.A., Andersen O.M.J.J., Bonvin A.M., Bjerrum-Bohr I., Etzerodt M.,
Thoegersen H.C., O'Shea C., Poulsen F.M., Kragelund B.B.;
"Binding site structure of one LRP-RAP complex: implications for a common
ligand-receptor binding motif.";
J. Mol. Biol. 362:700-716(2006).
[34]
VARIANTS [LARGE SCALE ANALYSIS] LYS-869 AND HIS-3760.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[35]
VARIANT GLN-3258.
PubMed=23033978; DOI=10.1056/nejmoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[36]
VARIANT KPA ARG-1245, CHARACTERIZATION OF VARIANT KPA ARG-1245, FUNCTION,
AND INVOLVEMENT IN KPA.
PubMed=26142438; DOI=10.1136/jmedgenet-2014-102931;
Klar J., Schuster J., Khan T.N., Jameel M., Maebert K., Forsberg L.,
Baig S.A., Baig S.M., Dahl N.;
"Whole exome sequencing identifies LRP1 as a pathogenic gene in autosomal
recessive keratosis pilaris atrophicans.";
J. Med. Genet. 52:599-606(2015).
-!- FUNCTION: Endocytic receptor involved in endocytosis and in
phagocytosis of apoptotic cells (PubMed:11907044, PubMed:12713657).
Required for early embryonic development (By similarity). Involved in
cellular lipid homeostasis. Involved in the plasma clearance of
chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as
well as the local metabolism of complexes between plasminogen
activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-
macroglobulin receptor (PubMed:26142438, PubMed:1702392). Acts as
TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as
its subsequent spread (PubMed:32296178). May modulate cellular events,
such as APP metabolism, kinase-dependent intracellular signaling,
neuronal calcium signaling as well as neurotransmission
(PubMed:12888553). {ECO:0000250|UniProtKB:Q91ZX7,
ECO:0000269|PubMed:11907044, ECO:0000269|PubMed:12713657,
ECO:0000269|PubMed:12888553, ECO:0000269|PubMed:1702392,
ECO:0000269|PubMed:26142438, ECO:0000269|PubMed:32296178}.
-!- FUNCTION: (Microbial infection) Functions as a receptor for Pseudomonas
aeruginosa exotoxin A. {ECO:0000269|PubMed:1618748}.
-!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a
non-covalently attached 515-kDa N-terminal subunit. Intracellular
domain interacts with MAFB (By similarity). Found in a complex with
PID1/PCLI1, LRP1 and CUBNI (PubMed:17124247). Interacts with SNX17,
PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with
SHC1, GULP1 and DAB1. Can weakly interact (via NPXY motif) with DAB2
(via PID domain); the interaction is enhanced by tyrosine
phosphorylation of the NPXY motif. Interacts with MDK; promotes
neuronal survival (PubMed:10772929). Interacts with LRPAP1; this
interaction is followed by rapid internalization (PubMed:15053742,
PubMed:32296178, PubMed:16938309). Interacts with uPA/PLAU and
PAI1/SERPINE1, either individually or in complex with each other,
leading to rapid endocytosis; this interaction is abolished in the
presence of LRPAP1/RAP (PubMed:15053742). Also interacts with tPA/PLAT
alone or in complex with SERPINE1 (PubMed:15053742). Interacts with the
urokinase receptor PLAUR; this interaction leads to PLAUR
internalization and is impaired in the presence of SORL1
(PubMed:14764453). Interacts with PDGFB (PubMed:15053742). Interacts
with TAU/MAPT, leading to endocytosis; this interaction is reduced in
the presence of LRPAP1/RAP (PubMed:32296178).
{ECO:0000250|UniProtKB:Q91ZX7, ECO:0000269|PubMed:10772929,
ECO:0000269|PubMed:11729193, ECO:0000269|PubMed:11854294,
ECO:0000269|PubMed:14764453, ECO:0000269|PubMed:15053742,
ECO:0000269|PubMed:15272003, ECO:0000269|PubMed:15769472,
ECO:0000269|PubMed:16938309, ECO:0000269|PubMed:17124247,
ECO:0000269|PubMed:32296178}.
-!- SUBUNIT: (Microbial infection) Interacts with bacterial exotoxins.
{ECO:0000269|PubMed:1618748}.
-!- INTERACTION:
Q07954; Q92685: ALG3; NbExp=2; IntAct=EBI-1046087, EBI-2848814;
Q07954; O00213: APBB1; NbExp=4; IntAct=EBI-1046087, EBI-81694;
Q07954; P02649: APOE; NbExp=23; IntAct=EBI-1046087, EBI-1222467;
Q07954; P78352: DLG4; NbExp=2; IntAct=EBI-1046087, EBI-80389;
Q07954; Q15485: FCN2; NbExp=2; IntAct=EBI-1046087, EBI-7468784;
Q07954; Q12879: GRIN2A; NbExp=2; IntAct=EBI-1046087, EBI-7249937;
Q07954; P30533: LRPAP1; NbExp=4; IntAct=EBI-1046087, EBI-715927;
Q07954; P11226: MBL2; NbExp=5; IntAct=EBI-1046087, EBI-5325353;
Q07954; Q63722: Jag1; Xeno; NbExp=4; IntAct=EBI-1046087, EBI-4567800;
Q07954; Q03350: Thbs2; Xeno; NbExp=2; IntAct=EBI-1046087, EBI-4567830;
Q07954-2; P05067: APP; NbExp=3; IntAct=EBI-25833471, EBI-77613;
Q07954-2; Q13867: BLMH; NbExp=3; IntAct=EBI-25833471, EBI-718504;
Q07954-2; P04271: S100B; NbExp=3; IntAct=EBI-25833471, EBI-458391;
Q07954-2; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-25833471, EBI-357085;
Q07954-2; P43405-2: SYK; NbExp=3; IntAct=EBI-25833471, EBI-25892332;
Q07954-2; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-25833471, EBI-11141397;
-!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
1 85 kDa subunit]: Cell membrane; Single-pass type I membrane protein.
Membrane, coated pit.
-!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
1 515 kDa subunit]: Cell membrane; Peripheral membrane protein;
Extracellular side. Membrane, coated pit.
-!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
1 intracellular domain]: Cytoplasm {ECO:0000269|PubMed:12888553}.
Nucleus {ECO:0000269|PubMed:12888553}. Note=After cleavage, the
intracellular domain (LRPICD) is detected both in the cytoplasm and in
the nucleus. {ECO:0000269|PubMed:12888553}.
-!- SUBCELLULAR LOCATION: Golgi outpost {ECO:0000250|UniProtKB:G3V928}.
Cytoplasm, cytoskeleton, microtubule organizing center
{ECO:0000250|UniProtKB:G3V928}. Note=Localizes to the postsynaptic
Golgi apparatus region, also named Golgi outpost, which shapes dendrite
morphology by functioning as sites of acentrosomal microtubule
nucleation. {ECO:0000250|UniProtKB:G3V928}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q07954-1; Sequence=Displayed;
Name=2;
IsoId=Q07954-2; Sequence=VSP_056919, VSP_056920;
-!- TISSUE SPECIFICITY: Most abundant in liver, brain and lung.
-!- PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515
kDa large extracellular domain (LRP-515) that remains non-covalently
associated. Gamma-secretase-dependent cleavage of LRP-85 releases the
intracellular domain from the membrane. {ECO:0000269|PubMed:11907044,
ECO:0000269|PubMed:2112085}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Phosphorylated on serine and threonine residues.
-!- PTM: Phosphorylated on tyrosine residues upon stimulation with PDGF.
Tyrosine phosphorylation promotes interaction with SHC1.
-!- DISEASE: Keratosis pilaris atrophicans (KPA) [MIM:604093]: A group of
rare genodermatoses characterized by keratotic follicular papules,
variable degrees of inflammation, and secondary atrophic scarring. Most
cases are associated with an atopic diathesis and keratosis pilaris on
the extensor extremities. KPA is comprised of three distinct clinical
subtypes: keratosis pilaris atrophicans faciei, atrophoderma
vermiculatum, and keratosis follicularis spinulosa decalvans. Affected
individuals may present with features overlapping the 3 subtypes.
{ECO:0000269|PubMed:26142438}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; X13916; CAA32112.1; -; mRNA.
EMBL; AF058427; AAC64265.1; -; Genomic_DNA.
EMBL; DQ314873; ABC40732.1; -; Genomic_DNA.
EMBL; AC023237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC045107; AAH45107.1; -; mRNA.
EMBL; X15424; CAA33464.1; -; Genomic_DNA.
EMBL; Y18524; CAD57169.1; -; Genomic_DNA.
CCDS; CCDS8932.1; -. [Q07954-1]
PIR; S02392; S02392.
RefSeq; NP_002323.2; NM_002332.2. [Q07954-1]
PDB; 1CR8; NMR; -; A=1059-1100.
PDB; 1D2L; NMR; -; A=851-893.
PDB; 1J8E; X-ray; 1.85 A; A=1011-1054.
PDB; 2FYJ; NMR; -; A=932-1013.
PDB; 2FYL; NMR; -; B=932-1013.
PDB; 2KNX; NMR; -; A=2770-2817.
PDB; 2KNY; NMR; -; A=2770-2817.
PDBsum; 1CR8; -.
PDBsum; 1D2L; -.
PDBsum; 1J8E; -.
PDBsum; 2FYJ; -.
PDBsum; 2FYL; -.
PDBsum; 2KNX; -.
PDBsum; 2KNY; -.
SMR; Q07954; -.
BioGRID; 110215; 137.
ComplexPortal; CPX-4310; Prolow-density lipoprotein receptor-related protein 1 complex.
CORUM; Q07954; -.
DIP; DIP-50613N; -.
ELM; Q07954; -.
IntAct; Q07954; 87.
MINT; Q07954; -.
STRING; 9606.ENSP00000243077; -.
DrugBank; DB00025; Antihemophilic factor, human recombinant.
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB13152; Coagulation Factor IX Human.
DrugBank; DB06245; Lanoteplase.
DrugBank; DB13998; Lonoctocog alfa.
DrugBank; DB13999; Moroctocog alfa.
DrugBank; DB00031; Tenecteplase.
TCDB; 9.B.87.1.16; the selenoprotein p receptor (selp-receptor) family.
CarbonylDB; Q07954; -.
GlyConnect; 1638; 61 N-Linked glycans (38 sites), 1 O-Linked glycan (1 site).
GlyGen; Q07954; 74 sites, 3 N-linked glycans (2 sites), 2 O-linked glycans (12 sites).
iPTMnet; Q07954; -.
MetOSite; Q07954; -.
PhosphoSitePlus; Q07954; -.
BioMuta; LRP1; -.
DMDM; 317373384; -.
CPTAC; CPTAC-1617; -.
CPTAC; CPTAC-2222; -.
CPTAC; CPTAC-2223; -.
EPD; Q07954; -.
jPOST; Q07954; -.
MassIVE; Q07954; -.
MaxQB; Q07954; -.
PaxDb; Q07954; -.
PeptideAtlas; Q07954; -.
PRIDE; Q07954; -.
ProteomicsDB; 58559; -. [Q07954-1]
ProteomicsDB; 69639; -.
Antibodypedia; 4353; 1105 antibodies.
Ensembl; ENST00000243077; ENSP00000243077; ENSG00000123384. [Q07954-1]
Ensembl; ENST00000338962; ENSP00000341264; ENSG00000123384. [Q07954-2]
GeneID; 4035; -.
KEGG; hsa:4035; -.
UCSC; uc001snd.4; human. [Q07954-1]
CTD; 4035; -.
DisGeNET; 4035; -.
GeneCards; LRP1; -.
HGNC; HGNC:6692; LRP1.
HPA; ENSG00000123384; Low tissue specificity.
MalaCards; LRP1; -.
MIM; 107770; gene.
MIM; 604093; phenotype.
neXtProt; NX_Q07954; -.
OpenTargets; ENSG00000123384; -.
Orphanet; 79100; Atrophoderma vermiculata.
Orphanet; 2340; Keratosis follicularis spinulosa decalvans.
PharmGKB; PA233; -.
VEuPathDB; HostDB:ENSG00000123384.13; -.
eggNOG; KOG1215; Eukaryota.
GeneTree; ENSGT00940000157899; -.
HOGENOM; CLU_000085_1_0_1; -.
InParanoid; Q07954; -.
OMA; QSRWGAV; -.
OrthoDB; 1606at2759; -.
PhylomeDB; Q07954; -.
TreeFam; TF315253; -.
PathwayCommons; Q07954; -.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; Q07954; -.
BioGRID-ORCS; 4035; 9 hits in 991 CRISPR screens.
ChiTaRS; LRP1; human.
EvolutionaryTrace; Q07954; -.
GeneWiki; LRP1; -.
GenomeRNAi; 4035; -.
Pharos; Q07954; Tbio.
PRO; PR:Q07954; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; Q07954; protein.
Bgee; ENSG00000123384; Expressed in stromal cell of endometrium and 240 other tissues.
ExpressionAtlas; Q07954; baseline and differential.
Genevisible; Q07954; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0032593; C:insulin-responsive compartment; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0016020; C:membrane; NAS:ARUK-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0098797; C:plasma membrane protein complex; TAS:ARUK-UCL.
GO; GO:0150051; C:postsynaptic Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0016964; F:alpha-2 macroglobulin receptor activity; IMP:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
GO; GO:0034185; F:apolipoprotein binding; IDA:UniProtKB.
GO; GO:0030226; F:apolipoprotein receptor activity; TAS:ARUK-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0038024; F:cargo receptor activity; IMP:ARUK-UCL.
GO; GO:0032050; F:clathrin heavy chain binding; IPI:ARUK-UCL.
GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; TAS:ARUK-UCL.
GO; GO:0070325; F:lipoprotein particle receptor binding; IC:BHF-UCL.
GO; GO:0005041; F:low-density lipoprotein particle receptor activity; TAS:ARUK-UCL.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0097242; P:amyloid-beta clearance; TAS:BHF-UCL.
GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IMP:ARUK-UCL.
GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IGI:ARUK-UCL.
GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0043277; P:apoptotic cell clearance; ISS:BHF-UCL.
GO; GO:0002265; P:astrocyte activation involved in immune response; ISS:ARUK-UCL.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0044242; P:cellular lipid catabolic process; IEA:Ensembl.
GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0061642; P:chemoattraction of axon; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; TAS:ARUK-UCL.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
GO; GO:0042953; P:lipoprotein transport; NAS:UniProtKB.
GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:1905049; P:negative regulation of metallopeptidase activity; IC:ARUK-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; ISS:BHF-UCL.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISS:BHF-UCL.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:BHF-UCL.
GO; GO:0006909; P:phagocytosis; IMP:ARUK-UCL.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IEA:Ensembl.
GO; GO:0010942; P:positive regulation of cell death; IGI:ARUK-UCL.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:BHF-UCL.
GO; GO:1904109; P:positive regulation of cholesterol import; IEA:Ensembl.
GO; GO:0048694; P:positive regulation of collateral sprouting of injured axon; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IGI:ARUK-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0032370; P:positive regulation of lipid transport; ISS:BHF-UCL.
GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IMP:ARUK-UCL.
GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IGI:ARUK-UCL.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IGI:ARUK-UCL.
GO; GO:1900149; P:positive regulation of Schwann cell migration; IEA:Ensembl.
GO; GO:1904300; P:positive regulation of transcytosis; ISS:ARUK-UCL.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0031623; P:receptor internalization; TAS:ARUK-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:BHF-UCL.
GO; GO:0032374; P:regulation of cholesterol transport; ISS:BHF-UCL.
GO; GO:0010715; P:regulation of extracellular matrix disassembly; TAS:ParkinsonsUK-UCL.
GO; GO:0032429; P:regulation of phospholipase A2 activity; ISS:BHF-UCL.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0045056; P:transcytosis; TAS:ARUK-UCL.
GO; GO:0150104; P:transport across blood-brain barrier; ISS:ARUK-UCL.
CDD; cd00112; LDLa; 31.
Gene3D; 2.120.10.30; -; 8.
Gene3D; 4.10.400.10; -; 29.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
InterPro; IPR032485; DUF5050.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; PF12662; cEGF; 1.
Pfam; PF16472; DUF5050; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00057; Ldl_recept_a; 29.
Pfam; PF00058; Ldl_recept_b; 12.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 26.
SMART; SM00179; EGF_CA; 7.
SMART; SM00192; LDLa; 31.
SMART; SM00135; LY; 35.
SUPFAM; SSF57184; SSF57184; 4.
SUPFAM; SSF57424; SSF57424; 30.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS00022; EGF_1; 5.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS01209; LDLRA_1; 27.
PROSITE; PS50068; LDLRA_2; 31.
PROSITE; PS51120; LDLRB; 34.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Calcium; Cell membrane;
Coated pit; Cytoplasm; Cytoskeleton; Developmental protein;
Direct protein sequencing; Disease variant; Disulfide bond;
EGF-like domain; Endocytosis; Glycoprotein; Golgi apparatus; Membrane;
Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1..19
/evidence="ECO:0000255"
CHAIN 20..4544
/note="Prolow-density lipoprotein receptor-related protein
1"
/id="PRO_0000017317"
CHAIN 20..?3943
/note="Low-density lipoprotein receptor-related protein 1
515 kDa subunit"
/id="PRO_0000302750"
CHAIN ?3944..4544
/note="Low-density lipoprotein receptor-related protein 1
85 kDa subunit"
/id="PRO_0000302751"
CHAIN ?4441..4544
/note="Low-density lipoprotein receptor-related protein 1
intracellular domain"
/id="PRO_0000302752"
TOPO_DOM 20..4419
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 4420..4444
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 4445..4544
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 25..66
/note="LDL-receptor class A 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 70..110
/note="LDL-receptor class A 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 111..149
/note="EGF-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 150..189
/note="EGF-like 2; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 292..334
/note="LDL-receptor class B 1"
REPEAT 335..378
/note="LDL-receptor class B 2"
REPEAT 379..422
/note="LDL-receptor class B 3"
DOMAIN 474..520
/note="EGF-like 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 571..613
/note="LDL-receptor class B 4"
REPEAT 614..659
/note="LDL-receptor class B 5"
REPEAT 660..710
/note="LDL-receptor class B 6"
REPEAT 711..754
/note="LDL-receptor class B 7"
DOMAIN 803..843
/note="EGF-like 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 852..892
/note="LDL-receptor class A 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 893..933
/note="LDL-receptor class A 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 934..973
/note="LDL-receptor class A 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 974..1013
/note="LDL-receptor class A 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 1013..1053
/note="LDL-receptor class A 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 1060..1099
/note="LDL-receptor class A 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 1102..1142
/note="LDL-receptor class A 9"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 1143..1182
/note="LDL-receptor class A 10"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 1183..1222
/note="EGF-like 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 1223..1262
/note="EGF-like 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 1309..1355
/note="LDL-receptor class B 8"
REPEAT 1356..1398
/note="LDL-receptor class B 9"
REPEAT 1399..1445
/note="LDL-receptor class B 10"
REPEAT 1446..1490
/note="LDL-receptor class B 11"
REPEAT 1491..1531
/note="LDL-receptor class B 12"
DOMAIN 1536..1579
/note="EGF-like 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 1627..1669
/note="LDL-receptor class B 13"
REPEAT 1670..1713
/note="LDL-receptor class B 14"
REPEAT 1714..1753
/note="LDL-receptor class B 15"
REPEAT 1754..1798
/note="LDL-receptor class B 16"
DOMAIN 1846..1887
/note="EGF-like 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 1934..1976
/note="LDL-receptor class B 17"
REPEAT 1977..2019
/note="LDL-receptor class B 18"
REPEAT 2020..2063
/note="LDL-receptor class B 19"
REPEAT 2064..2107
/note="LDL-receptor class B 20"
DOMAIN 2155..2195
/note="EGF-like 9"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 2253..2294
/note="LDL-receptor class B 21"
REPEAT 2295..2343
/note="LDL-receptor class B 22"
REPEAT 2344..2388
/note="LDL-receptor class B 23"
REPEAT 2389..2431
/note="LDL-receptor class B 24"
REPEAT 2432..2473
/note="LDL-receptor class B 25"
DOMAIN 2478..2518
/note="EGF-like 10"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 2522..2563
/note="LDL-receptor class A 11"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2564..2602
/note="LDL-receptor class A 12"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2603..2641
/note="LDL-receptor class A 13"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2642..2690
/note="LDL-receptor class A 14"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2694..2732
/note="LDL-receptor class A 15"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2732..2771
/note="LDL-receptor class A 16"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2772..2814
/note="LDL-receptor class A 17"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2816..2855
/note="LDL-receptor class A 18"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2856..2899
/note="LDL-receptor class A 19"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2902..2940
/note="LDL-receptor class A 20"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 2941..2981
/note="EGF-like 11"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 2982..3022
/note="EGF-like 12; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 3069..3113
/note="LDL-receptor class B 26"
REPEAT 3114..3156
/note="LDL-receptor class B 27"
REPEAT 3157..3200
/note="LDL-receptor class B 28"
REPEAT 3201..3243
/note="LDL-receptor class B 29"
REPEAT 3244..3284
/note="LDL-receptor class B 30"
DOMAIN 3290..3331
/note="EGF-like 13"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 3332..3371
/note="LDL-receptor class A 21"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3372..3410
/note="LDL-receptor class A 22"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3411..3450
/note="LDL-receptor class A 23"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3451..3491
/note="LDL-receptor class A 24"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3492..3533
/note="LDL-receptor class A 25"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3534..3572
/note="LDL-receptor class A 26"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3573..3611
/note="LDL-receptor class A 27"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3611..3649
/note="LDL-receptor class A 28"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3652..3692
/note="LDL-receptor class A 29"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3693..3733
/note="LDL-receptor class A 30"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3739..3778
/note="LDL-receptor class A 31"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 3781..3823
/note="EGF-like 14"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 3824..3861
/note="EGF-like 15"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 3912..3954
/note="LDL-receptor class B 31"
REPEAT 3970..4012
/note="LDL-receptor class B 32"
REPEAT 4013..4056
/note="LDL-receptor class B 33"
REPEAT 4057..4101
/note="LDL-receptor class B 34"
DOMAIN 4147..4183
/note="EGF-like 16"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 4196..4232
/note="EGF-like 17"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 4232..4268
/note="EGF-like 18"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 4268..4304
/note="EGF-like 19"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 4304..4340
/note="EGF-like 20"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 4340..4375
/note="EGF-like 21"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 4373..4409
/note="EGF-like 22"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REGION 4445..4544
/note="Interaction with MAFB"
/evidence="ECO:0000250|UniProtKB:Q91ZX7"
MOTIF 3940..3943
/note="Recognition site for proteolytical processing"
/evidence="ECO:0000255"
MOTIF 4502..4507
/note="NPXY motif"
METAL 871
/note="Calcium 1; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:10652313"
METAL 874
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:10652313"
METAL 876
/note="Calcium 1; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:10652313"
METAL 878
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:10652313"
METAL 884
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:10652313"
METAL 885
/note="Calcium 1"
/evidence="ECO:0000269|PubMed:10652313"
METAL 1032
/note="Calcium 2; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:11735395"
METAL 1035
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:11735395"
METAL 1037
/note="Calcium 2; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:11735395"
METAL 1039
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:11735395"
METAL 1045
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:11735395"
METAL 1046
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:11735395"
METAL 1080
/note="Calcium 3; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:10318830"
METAL 1083
/note="Calcium 3"
/evidence="ECO:0000269|PubMed:10318830"
METAL 1085
/note="Calcium 3; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:10318830"
METAL 1087
/note="Calcium 3"
/evidence="ECO:0000269|PubMed:10318830"
METAL 1093
/note="Calcium 3"
/evidence="ECO:0000269|PubMed:10318830"
METAL 1094
/note="Calcium 3"
/evidence="ECO:0000269|PubMed:10318830"
MOD_RES 2009
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q91ZX7"
MOD_RES 4460
/note="Phosphothreonine"
/evidence="ECO:0000305|PubMed:15272003"
MOD_RES 4507
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:11854294"
MOD_RES 4517
/note="Phosphoserine"
/evidence="ECO:0000305|PubMed:15272003"
MOD_RES 4520
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 4523
/note="Phosphoserine"
/evidence="ECO:0000305|PubMed:15272003"
CARBOHYD 114
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 136
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 185
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 239
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 274
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 357
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 446
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218"
CARBOHYD 729
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
CARBOHYD 928
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1050
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1154
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1155
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1195
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1218
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1511
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218"
CARBOHYD 1558
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1575
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 1616
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 1645
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 1723
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1733
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1763
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 1825
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1933
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1995
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2048
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2117
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2127
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218"
CARBOHYD 2472
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2502
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2521
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2539
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2601
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2620
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2638
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2815
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 2905
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 3048
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218"
CARBOHYD 3089
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 3264
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 3333
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 3488
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 3662
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 3788
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 3839
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 3953
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 4075
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 4125
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 4179
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 4278
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 4279
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 4364
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 27..40
/evidence="ECO:0000250"
DISULFID 34..53
/evidence="ECO:0000250"
DISULFID 47..64
/evidence="ECO:0000250"
DISULFID 72..85
/evidence="ECO:0000250"
DISULFID 79..98
/evidence="ECO:0000250"
DISULFID 92..108
/evidence="ECO:0000250"
DISULFID 115..124
/evidence="ECO:0000250"
DISULFID 120..133
/evidence="ECO:0000250"
DISULFID 135..148
/evidence="ECO:0000250"
DISULFID 154..164
/evidence="ECO:0000250"
DISULFID 160..173
/evidence="ECO:0000250"
DISULFID 175..188
/evidence="ECO:0000250"
DISULFID 478..493
/evidence="ECO:0000250"
DISULFID 489..504
/evidence="ECO:0000250"
DISULFID 506..519
/evidence="ECO:0000250"
DISULFID 807..818
/evidence="ECO:0000250"
DISULFID 814..827
/evidence="ECO:0000250"
DISULFID 829..842
/evidence="ECO:0000250"
DISULFID 854..866
DISULFID 861..879
DISULFID 873..890
DISULFID 895..907
/evidence="ECO:0000250"
DISULFID 902..920
/evidence="ECO:0000250"
DISULFID 914..931
/evidence="ECO:0000250"
DISULFID 936..948
DISULFID 943..961
DISULFID 955..971
DISULFID 976..989
DISULFID 984..1002
DISULFID 996..1011
DISULFID 1015..1027
DISULFID 1022..1040
DISULFID 1034..1051
DISULFID 1062..1075
DISULFID 1069..1088
DISULFID 1082..1097
DISULFID 1104..1118
/evidence="ECO:0000250"
DISULFID 1112..1131
/evidence="ECO:0000250"
DISULFID 1125..1140
/evidence="ECO:0000250"
DISULFID 1145..1159
/evidence="ECO:0000250"
DISULFID 1152..1172
/evidence="ECO:0000250"
DISULFID 1166..1182
/evidence="ECO:0000250"
DISULFID 1185..1196
/evidence="ECO:0000250"
DISULFID 1192..1206
/evidence="ECO:0000250"
DISULFID 1208..1221
/evidence="ECO:0000250"
DISULFID 1227..1237
/evidence="ECO:0000250"
DISULFID 1233..1246
/evidence="ECO:0000250"
DISULFID 1248..1261
/evidence="ECO:0000250"
DISULFID 1540..1553
/evidence="ECO:0000250"
DISULFID 1549..1563
/evidence="ECO:0000250"
DISULFID 1565..1578
/evidence="ECO:0000250"
DISULFID 1850..1861
/evidence="ECO:0000250"
DISULFID 1857..1871
/evidence="ECO:0000250"
DISULFID 1873..1886
/evidence="ECO:0000250"
DISULFID 2159..2170
/evidence="ECO:0000250"
DISULFID 2166..2180
/evidence="ECO:0000250"
DISULFID 2182..2194
/evidence="ECO:0000250"
DISULFID 2482..2493
/evidence="ECO:0000250"
DISULFID 2489..2503
/evidence="ECO:0000250"
DISULFID 2505..2517
/evidence="ECO:0000250"
DISULFID 2524..2537
/evidence="ECO:0000250"
DISULFID 2532..2550
/evidence="ECO:0000250"
DISULFID 2544..2561
/evidence="ECO:0000250"
DISULFID 2566..2578
/evidence="ECO:0000250"
DISULFID 2573..2591
/evidence="ECO:0000250"
DISULFID 2585..2600
/evidence="ECO:0000250"
DISULFID 2605..2617
/evidence="ECO:0000250"
DISULFID 2612..2630
/evidence="ECO:0000250"
DISULFID 2624..2639
/evidence="ECO:0000250"
DISULFID 2644..2666
/evidence="ECO:0000250"
DISULFID 2660..2679
/evidence="ECO:0000250"
DISULFID 2673..2688
/evidence="ECO:0000250"
DISULFID 2696..2708
/evidence="ECO:0000250"
DISULFID 2703..2721
/evidence="ECO:0000250"
DISULFID 2715..2730
/evidence="ECO:0000250"
DISULFID 2734..2746
/evidence="ECO:0000250"
DISULFID 2741..2759
/evidence="ECO:0000250"
DISULFID 2753..2769
/evidence="ECO:0000250"
DISULFID 2774..2787
/evidence="ECO:0000250"
DISULFID 2781..2800
/evidence="ECO:0000250"
DISULFID 2794..2812
/evidence="ECO:0000250"
DISULFID 2818..2830
/evidence="ECO:0000250"
DISULFID 2825..2843
/evidence="ECO:0000250"
DISULFID 2837..2853
/evidence="ECO:0000250"
DISULFID 2858..2870
/evidence="ECO:0000250"
DISULFID 2865..2884
/evidence="ECO:0000250"
DISULFID 2878..2897
/evidence="ECO:0000250"
DISULFID 2904..2917
/evidence="ECO:0000250"
DISULFID 2912..2930
/evidence="ECO:0000250"
DISULFID 2924..2939
/evidence="ECO:0000250"
DISULFID 2944..2956
/evidence="ECO:0000250"
DISULFID 2952..2965
/evidence="ECO:0000250"
DISULFID 2967..2980
/evidence="ECO:0000250"
DISULFID 2986..2996
/evidence="ECO:0000250"
DISULFID 2992..3005
/evidence="ECO:0000250"
DISULFID 3007..3021
/evidence="ECO:0000250"
DISULFID 3294..3305
/evidence="ECO:0000250"
DISULFID 3301..3315
/evidence="ECO:0000250"
DISULFID 3317..3330
/evidence="ECO:0000250"
DISULFID 3334..3346
/evidence="ECO:0000250"
DISULFID 3341..3359
/evidence="ECO:0000250"
DISULFID 3353..3369
/evidence="ECO:0000250"
DISULFID 3374..3386
/evidence="ECO:0000250"
DISULFID 3381..3399
/evidence="ECO:0000250"
DISULFID 3393..3408
/evidence="ECO:0000250"
DISULFID 3413..3426
/evidence="ECO:0000250"
DISULFID 3420..3439
/evidence="ECO:0000250"
DISULFID 3433..3448
/evidence="ECO:0000250"
DISULFID 3453..3466
/evidence="ECO:0000250"
DISULFID 3460..3479
/evidence="ECO:0000250"
DISULFID 3473..3489
/evidence="ECO:0000250"
DISULFID 3494..3507
/evidence="ECO:0000250"
DISULFID 3501..3520
/evidence="ECO:0000250"
DISULFID 3514..3531
/evidence="ECO:0000250"
DISULFID 3536..3548
/evidence="ECO:0000250"
DISULFID 3543..3561
/evidence="ECO:0000250"
DISULFID 3555..3570
/evidence="ECO:0000250"
DISULFID 3575..3587
/evidence="ECO:0000250"
DISULFID 3582..3600
/evidence="ECO:0000250"
DISULFID 3594..3609
/evidence="ECO:0000250"
DISULFID 3613..3625
/evidence="ECO:0000250"
DISULFID 3620..3638
/evidence="ECO:0000250"
DISULFID 3632..3647
/evidence="ECO:0000250"
DISULFID 3654..3666
/evidence="ECO:0000250"
DISULFID 3661..3679
/evidence="ECO:0000250"
DISULFID 3673..3690
/evidence="ECO:0000250"
DISULFID 3695..3709
/evidence="ECO:0000250"
DISULFID 3703..3722
/evidence="ECO:0000250"
DISULFID 3716..3731
/evidence="ECO:0000250"
DISULFID 3741..3754
/evidence="ECO:0000250"
DISULFID 3749..3767
/evidence="ECO:0000250"
DISULFID 3761..3776
/evidence="ECO:0000250"
DISULFID 3785..3798
/evidence="ECO:0000250"
DISULFID 3792..3807
/evidence="ECO:0000250"
DISULFID 3809..3822
/evidence="ECO:0000250"
DISULFID 3828..3838
/evidence="ECO:0000250"
DISULFID 3834..3847
/evidence="ECO:0000250"
DISULFID 3849..3860
/evidence="ECO:0000250"
DISULFID 4151..4160
/evidence="ECO:0000250"
DISULFID 4156..4169
/evidence="ECO:0000250"
DISULFID 4171..4182
/evidence="ECO:0000250"
DISULFID 4200..4210
/evidence="ECO:0000250"
DISULFID 4204..4220
/evidence="ECO:0000250"
DISULFID 4222..4231
/evidence="ECO:0000250"
DISULFID 4236..4246
/evidence="ECO:0000250"
DISULFID 4240..4256
/evidence="ECO:0000250"
DISULFID 4258..4267
/evidence="ECO:0000250"
DISULFID 4272..4282
/evidence="ECO:0000250"
DISULFID 4276..4292
/evidence="ECO:0000250"
DISULFID 4294..4303
/evidence="ECO:0000250"
DISULFID 4308..4318
/evidence="ECO:0000250"
DISULFID 4312..4328
/evidence="ECO:0000250"
DISULFID 4330..4339
/evidence="ECO:0000250"
DISULFID 4344..4352
/evidence="ECO:0000250"
DISULFID 4347..4363
/evidence="ECO:0000250"
DISULFID 4365..4374
/evidence="ECO:0000250"
DISULFID 4377..4387
/evidence="ECO:0000250"
DISULFID 4381..4397
/evidence="ECO:0000250"
DISULFID 4399..4408
/evidence="ECO:0000250"
VAR_SEQ 281..292
/note="HVEQMAIDWLTG -> LCVFSKSQQEMG (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_056919"
VAR_SEQ 293..4544
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_056920"
VARIANT 166
/note="N -> D (in dbSNP:rs2306691)"
/id="VAR_021885"
VARIANT 217
/note="A -> V (in dbSNP:rs1800127)"
/id="VAR_014725"
VARIANT 869
/note="E -> K (in a colorectal cancer sample; somatic
mutation; dbSNP:rs1207947902)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035994"
VARIANT 1245
/note="K -> R (in KPA; reduced alpha-2 macroglobulin
receptor activity; reduced protein abundance;
dbSNP:rs483353013)"
/evidence="ECO:0000269|PubMed:26142438"
/id="VAR_077982"
VARIANT 2059
/note="V -> L (in dbSNP:rs2229278)"
/id="VAR_029181"
VARIANT 2080
/note="D -> N (in dbSNP:rs34577247)"
/id="VAR_047525"
VARIANT 2900
/note="Q -> P (in dbSNP:rs7397167)"
/evidence="ECO:0000269|PubMed:3266596,
ECO:0000269|PubMed:9782078, ECO:0000269|Ref.4"
/id="VAR_047526"
VARIANT 3258
/note="H -> Q (found in a patient with severe mental
retardation, seizures, stereotypic behavior, high pain
threshold and sleep disturbances; dbSNP:rs1565750061)"
/evidence="ECO:0000269|PubMed:23033978"
/id="VAR_069388"
VARIANT 3760
/note="R -> H (in a colorectal cancer sample; somatic
mutation; dbSNP:rs569866427)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035995"
VARIANT 4536
/note="E -> G (in dbSNP:rs17357542)"
/id="VAR_047527"
MUTAGEN 4460
/note="T->A: Strongly reduced phosphorylation and loss of
interaction with SHC1; when associated with A-4517; A-4520
and A-4523."
/evidence="ECO:0000269|PubMed:15272003"
MUTAGEN 4470..4473
/note="NPTY->APTA: No effect on tyrosine phosphorylation."
/evidence="ECO:0000269|PubMed:11854294"
MUTAGEN 4470
/note="N->A: No effect on interaction with GULP1."
/evidence="ECO:0000269|PubMed:11729193"
MUTAGEN 4472
/note="T->A: No detectable effect on phosphorylation."
/evidence="ECO:0000269|PubMed:15272003"
MUTAGEN 4504..4507
/note="NPVY->APVA: Loss of tyrosine phosphorylation.
Abolishes interaction with SHC1 and GULP1."
/evidence="ECO:0000269|PubMed:11854294"
MUTAGEN 4504
/note="N->A: Loss of interaction with GULP1."
/evidence="ECO:0000269|PubMed:11729193"
MUTAGEN 4517
/note="S->A: Strongly reduced phosphorylation and loss of
interaction with SHC1; when associated with A-4460; A-4520
and A-4523."
/evidence="ECO:0000269|PubMed:15272003"
MUTAGEN 4520
/note="S->A: Strongly reduced phosphorylation and loss of
interaction with SHC1; when associated with A-4460; A-4517
and A-4523."
/evidence="ECO:0000269|PubMed:15272003"
MUTAGEN 4523
/note="S->A: Strongly reduced phosphorylation and loss of
interaction with SHC1; when associated with A-4460; A-4517
and A-4520."
/evidence="ECO:0000269|PubMed:15272003"
CONFLICT 685
/note="D -> G (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 1743
/note="G -> S (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 2871..2872
/note="LS -> IA (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 3036
/note="R -> M (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
TURN 853..857
/evidence="ECO:0007744|PDB:1D2L"
STRAND 859..861
/evidence="ECO:0007744|PDB:1D2L"
TURN 862..864
/evidence="ECO:0007744|PDB:1D2L"
STRAND 865..867
/evidence="ECO:0007744|PDB:1D2L"
HELIX 869..871
/evidence="ECO:0007744|PDB:1D2L"
STRAND 874..876
/evidence="ECO:0007744|PDB:1D2L"
TURN 878..881
/evidence="ECO:0007744|PDB:1D2L"
STRAND 934..936
/evidence="ECO:0007744|PDB:2FYJ"
STRAND 940..942
/evidence="ECO:0007744|PDB:2FYJ"
TURN 944..946
/evidence="ECO:0007744|PDB:2FYL"
STRAND 948..950
/evidence="ECO:0007744|PDB:2FYJ"
STRAND 953..956
/evidence="ECO:0007744|PDB:2FYJ"
STRAND 958..961
/evidence="ECO:0007744|PDB:2FYJ"
TURN 964..968
/evidence="ECO:0007744|PDB:2FYJ"
TURN 969..971
/evidence="ECO:0007744|PDB:2FYL"
STRAND 974..976
/evidence="ECO:0007744|PDB:2FYJ"
STRAND 978..983
/evidence="ECO:0007744|PDB:2FYJ"
TURN 985..987
/evidence="ECO:0007744|PDB:2FYL"
STRAND 989..991
/evidence="ECO:0007744|PDB:2FYJ"
STRAND 995..1000
/evidence="ECO:0007744|PDB:2FYJ"
STRAND 1003..1007
/evidence="ECO:0007744|PDB:2FYJ"
STRAND 1009..1011
/evidence="ECO:0007744|PDB:2FYL"
STRAND 1013..1015
/evidence="ECO:0007744|PDB:1J8E"
STRAND 1019..1021
/evidence="ECO:0007744|PDB:1J8E"
STRAND 1027..1029
/evidence="ECO:0007744|PDB:1J8E"
HELIX 1030..1032
/evidence="ECO:0007744|PDB:1J8E"
STRAND 1035..1037
/evidence="ECO:0007744|PDB:1J8E"
STRAND 1040..1043
/evidence="ECO:0007744|PDB:1J8E"
HELIX 1044..1046
/evidence="ECO:0007744|PDB:1J8E"
HELIX 1048..1051
/evidence="ECO:0007744|PDB:1J8E"
TURN 1070..1072
/evidence="ECO:0007744|PDB:1CR8"
HELIX 1078..1080
/evidence="ECO:0007744|PDB:1CR8"
STRAND 1081..1085
/evidence="ECO:0007744|PDB:1CR8"
STRAND 1088..1091
/evidence="ECO:0007744|PDB:1CR8"
TURN 1092..1096
/evidence="ECO:0007744|PDB:1CR8"
STRAND 2778..2781
/evidence="ECO:0007744|PDB:2KNX"
TURN 2782..2785
/evidence="ECO:0007744|PDB:2KNX"
STRAND 2786..2789
/evidence="ECO:0007744|PDB:2KNX"
TURN 2790..2794
/evidence="ECO:0007744|PDB:2KNX"
STRAND 2795..2797
/evidence="ECO:0007744|PDB:2KNX"
STRAND 2800..2803
/evidence="ECO:0007744|PDB:2KNY"
HELIX 2804..2806
/evidence="ECO:0007744|PDB:2KNX"
HELIX 2808..2810
/evidence="ECO:0007744|PDB:2KNX"
STRAND 2813..2816
/evidence="ECO:0007744|PDB:2KNY"
SEQUENCE 4544 AA; 504606 MW; 5A11CC02FAB127BE CRC64;
MLTPPLLLLL PLLSALVAAA IDAPKTCSPK QFACRDQITC ISKGWRCDGE RDCPDGSDEA
PEICPQSKAQ RCQPNEHNCL GTELCVPMSR LCNGVQDCMD GSDEGPHCRE LQGNCSRLGC
QHHCVPTLDG PTCYCNSSFQ LQADGKTCKD FDECSVYGTC SQLCTNTDGS FICGCVEGYL
LQPDNRSCKA KNEPVDRPPV LLIANSQNIL ATYLSGAQVS TITPTSTRQT TAMDFSYANE
TVCWVHVGDS AAQTQLKCAR MPGLKGFVDE HTINISLSLH HVEQMAIDWL TGNFYFVDDI
DDRIFVCNRN GDTCVTLLDL ELYNPKGIAL DPAMGKVFFT DYGQIPKVER CDMDGQNRTK
LVDSKIVFPH GITLDLVSRL VYWADAYLDY IEVVDYEGKG RQTIIQGILI EHLYGLTVFE
NYLYATNSDN ANAQQKTSVI RVNRFNSTEY QVVTRVDKGG ALHIYHQRRQ PRVRSHACEN
DQYGKPGGCS DICLLANSHK ARTCRCRSGF SLGSDGKSCK KPEHELFLVY GKGRPGIIRG
MDMGAKVPDE HMIPIENLMN PRALDFHAET GFIYFADTTS YLIGRQKIDG TERETILKDG
IHNVEGVAVD WMGDNLYWTD DGPKKTISVA RLEKAAQTRK TLIEGKMTHP RAIVVDPLNG
WMYWTDWEED PKDSRRGRLE RAWMDGSHRD IFVTSKTVLW PNGLSLDIPA GRLYWVDAFY
DRIETILLNG TDRKIVYEGP ELNHAFGLCH HGNYLFWTEY RSGSVYRLER GVGGAPPTVT
LLRSERPPIF EIRMYDAQQQ QVGTNKCRVN NGGCSSLCLA TPGSRQCACA EDQVLDADGV
TCLANPSYVP PPQCQPGEFA CANSRCIQER WKCDGDNDCL DNSDEAPALC HQHTCPSDRF
KCENNRCIPN RWLCDGDNDC GNSEDESNAT CSARTCPPNQ FSCASGRCIP ISWTCDLDDD
CGDRSDESAS CAYPTCFPLT QFTCNNGRCI NINWRCDNDN DCGDNSDEAG CSHSCSSTQF
KCNSGRCIPE HWTCDGDNDC GDYSDETHAN CTNQATRPPG GCHTDEFQCR LDGLCIPLRW
RCDGDTDCMD SSDEKSCEGV THVCDPSVKF GCKDSARCIS KAWVCDGDND CEDNSDEENC
ESLACRPPSH PCANNTSVCL PPDKLCDGND DCGDGSDEGE LCDQCSLNNG GCSHNCSVAP
GEGIVCSCPL GMELGPDNHT CQIQSYCAKH LKCSQKCDQN KFSVKCSCYE GWVLEPDGES
CRSLDPFKPF IIFSNRHEIR RIDLHKGDYS VLVPGLRNTI ALDFHLSQSA LYWTDVVEDK
IYRGKLLDNG ALTSFEVVIQ YGLATPEGLA VDWIAGNIYW VESNLDQIEV AKLDGTLRTT
LLAGDIEHPR AIALDPRDGI LFWTDWDASL PRIEAASMSG AGRRTVHRET GSGGWPNGLT
VDYLEKRILW IDARSDAIYS ARYDGSGHME VLRGHEFLSH PFAVTLYGGE VYWTDWRTNT
LAKANKWTGH NVTVVQRTNT QPFDLQVYHP SRQPMAPNPC EANGGQGPCS HLCLINYNRT
VSCACPHLMK LHKDNTTCYE FKKFLLYARQ MEIRGVDLDA PYYNYIISFT VPDIDNVTVL
DYDAREQRVY WSDVRTQAIK RAFINGTGVE TVVSADLPNA HGLAVDWVSR NLFWTSYDTN
KKQINVARLD GSFKNAVVQG LEQPHGLVVH PLRGKLYWTD GDNISMANMD GSNRTLLFSG
QKGPVGLAID FPESKLYWIS SGNHTINRCN LDGSGLEVID AMRSQLGKAT ALAIMGDKLW
WADQVSEKMG TCSKADGSGS VVLRNSTTLV MHMKVYDESI QLDHKGTNPC SVNNGDCSQL
CLPTSETTRS CMCTAGYSLR SGQQACEGVG SFLLYSVHEG IRGIPLDPND KSDALVPVSG
TSLAVGIDFH AENDTIYWVD MGLSTISRAK RDQTWREDVV TNGIGRVEGI AVDWIAGNIY
WTDQGFDVIE VARLNGSFRY VVISQGLDKP RAITVHPEKG YLFWTEWGQY PRIERSRLDG
TERVVLVNVS ISWPNGISVD YQDGKLYWCD ARTDKIERID LETGENREVV LSSNNMDMFS
VSVFEDFIYW SDRTHANGSI KRGSKDNATD SVPLRTGIGV QLKDIKVFNR DRQKGTNVCA
VANGGCQQLC LYRGRGQRAC ACAHGMLAED GASCREYAGY LLYSERTILK SIHLSDERNL
NAPVQPFEDP EHMKNVIALA FDYRAGTSPG TPNRIFFSDI HFGNIQQIND DGSRRITIVE
NVGSVEGLAY HRGWDTLYWT SYTTSTITRH TVDQTRPGAF ERETVITMSG DDHPRAFVLD
ECQNLMFWTN WNEQHPSIMR AALSGANVLT LIEKDIRTPN GLAIDHRAEK LYFSDATLDK
IERCEYDGSH RYVILKSEPV HPFGLAVYGE HIFWTDWVRR AVQRANKHVG SNMKLLRVDI
PQQPMGIIAV ANDTNSCELS PCRINNGGCQ DLCLLTHQGH VNCSCRGGRI LQDDLTCRAV
NSSCRAQDEF ECANGECINF SLTCDGVPHC KDKSDEKPSY CNSRRCKKTF RQCSNGRCVS
NMLWCNGADD CGDGSDEIPC NKTACGVGEF RCRDGTCIGN SSRCNQFVDC EDASDEMNCS
ATDCSSYFRL GVKGVLFQPC ERTSLCYAPS WVCDGANDCG DYSDERDCPG VKRPRCPLNY
FACPSGRCIP MSWTCDKEDD CEHGEDETHC NKFCSEAQFE CQNHRCISKQ WLCDGSDDCG
DGSDEAAHCE GKTCGPSSFS CPGTHVCVPE RWLCDGDKDC ADGADESIAA GCLYNSTCDD
REFMCQNRQC IPKHFVCDHD RDCADGSDES PECEYPTCGP SEFRCANGRC LSSRQWECDG
ENDCHDQSDE APKNPHCTSQ EHKCNASSQF LCSSGRCVAE ALLCNGQDDC GDSSDERGCH
INECLSRKLS GCSQDCEDLK IGFKCRCRPG FRLKDDGRTC ADVDECSTTF PCSQRCINTH
GSYKCLCVEG YAPRGGDPHS CKAVTDEEPF LIFANRYYLR KLNLDGSNYT LLKQGLNNAV
ALDFDYREQM IYWTDVTTQG SMIRRMHLNG SNVQVLHRTG LSNPDGLAVD WVGGNLYWCD
KGRDTIEVSK LNGAYRTVLV SSGLREPRAL VVDVQNGYLY WTDWGDHSLI GRIGMDGSSR
SVIVDTKITW PNGLTLDYVT ERIYWADARE DYIEFASLDG SNRHVVLSQD IPHIFALTLF
EDYVYWTDWE TKSINRAHKT TGTNKTLLIS TLHRPMDLHV FHALRQPDVP NHPCKVNNGG
CSNLCLLSPG GGHKCACPTN FYLGSDGRTC VSNCTASQFV CKNDKCIPFW WKCDTEDDCG
DHSDEPPDCP EFKCRPGQFQ CSTGICTNPA FICDGDNDCQ DNSDEANCDI HVCLPSQFKC
TNTNRCIPGI FRCNGQDNCG DGEDERDCPE VTCAPNQFQC SITKRCIPRV WVCDRDNDCV
DGSDEPANCT QMTCGVDEFR CKDSGRCIPA RWKCDGEDDC GDGSDEPKEE CDERTCEPYQ
FRCKNNRCVP GRWQCDYDND CGDNSDEESC TPRPCSESEF SCANGRCIAG RWKCDGDHDC
ADGSDEKDCT PRCDMDQFQC KSGHCIPLRW RCDADADCMD GSDEEACGTG VRTCPLDEFQ
CNNTLCKPLA WKCDGEDDCG DNSDENPEEC ARFVCPPNRP FRCKNDRVCL WIGRQCDGTD
NCGDGTDEED CEPPTAHTTH CKDKKEFLCR NQRCLSSSLR CNMFDDCGDG SDEEDCSIDP
KLTSCATNAS ICGDEARCVR TEKAAYCACR SGFHTVPGQP GCQDINECLR FGTCSQLCNN
TKGGHLCSCA RNFMKTHNTC KAEGSEYQVL YIADDNEIRS LFPGHPHSAY EQAFQGDESV
RIDAMDVHVK AGRVYWTNWH TGTISYRSLP PAAPPTTSNR HRRQIDRGVT HLNISGLKMP
RGIAIDWVAG NVYWTDSGRD VIEVAQMKGE NRKTLISGMI DEPHAIVVDP LRGTMYWSDW
GNHPKIETAA MDGTLRETLV QDNIQWPTGL AVDYHNERLY WADAKLSVIG SIRLNGTDPI
VAADSKRGLS HPFSIDVFED YIYGVTYINN RVFKIHKFGH SPLVNLTGGL SHASDVVLYH
QHKQPEVTNP CDRKKCEWLC LLSPSGPVCT CPNGKRLDNG TCVPVPSPTP PPDAPRPGTC
NLQCFNGGSC FLNARRQPKC RCQPRYTGDK CELDQCWEHC RNGGTCAASP SGMPTCRCPT
GFTGPKCTQQ VCAGYCANNS TCTVNQGNQP QCRCLPGFLG DRCQYRQCSG YCENFGTCQM
AADGSRQCRC TAYFEGSRCE VNKCSRCLEG ACVVNKQSGD VTCNCTDGRV APSCLTCVGH
CSNGGSCTMN SKMMPECQCP PHMTGPRCEE HVFSQQQPGH IASILIPLLL LLLLVLVAGV
VFWYKRRVQG AKGFQHQRMT NGAMNVEIGN PTYKMYEGGE PDDVGGLLDA DFALDPDKPT
NFTNPVYATL YMGGHGSRHS LASTDEKREL LGRGPEDEIG DPLA


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Related Genes :
[LRP1 A2MR APR] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (Apolipoprotein E receptor) (APOER) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[Lrp1 A2mr] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[Lrp1] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[Lrp8 Apoer2] Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2)
[LRP8 APOER2] Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2)
[LRP5 LR3 LRP7] Low-density lipoprotein receptor-related protein 5 (LRP-5) (Low-density lipoprotein receptor-related protein 7) (LRP-7)
[Lrp5 Lr3 Lrp7] Low-density lipoprotein receptor-related protein 5 (LRP-5) (Low-density lipoprotein receptor-related protein 7) (LRP-7)
[LRP3] Low-density lipoprotein receptor-related protein 3 (LRP-3) (105 kDa low-density lipoprotein receptor-related protein) (hLRp105)
[Lrp2] Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)
[SORL1 C11orf32] Sortilin-related receptor (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (SorLA)
[LRP6] Low-density lipoprotein receptor-related protein 6 (LRP-6)
[Lrp6] Low-density lipoprotein receptor-related protein 6 (LRP-6)
[LRP12 ST7] Low-density lipoprotein receptor-related protein 12 (LDLR-related protein 12) (LRP-12) (Suppressor of tumorigenicity 7 protein)
[LRP10 MSTP087 SP220 UNQ389/PRO724] Low-density lipoprotein receptor-related protein 10 (LRP-10)
[Corin Crn Lrp4] Atrial natriuretic peptide-converting enzyme (EC 3.4.21.-) (Corin) (Low density lipoprotein receptor-related protein 4) (Pro-ANP-converting enzyme) [Cleaved into: Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Atrial natriuretic peptide-converting enzyme, activated protease fragment; Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment]
[Sorl1] Sortilin-related receptor (Gp250) (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (mSorLA)
[SORL1] Sortilin-related receptor (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (SorLA)
[Sorl1] Sortilin-related receptor (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (Sorting protein-related receptor containing LDLR class A repeats) (SorLA)
[Lrp10 Lrp9] Low-density lipoprotein receptor-related protein 10 (LRP-10)
[LDLR] Low-density lipoprotein receptor (LDL receptor)
[VLDLR] Very low-density lipoprotein receptor (VLDL receptor) (VLDL-R)
[LRP8 LR8B] Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2) (Protein LR8B)
[Lrp3 Lrp105] Low-density lipoprotein receptor-related protein 3 (LRP-3) (105 kDa low-density lipoprotein receptor-related protein) (rLRp105)
[SORL1] Sortilin-related receptor (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (SorLA) (Fragment)
[RPSA LAMBR LAMR1] 40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Colon carcinoma laminin-binding protein) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (Multidrug resistance-associated protein MGr1-Ag) (NEM/1CHD4) (Small ribosomal subunit protein uS2)
[Lrp12] Low-density lipoprotein receptor-related protein 12 (LRP-12)
[PTPRJ DEP1] Receptor-type tyrosine-protein phosphatase eta (Protein-tyrosine phosphatase eta) (R-PTP-eta) (EC 3.1.3.48) (Density-enhanced phosphatase 1) (DEP-1) (HPTP eta) (Protein-tyrosine phosphatase receptor type J) (R-PTP-J) (CD antigen CD148)
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[Rpsa Lamr1 P40-8] 40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37 kDa oncofetal antigen) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (OFA/iLRP)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)

Bibliography :