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Database: UniProt
Entry: Q07954
LinkDB: Q07954
Original site: Q07954 
ID   LRP1_HUMAN              Reviewed;        4544 AA.
AC   Q07954; Q2PP12; Q86SW0; Q8IVG8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   13-FEB-2019, entry version 210.
DE   RecName: Full=Prolow-density lipoprotein receptor-related protein 1;
DE            Short=LRP-1;
DE   AltName: Full=Alpha-2-macroglobulin receptor {ECO:0000303|PubMed:26142438};
DE            Short=A2MR;
DE   AltName: Full=Apolipoprotein E receptor;
DE            Short=APOER;
DE   AltName: CD_antigen=CD91;
DE   Contains:
DE     RecName: Full=Low-density lipoprotein receptor-related protein 1 85 kDa subunit;
DE              Short=LRP-85;
DE   Contains:
DE     RecName: Full=Low-density lipoprotein receptor-related protein 1 515 kDa subunit;
DE              Short=LRP-515;
DE   Contains:
DE     RecName: Full=Low-density lipoprotein receptor-related protein 1 intracellular domain;
DE              Short=LRPICD;
DE   Flags: Precursor;
GN   Name=LRP1; Synonyms=A2MR, APR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-2900.
RC   TISSUE=Liver;
RX   PubMed=3266596;
RA   Herz J., Hamann U., Rogne S., Myklebost O., Gausepohl H.,
RA   Stanley K.K.;
RT   "Surface location and high affinity for calcium of a 500-kd liver
RT   membrane protein closely related to the LDL-receptor suggest a
RT   physiological role as lipoprotein receptor.";
RL   EMBO J. 7:4119-4127(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7534747; DOI=10.1006/geno.1994.1584;
RA   Van Leuven F., Stas L., Hilliker C., Lorent K., Umans L., Serneels L.,
RA   Overbergh L., Torrekens S., Moechars D., De Strooper B.,
RA   Van den Berghe H.;
RT   "Structure of the gene (LRP1) coding for the human alpha 2-
RT   macroglobulin receptor lipoprotein receptor-related protein.";
RL   Genomics 24:78-89(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-2900.
RX   PubMed=9782078; DOI=10.1006/geno.1998.5408;
RA   Van Leuven F., Stas L., Thiry E., Nelissen B., Miyake Y.;
RT   "Strategy to sequence the 89 exons of the human LRP1 gene coding for
RT   the lipoprotein receptor related protein: identification of one
RT   expressed mutation among 48 polymorphisms.";
RL   Genomics 52:138-144(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-2900.
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX   PubMed=2597675;
RA   Kutt H., Herz J., Stanley K.K.;
RT   "Structure of the low-density lipoprotein receptor-related protein
RT   (LRP) promoter.";
RL   Biochim. Biophys. Acta 1009:229-236(1989).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC   TISSUE=Blood;
RA   Glaeser C.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PROTEIN SEQUENCE OF 150-166; 234-252; 685-695; 902-916; 1096-1109;
RP   1743-1756; 2863-2874; 2949-2960; 3023-3039 AND 3277-3291.
RC   TISSUE=Placenta;
RX   PubMed=1698775;
RA   Strickland D.K., Ashcom J.D., Williams S., Burgess W.H.,
RA   Migliorini M., Argraves W.S.;
RT   "Sequence identity between the alpha 2-macroglobulin receptor and low
RT   density lipoprotein receptor-related protein suggests that this
RT   molecule is a multifunctional receptor.";
RL   J. Biol. Chem. 265:17401-17404(1990).
RN   [10]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=2112085;
RA   Herz J., Kowal R.C., Goldstein J.L., Brown M.S.;
RT   "Proteolytic processing of the 600 kd low density lipoprotein
RT   receptor-related protein (LRP) occurs in a trans-Golgi compartment.";
RL   EMBO J. 9:1769-1776(1990).
RN   [11]
RP   FUNCTION.
RX   PubMed=1702392; DOI=10.1016/0014-5793(90)80530-V;
RA   Kristensen T., Moestrup S.K., Gliemann J., Bendtsen L., Sand O.,
RA   Sottrup-Jensen L.;
RT   "Evidence that the newly cloned low-density-lipoprotein receptor
RT   related protein (LRP) is the alpha 2-macroglobulin receptor.";
RL   FEBS Lett. 276:151-155(1990).
RN   [12]
RP   FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
RX   PubMed=1618748;
RA   Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J.,
RA   Strickland D.K., Saelinger C.B.;
RT   "The alpha 2-macroglobulin receptor/low density lipoprotein receptor-
RT   related protein binds and internalizes Pseudomonas exotoxin A.";
RL   J. Biol. Chem. 267:12420-12423(1992).
RN   [13]
RP   INTERACTION WITH GULP1, AND MUTAGENESIS OF ASN-4470 AND ASN-4504.
RX   PubMed=11729193; DOI=10.1074/jbc.M109336200;
RA   Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G.,
RA   Henson P.M., Ravichandran K.S.;
RT   "Interaction of CED-6/GULP, an adapter protein involved in engulfment
RT   of apoptotic cells with CED-1 and CD91/low density lipoprotein
RT   receptor-related protein (LRP).";
RL   J. Biol. Chem. 277:11772-11779(2002).
RN   [14]
RP   PHOSPHORYLATION AT TYR-4507, MUTAGENESIS OF 4470-ASN--TYR-4473 AND
RP   4504-ASN--TYR-4507, AND INTERACTION WITH PDGF.
RX   PubMed=11854294; DOI=10.1074/jbc.M200427200;
RA   Loukinova E., Ranganathan S., Kuznetsov S., Gorlatova N.,
RA   Migliorini M.M., Loukinov D., Ulery P.G., Mikhailenko I.,
RA   Lawrence D.A., Strickland D.K.;
RT   "Platelet-derived growth factor (PDGF)-induced tyrosine
RT   phosphorylation of the low density lipoprotein receptor-related
RT   protein (LRP). Evidence for integrated co-receptor function between
RT   LRP and the PDGF.";
RL   J. Biol. Chem. 277:15499-15506(2002).
RN   [15]
RP   FUNCTION, AND PROTEOLYTIC PROCESSING.
RX   PubMed=11907044; DOI=10.1074/jbc.M201979200;
RA   May P., Reddy Y.K., Herz J.;
RT   "Proteolytic processing of low density lipoprotein receptor-related
RT   protein mediates regulated release of its intracellular domain.";
RL   J. Biol. Chem. 277:18736-18743(2002).
RN   [16]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12888553; DOI=10.1074/jbc.M306403200;
RA   Kinoshita A., Shah T., Tangredi M.M., Strickland D.K., Hyman B.T.;
RT   "The intracellular domain of the low density lipoprotein receptor-
RT   related protein modulates transactivation mediated by amyloid
RT   precursor protein and Fe65.";
RL   J. Biol. Chem. 278:41182-41188(2003).
RN   [17]
RP   FUNCTION.
RX   PubMed=12713657; DOI=10.1034/j.1600-0854.2003.00086_4_5.x;
RA   May P., Herz J.;
RT   "LDL receptor-related proteins in neurodevelopment.";
RL   Traffic 4:291-301(2003).
RN   [18]
RP   PHOSPHORYLATION AT THR-4460; SER-4517; SER-4520 AND SER-4523,
RP   MUTAGENESIS OF THR-4460; THR-4472; SER-4517; SER-4520 AND SER-4523,
RP   AND INTERACTION WITH SHC1; GULP1 AND DAB1.
RX   PubMed=15272003; DOI=10.1074/jbc.M407592200;
RA   Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F.,
RA   Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.;
RT   "Serine and threonine phosphorylation of the low density lipoprotein
RT   receptor-related protein by protein kinase Calpha regulates
RT   endocytosis and association with adaptor molecules.";
RL   J. Biol. Chem. 279:40536-40544(2004).
RN   [19]
RP   INTERACTION WITH SNX17.
RX   PubMed=15769472; DOI=10.1016/j.jmb.2005.02.004;
RA   Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V.,
RA   Schreckenberger S., Hahn H., Bohnensack R.;
RT   "Functions of sorting nexin 17 domains and recognition motif for P-
RT   selectin trafficking.";
RL   J. Mol. Biol. 347:813-825(2005).
RN   [20]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-2127 AND
RP   ASN-3048.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [21]
RP   IDENTIFICATION IN A COMPLEX WITH CUBN AND PID1, AND INTERACTION WITH
RP   CUBN AND PID1.
RX   PubMed=17124247; DOI=10.1074/mcp.M600289-MCP200;
RA   Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C.,
RA   Scaloni A., Napolitano M., Russo T., Zambrano N.;
RT   "Identification of the ligands of protein interaction domains through
RT   a functional approach.";
RL   Mol. Cell. Proteomics 6:333-345(2007).
RN   [22]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-1511;
RP   ASN-1575; ASN-1616; ASN-1645; ASN-1763; ASN-2127; ASN-2815; ASN-3048;
RP   ASN-3089; ASN-3488; ASN-3788; ASN-3953; ASN-4075 AND ASN-4125.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [23]
RP   GLYCOSYLATION AT ASN-729 AND ASN-1511.
RX   PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA   Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA   Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core
RT   fucosylated glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4520, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [26]
RP   STRUCTURE BY NMR OF 1059-1100 IN COMPLEX WITH CALCIUM IONS, AND
RP   DISULFIDE BONDS.
RX   PubMed=10318830; DOI=10.1074/jbc.274.20.14130;
RA   Huang W., Dolmer K., Gettins P.G.W.;
RT   "NMR solution structure of complement-like repeat CR8 from the low
RT   density lipoprotein receptor-related protein.";
RL   J. Biol. Chem. 274:14130-14136(1999).
RN   [27]
RP   STRUCTURE BY NMR OF 851-893 IN COMPLEX WITH CALCIUM IONS, AND
RP   DISULFIDE BONDS.
RX   PubMed=10652313; DOI=10.1074/jbc.275.5.3264;
RA   Dolmer K., Huang W., Gettins P.G.W.;
RT   "NMR solution structure of complement-like repeat CR3 from the low
RT   density lipoprotein receptor-related protein. Evidence for specific
RT   binding to the receptor binding domain of human alpha(2)-
RT   macroglobulin.";
RL   J. Biol. Chem. 275:3264-3269(2000).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1012-1054 IN COMPLEX WITH
RP   CALCIUM IONS, AND DISULFIDE BONDS.
RX   PubMed=11735395; DOI=10.1021/bi015688m;
RA   Simonovic M., Dolmer K., Huang W., Strickland D.K., Volz K.,
RA   Gettins P.G.;
RT   "Calcium coordination and pH dependence of the calcium affinity of
RT   ligand-binding repeat CR7 from the LRP. Comparison with related
RT   domains from the LRP and the LDL receptor.";
RL   Biochemistry 40:15127-15134(2001).
RN   [29]
RP   STRUCTURE BY NMR OF 932-1013 IN COMPLEX WITH LRPAP1 AND CALCIUM IONS,
RP   AND DISULFIDE BONDS.
RX   PubMed=16938309; DOI=10.1016/j.jmb.2006.07.013;
RA   Jensen G.A., Andersen O.M.J.J., Bonvin A.M., Bjerrum-Bohr I.,
RA   Etzerodt M., Thoegersen H.C., O'Shea C., Poulsen F.M., Kragelund B.B.;
RT   "Binding site structure of one LRP-RAP complex: implications for a
RT   common ligand-receptor binding motif.";
RL   J. Mol. Biol. 362:700-716(2006).
RN   [30]
RP   VARIANTS [LARGE SCALE ANALYSIS] LYS-869 AND HIS-3760.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [31]
RP   VARIANT GLN-3258.
RX   PubMed=23033978; DOI=10.1056/NEJMoa1206524;
RA   de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA   Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
RA   Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA   Brunner H.G., Veltman J.A., Vissers L.E.;
RT   "Diagnostic exome sequencing in persons with severe intellectual
RT   disability.";
RL   N. Engl. J. Med. 367:1921-1929(2012).
RN   [32]
RP   VARIANT KPA ARG-1245, CHARACTERIZATION OF VARIANT KPA ARG-1245,
RP   FUNCTION, AND INVOLVEMENT IN KPA.
RX   PubMed=26142438; DOI=10.1136/jmedgenet-2014-102931;
RA   Klar J., Schuster J., Khan T.N., Jameel M., Maebert K., Forsberg L.,
RA   Baig S.A., Baig S.M., Dahl N.;
RT   "Whole exome sequencing identifies LRP1 as a pathogenic gene in
RT   autosomal recessive keratosis pilaris atrophicans.";
RL   J. Med. Genet. 52:599-606(2015).
CC   -!- FUNCTION: Endocytic receptor involved in endocytosis and in
CC       phagocytosis of apoptotic cells. Required for early embryonic
CC       development. Involved in cellular lipid homeostasis. Involved in
CC       the plasma clearance of chylomicron remnants and activated LRPAP1
CC       (alpha 2-macroglobulin), as well as the local metabolism of
CC       complexes between plasminogen activators and their endogenous
CC       inhibitors. May modulate cellular events, such as APP metabolism,
CC       kinase-dependent intracellular signaling, neuronal calcium
CC       signaling as well as neurotransmission (PubMed:11907044,
CC       PubMed:12888553, PubMed:12713657). Acts as an alpha-2-
CC       macroglobulin receptor (PubMed:26142438).
CC       {ECO:0000269|PubMed:11907044, ECO:0000269|PubMed:12713657,
CC       ECO:0000269|PubMed:12888553, ECO:0000269|PubMed:26142438}.
CC   -!- FUNCTION: (Microbial infection) Functions as a receptor for
CC       Pseudomonas aeruginosa exotoxin A. {ECO:0000269|PubMed:1618748}.
CC   -!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit
CC       and a non-covalently attached 515-kDa N-terminal subunit.
CC       Intracellular domain interacts with MAFB (By similarity). Found in
CC       a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17,
CC       PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with
CC       SHC1, GULP1 and DAB1. Interacts with LRPAP1. Can weakly interact
CC       (via NPXY motif) with DAB2 (via PID domain); the interaction is
CC       enhanced by tyrosine phosphorylation of the NPXY motif. Interacts
CC       with bacterial exotoxins. {ECO:0000250,
CC       ECO:0000269|PubMed:10318830, ECO:0000269|PubMed:10652313,
CC       ECO:0000269|PubMed:11729193, ECO:0000269|PubMed:11735395,
CC       ECO:0000269|PubMed:11854294, ECO:0000269|PubMed:15272003,
CC       ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:16938309,
CC       ECO:0000269|PubMed:17124247}.
CC   -!- INTERACTION:
CC       O00213:APBB1; NbExp=3; IntAct=EBI-1046087, EBI-81694;
CC       P78352:DLG4; NbExp=2; IntAct=EBI-1046087, EBI-80389;
CC       Q15485:FCN2; NbExp=2; IntAct=EBI-1046087, EBI-7468784;
CC       Q12879:GRIN2A; NbExp=2; IntAct=EBI-1046087, EBI-7249937;
CC       Q63722:Jag1 (xeno); NbExp=4; IntAct=EBI-1046087, EBI-4567800;
CC       P11226:MBL2; NbExp=5; IntAct=EBI-1046087, EBI-5325353;
CC       Q03350:Thbs2 (xeno); NbExp=2; IntAct=EBI-1046087, EBI-4567830;
CC   -!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
CC       protein 1 85 kDa subunit: Cell membrane; Single-pass type I
CC       membrane protein. Membrane, coated pit.
CC   -!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
CC       protein 1 515 kDa subunit: Cell membrane; Peripheral membrane
CC       protein; Extracellular side. Membrane, coated pit.
CC   -!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
CC       protein 1 intracellular domain: Cytoplasm. Nucleus. Note=After
CC       cleavage, the intracellular domain (LRPICD) is detected both in
CC       the cytoplasm and in the nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q07954-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q07954-2; Sequence=VSP_056919, VSP_056920;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Most abundant in liver, brain and lung.
CC   -!- PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and
CC       a 515 kDa large extracellular domain (LRP-515) that remains non-
CC       covalently associated. Gamma-secretase-dependent cleavage of LRP-
CC       85 releases the intracellular domain from the membrane.
CC       {ECO:0000269|PubMed:11907044, ECO:0000269|PubMed:2112085}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC   -!- PTM: Phosphorylated on tyrosine residues upon stimulation with
CC       PDGF. Tyrosine phosphorylation promotes interaction with SHC1.
CC   -!- DISEASE: Keratosis pilaris atrophicans (KPA) [MIM:604093]: A group
CC       of rare genodermatoses characterized by keratotic follicular
CC       papules, variable degrees of inflammation, and secondary atrophic
CC       scarring. Most cases are associated with an atopic diathesis and
CC       keratosis pilaris on the extensor extremities. KPA is comprised of
CC       three distinct clinical subtypes: keratosis pilaris atrophicans
CC       faciei, atrophoderma vermiculatum, and keratosis follicularis
CC       spinulosa decalvans. Affected individuals may present with
CC       features overlapping the 3 subtypes.
CC       {ECO:0000269|PubMed:26142438}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
DR   EMBL; X13916; CAA32112.1; -; mRNA.
DR   EMBL; AF058427; AAC64265.1; -; Genomic_DNA.
DR   EMBL; DQ314873; ABC40732.1; -; Genomic_DNA.
DR   EMBL; AC023237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC137628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC137834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC045107; AAH45107.1; -; mRNA.
DR   EMBL; X15424; CAA33464.1; -; Genomic_DNA.
DR   EMBL; Y18524; CAD57169.1; -; Genomic_DNA.
DR   CCDS; CCDS8932.1; -. [Q07954-1]
DR   PIR; S02392; S02392.
DR   RefSeq; NP_002323.2; NM_002332.2. [Q07954-1]
DR   UniGene; Hs.162757; -.
DR   PDB; 1CR8; NMR; -; A=1059-1100.
DR   PDB; 1D2L; NMR; -; A=851-893.
DR   PDB; 1J8E; X-ray; 1.85 A; A=1011-1054.
DR   PDB; 2FYJ; NMR; -; A=932-1013.
DR   PDB; 2FYL; NMR; -; B=932-1013.
DR   PDB; 2KNX; NMR; -; A=2770-2817.
DR   PDB; 2KNY; NMR; -; A=2770-2817.
DR   PDBsum; 1CR8; -.
DR   PDBsum; 1D2L; -.
DR   PDBsum; 1J8E; -.
DR   PDBsum; 2FYJ; -.
DR   PDBsum; 2FYL; -.
DR   PDBsum; 2KNX; -.
DR   PDBsum; 2KNY; -.
DR   ProteinModelPortal; Q07954; -.
DR   SMR; Q07954; -.
DR   BioGrid; 110215; 124.
DR   CORUM; Q07954; -.
DR   DIP; DIP-50613N; -.
DR   ELM; Q07954; -.
DR   IntAct; Q07954; 26.
DR   MINT; Q07954; -.
DR   STRING; 9606.ENSP00000243077; -.
DR   DrugBank; DB00025; Antihemophilic Factor (Recombinant).
DR   DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DR   DrugBank; DB00031; Tenecteplase.
DR   CarbonylDB; Q07954; -.
DR   GlyConnect; 1638; -.
DR   iPTMnet; Q07954; -.
DR   PhosphoSitePlus; Q07954; -.
DR   BioMuta; LRP1; -.
DR   DMDM; 317373384; -.
DR   EPD; Q07954; -.
DR   jPOST; Q07954; -.
DR   MaxQB; Q07954; -.
DR   PaxDb; Q07954; -.
DR   PeptideAtlas; Q07954; -.
DR   PRIDE; Q07954; -.
DR   ProteomicsDB; 58559; -.
DR   Ensembl; ENST00000243077; ENSP00000243077; ENSG00000123384. [Q07954-1]
DR   Ensembl; ENST00000338962; ENSP00000341264; ENSG00000123384. [Q07954-2]
DR   GeneID; 4035; -.
DR   KEGG; hsa:4035; -.
DR   UCSC; uc001snd.4; human. [Q07954-1]
DR   CTD; 4035; -.
DR   DisGeNET; 4035; -.
DR   EuPathDB; HostDB:ENSG00000123384.13; -.
DR   GeneCards; LRP1; -.
DR   HGNC; HGNC:6692; LRP1.
DR   HPA; CAB018621; -.
DR   HPA; HPA004182; -.
DR   HPA; HPA022903; -.
DR   MalaCards; LRP1; -.
DR   MIM; 107770; gene.
DR   MIM; 604093; phenotype.
DR   neXtProt; NX_Q07954; -.
DR   OpenTargets; ENSG00000123384; -.
DR   Orphanet; 79100; Atrophoderma vermiculata.
DR   Orphanet; 2340; Keratosis follicularis spinulosa decalvans.
DR   PharmGKB; PA233; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   eggNOG; ENOG410XP34; LUCA.
DR   GeneTree; ENSGT00940000157899; -.
DR   HOGENOM; HOG000230574; -.
DR   HOVERGEN; HBG066902; -.
DR   InParanoid; Q07954; -.
DR   KO; K04550; -.
DR   OMA; TSKATCD; -.
DR   OrthoDB; 1606at2759; -.
DR   PhylomeDB; Q07954; -.
DR   TreeFam; TF315253; -.
DR   Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SIGNOR; Q07954; -.
DR   ChiTaRS; LRP1; human.
DR   EvolutionaryTrace; Q07954; -.
DR   GeneWiki; LRP1; -.
DR   GenomeRNAi; 4035; -.
DR   PRO; PR:Q07954; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000123384; Expressed in 230 organ(s), highest expression level in thoracic aorta.
DR   ExpressionAtlas; Q07954; baseline and differential.
DR   Genevisible; Q07954; HS.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
DR   GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0032593; C:insulin-responsive compartment; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; NAS:ARUK-UCL.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0098797; C:plasma membrane protein complex; TAS:ARUK-UCL.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0016964; F:alpha-2 macroglobulin receptor activity; IMP:UniProtKB.
DR   GO; GO:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
DR   GO; GO:0034185; F:apolipoprotein binding; IDA:UniProtKB.
DR   GO; GO:0030226; F:apolipoprotein receptor activity; TAS:ARUK-UCL.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0038024; F:cargo receptor activity; IMP:ARUK-UCL.
DR   GO; GO:0032050; F:clathrin heavy chain binding; IPI:ARUK-UCL.
DR   GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR   GO; GO:0043395; F:heparan sulfate proteoglycan binding; TAS:ARUK-UCL.
DR   GO; GO:0070325; F:lipoprotein particle receptor binding; IC:BHF-UCL.
DR   GO; GO:0042954; F:lipoprotein transporter activity; NAS:UniProtKB.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; TAS:ARUK-UCL.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:BHF-UCL.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0097242; P:amyloid-beta clearance; TAS:BHF-UCL.
DR   GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IMP:ARUK-UCL.
DR   GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IGI:ARUK-UCL.
DR   GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0043277; P:apoptotic cell clearance; ISS:BHF-UCL.
DR   GO; GO:0002265; P:astrocyte activation involved in immune response; ISS:ARUK-UCL.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0044242; P:cellular lipid catabolic process; IEA:Ensembl.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR   GO; GO:0061642; P:chemoattraction of axon; IEA:Ensembl.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ARUK-UCL.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
DR   GO; GO:0042953; P:lipoprotein transport; NAS:UniProtKB.
DR   GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISS:BHF-UCL.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0006909; P:phagocytosis; IMP:ARUK-UCL.
DR   GO; GO:1900223; P:positive regulation of amyloid-beta clearance; TAS:ARUK-UCL.
DR   GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IEA:Ensembl.
DR   GO; GO:0010942; P:positive regulation of cell death; IGI:ARUK-UCL.
DR   GO; GO:1904209; P:positive regulation of chemokine (C-C motif) ligand 2 secretion; IEA:Ensembl.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:BHF-UCL.
DR   GO; GO:1904109; P:positive regulation of cholesterol import; IEA:Ensembl.
DR   GO; GO:0048694; P:positive regulation of collateral sprouting of injured axon; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IGI:ARUK-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0032370; P:positive regulation of lipid transport; ISS:BHF-UCL.
DR   GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IMP:ARUK-UCL.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR   GO; GO:0032092; P:positive regulation of protein binding; IGI:ARUK-UCL.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IGI:ARUK-UCL.
DR   GO; GO:1900149; P:positive regulation of Schwann cell migration; IEA:Ensembl.
DR   GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0031623; P:receptor internalization; TAS:ARUK-UCL.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:BHF-UCL.
DR   GO; GO:0032374; P:regulation of cholesterol transport; ISS:BHF-UCL.
DR   GO; GO:0010715; P:regulation of extracellular matrix disassembly; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0032429; P:regulation of phospholipase A2 activity; ISS:BHF-UCL.
DR   GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR   GO; GO:0045056; P:transcytosis; TAS:ARUK-UCL.
DR   CDD; cd00112; LDLa; 31.
DR   Gene3D; 2.120.10.30; -; 8.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR032485; DUF5050.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF16472; DUF5050; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00057; Ldl_recept_a; 29.
DR   Pfam; PF00058; Ldl_recept_b; 12.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 26.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM00192; LDLa; 31.
DR   SMART; SM00135; LY; 35.
DR   SUPFAM; SSF57184; SSF57184; 4.
DR   SUPFAM; SSF57424; SSF57424; 30.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 8.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS01209; LDLRA_1; 27.
DR   PROSITE; PS50068; LDLRA_2; 31.
DR   PROSITE; PS51120; LDLRB; 34.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Calcium;
KW   Cell membrane; Coated pit; Complete proteome; Cytoplasm;
KW   Developmental protein; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Membrane;
KW   Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   4544       Prolow-density lipoprotein receptor-
FT                                related protein 1.
FT                                /FTId=PRO_0000017317.
FT   CHAIN        20  ?3943       Low-density lipoprotein receptor-related
FT                                protein 1 515 kDa subunit.
FT                                /FTId=PRO_0000302750.
FT   CHAIN     ?3944   4544       Low-density lipoprotein receptor-related
FT                                protein 1 85 kDa subunit.
FT                                /FTId=PRO_0000302751.
FT   CHAIN     ?4441   4544       Low-density lipoprotein receptor-related
FT                                protein 1 intracellular domain.
FT                                /FTId=PRO_0000302752.
FT   TOPO_DOM     20   4419       Extracellular. {ECO:0000255}.
FT   TRANSMEM   4420   4444       Helical. {ECO:0000255}.
FT   TOPO_DOM   4445   4544       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       25     66       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       70    110       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      111    149       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      150    189       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT      292    334       LDL-receptor class B 1.
FT   REPEAT      335    378       LDL-receptor class B 2.
FT   REPEAT      379    422       LDL-receptor class B 3.
FT   DOMAIN      474    520       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      571    613       LDL-receptor class B 4.
FT   REPEAT      614    659       LDL-receptor class B 5.
FT   REPEAT      660    710       LDL-receptor class B 6.
FT   REPEAT      711    754       LDL-receptor class B 7.
FT   DOMAIN      803    843       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      852    892       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      893    933       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      934    973       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      974   1013       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1013   1053       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1060   1099       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1102   1142       LDL-receptor class A 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1143   1182       LDL-receptor class A 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1183   1222       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1223   1262       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1309   1355       LDL-receptor class B 8.
FT   REPEAT     1356   1398       LDL-receptor class B 9.
FT   REPEAT     1399   1445       LDL-receptor class B 10.
FT   REPEAT     1446   1490       LDL-receptor class B 11.
FT   REPEAT     1491   1531       LDL-receptor class B 12.
FT   DOMAIN     1536   1579       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1627   1669       LDL-receptor class B 13.
FT   REPEAT     1670   1713       LDL-receptor class B 14.
FT   REPEAT     1714   1753       LDL-receptor class B 15.
FT   REPEAT     1754   1798       LDL-receptor class B 16.
FT   DOMAIN     1846   1887       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1934   1976       LDL-receptor class B 17.
FT   REPEAT     1977   2019       LDL-receptor class B 18.
FT   REPEAT     2020   2063       LDL-receptor class B 19.
FT   REPEAT     2064   2107       LDL-receptor class B 20.
FT   DOMAIN     2155   2195       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     2253   2294       LDL-receptor class B 21.
FT   REPEAT     2295   2343       LDL-receptor class B 22.
FT   REPEAT     2344   2388       LDL-receptor class B 23.
FT   REPEAT     2389   2431       LDL-receptor class B 24.
FT   REPEAT     2432   2473       LDL-receptor class B 25.
FT   DOMAIN     2478   2518       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     2522   2563       LDL-receptor class A 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2564   2602       LDL-receptor class A 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2603   2641       LDL-receptor class A 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2642   2690       LDL-receptor class A 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2694   2732       LDL-receptor class A 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2732   2771       LDL-receptor class A 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2772   2814       LDL-receptor class A 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2816   2855       LDL-receptor class A 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2856   2899       LDL-receptor class A 19.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2902   2940       LDL-receptor class A 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2941   2981       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     2982   3022       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT     3069   3113       LDL-receptor class B 26.
FT   REPEAT     3114   3156       LDL-receptor class B 27.
FT   REPEAT     3157   3200       LDL-receptor class B 28.
FT   REPEAT     3201   3243       LDL-receptor class B 29.
FT   REPEAT     3244   3284       LDL-receptor class B 30.
FT   DOMAIN     3290   3331       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3332   3371       LDL-receptor class A 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3372   3410       LDL-receptor class A 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3411   3450       LDL-receptor class A 23.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3451   3491       LDL-receptor class A 24.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3492   3533       LDL-receptor class A 25.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3534   3572       LDL-receptor class A 26.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3573   3611       LDL-receptor class A 27.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3611   3649       LDL-receptor class A 28.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3652   3692       LDL-receptor class A 29.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3693   3733       LDL-receptor class A 30.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3739   3778       LDL-receptor class A 31.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3781   3823       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3824   3861       EGF-like 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     3912   3954       LDL-receptor class B 31.
FT   REPEAT     3970   4012       LDL-receptor class B 32.
FT   REPEAT     4013   4056       LDL-receptor class B 33.
FT   REPEAT     4057   4101       LDL-receptor class B 34.
FT   DOMAIN     4147   4183       EGF-like 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4196   4232       EGF-like 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4232   4268       EGF-like 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4268   4304       EGF-like 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4304   4340       EGF-like 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4340   4375       EGF-like 21. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4373   4409       EGF-like 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION     4445   4544       Interaction with MAFB. {ECO:0000250}.
FT   MOTIF      3940   3943       Recognition site for proteolytical
FT                                processing. {ECO:0000255}.
FT   MOTIF      4502   4507       NPXY motif.
FT   METAL       871    871       Calcium 1; via carbonyl oxygen.
FT   METAL       874    874       Calcium 1.
FT   METAL       876    876       Calcium 1; via carbonyl oxygen.
FT   METAL       878    878       Calcium 1.
FT   METAL       884    884       Calcium 1.
FT   METAL       885    885       Calcium 1.
FT   METAL      1032   1032       Calcium 2; via carbonyl oxygen.
FT   METAL      1035   1035       Calcium 2.
FT   METAL      1037   1037       Calcium 2; via carbonyl oxygen.
FT   METAL      1039   1039       Calcium 2.
FT   METAL      1045   1045       Calcium 2.
FT   METAL      1046   1046       Calcium 2.
FT   METAL      1080   1080       Calcium 3; via carbonyl oxygen.
FT   METAL      1083   1083       Calcium 3.
FT   METAL      1085   1085       Calcium 3; via carbonyl oxygen.
FT   METAL      1087   1087       Calcium 3.
FT   METAL      1093   1093       Calcium 3.
FT   METAL      1094   1094       Calcium 3.
FT   MOD_RES    2009   2009       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZX7}.
FT   MOD_RES    4460   4460       Phosphothreonine.
FT                                {ECO:0000305|PubMed:15272003}.
FT   MOD_RES    4507   4507       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:11854294}.
FT   MOD_RES    4517   4517       Phosphoserine.
FT                                {ECO:0000305|PubMed:15272003}.
FT   MOD_RES    4520   4520       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    4523   4523       Phosphoserine.
FT                                {ECO:0000305|PubMed:15272003}.
FT   CARBOHYD    114    114       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    136    136       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    185    185       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    239    239       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    274    274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    357    357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    446    446       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    729    729       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19139490,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    928    928       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1050   1050       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1154   1154       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1155   1155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1195   1195       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1218   1218       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1511   1511       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000269|PubMed:19139490,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1558   1558       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1575   1575       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1616   1616       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1645   1645       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1723   1723       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1733   1733       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1763   1763       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1825   1825       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1933   1933       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1995   1995       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2048   2048       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2117   2117       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2127   2127       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   2472   2472       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2502   2502       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2521   2521       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2539   2539       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2601   2601       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2620   2620       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2638   2638       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2815   2815       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   2905   2905       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3048   3048       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   3089   3089       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   3264   3264       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3333   3333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3488   3488       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   3662   3662       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3788   3788       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   3839   3839       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3953   3953       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   4075   4075       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   4125   4125       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   4179   4179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4278   4278       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4279   4279       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4364   4364       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     40       {ECO:0000250}.
FT   DISULFID     34     53       {ECO:0000250}.
FT   DISULFID     47     64       {ECO:0000250}.
FT   DISULFID     72     85       {ECO:0000250}.
FT   DISULFID     79     98       {ECO:0000250}.
FT   DISULFID     92    108       {ECO:0000250}.
FT   DISULFID    115    124       {ECO:0000250}.
FT   DISULFID    120    133       {ECO:0000250}.
FT   DISULFID    135    148       {ECO:0000250}.
FT   DISULFID    154    164       {ECO:0000250}.
FT   DISULFID    160    173       {ECO:0000250}.
FT   DISULFID    175    188       {ECO:0000250}.
FT   DISULFID    478    493       {ECO:0000250}.
FT   DISULFID    489    504       {ECO:0000250}.
FT   DISULFID    506    519       {ECO:0000250}.
FT   DISULFID    807    818       {ECO:0000250}.
FT   DISULFID    814    827       {ECO:0000250}.
FT   DISULFID    829    842       {ECO:0000250}.
FT   DISULFID    854    866
FT   DISULFID    861    879
FT   DISULFID    873    890
FT   DISULFID    895    907       {ECO:0000250}.
FT   DISULFID    902    920       {ECO:0000250}.
FT   DISULFID    914    931       {ECO:0000250}.
FT   DISULFID    936    948
FT   DISULFID    943    961
FT   DISULFID    955    971
FT   DISULFID    976    989
FT   DISULFID    984   1002
FT   DISULFID    996   1011
FT   DISULFID   1015   1027
FT   DISULFID   1022   1040
FT   DISULFID   1034   1051
FT   DISULFID   1062   1075
FT   DISULFID   1069   1088
FT   DISULFID   1082   1097
FT   DISULFID   1104   1118       {ECO:0000250}.
FT   DISULFID   1112   1131       {ECO:0000250}.
FT   DISULFID   1125   1140       {ECO:0000250}.
FT   DISULFID   1145   1159       {ECO:0000250}.
FT   DISULFID   1152   1172       {ECO:0000250}.
FT   DISULFID   1166   1182       {ECO:0000250}.
FT   DISULFID   1185   1196       {ECO:0000250}.
FT   DISULFID   1192   1206       {ECO:0000250}.
FT   DISULFID   1208   1221       {ECO:0000250}.
FT   DISULFID   1227   1237       {ECO:0000250}.
FT   DISULFID   1233   1246       {ECO:0000250}.
FT   DISULFID   1248   1261       {ECO:0000250}.
FT   DISULFID   1540   1553       {ECO:0000250}.
FT   DISULFID   1549   1563       {ECO:0000250}.
FT   DISULFID   1565   1578       {ECO:0000250}.
FT   DISULFID   1850   1861       {ECO:0000250}.
FT   DISULFID   1857   1871       {ECO:0000250}.
FT   DISULFID   1873   1886       {ECO:0000250}.
FT   DISULFID   2159   2170       {ECO:0000250}.
FT   DISULFID   2166   2180       {ECO:0000250}.
FT   DISULFID   2182   2194       {ECO:0000250}.
FT   DISULFID   2482   2493       {ECO:0000250}.
FT   DISULFID   2489   2503       {ECO:0000250}.
FT   DISULFID   2505   2517       {ECO:0000250}.
FT   DISULFID   2524   2537       {ECO:0000250}.
FT   DISULFID   2532   2550       {ECO:0000250}.
FT   DISULFID   2544   2561       {ECO:0000250}.
FT   DISULFID   2566   2578       {ECO:0000250}.
FT   DISULFID   2573   2591       {ECO:0000250}.
FT   DISULFID   2585   2600       {ECO:0000250}.
FT   DISULFID   2605   2617       {ECO:0000250}.
FT   DISULFID   2612   2630       {ECO:0000250}.
FT   DISULFID   2624   2639       {ECO:0000250}.
FT   DISULFID   2644   2666       {ECO:0000250}.
FT   DISULFID   2660   2679       {ECO:0000250}.
FT   DISULFID   2673   2688       {ECO:0000250}.
FT   DISULFID   2696   2708       {ECO:0000250}.
FT   DISULFID   2703   2721       {ECO:0000250}.
FT   DISULFID   2715   2730       {ECO:0000250}.
FT   DISULFID   2734   2746       {ECO:0000250}.
FT   DISULFID   2741   2759       {ECO:0000250}.
FT   DISULFID   2753   2769       {ECO:0000250}.
FT   DISULFID   2774   2787       {ECO:0000250}.
FT   DISULFID   2781   2800       {ECO:0000250}.
FT   DISULFID   2794   2812       {ECO:0000250}.
FT   DISULFID   2818   2830       {ECO:0000250}.
FT   DISULFID   2825   2843       {ECO:0000250}.
FT   DISULFID   2837   2853       {ECO:0000250}.
FT   DISULFID   2858   2870       {ECO:0000250}.
FT   DISULFID   2865   2884       {ECO:0000250}.
FT   DISULFID   2878   2897       {ECO:0000250}.
FT   DISULFID   2904   2917       {ECO:0000250}.
FT   DISULFID   2912   2930       {ECO:0000250}.
FT   DISULFID   2924   2939       {ECO:0000250}.
FT   DISULFID   2944   2956       {ECO:0000250}.
FT   DISULFID   2952   2965       {ECO:0000250}.
FT   DISULFID   2967   2980       {ECO:0000250}.
FT   DISULFID   2986   2996       {ECO:0000250}.
FT   DISULFID   2992   3005       {ECO:0000250}.
FT   DISULFID   3007   3021       {ECO:0000250}.
FT   DISULFID   3294   3305       {ECO:0000250}.
FT   DISULFID   3301   3315       {ECO:0000250}.
FT   DISULFID   3317   3330       {ECO:0000250}.
FT   DISULFID   3334   3346       {ECO:0000250}.
FT   DISULFID   3341   3359       {ECO:0000250}.
FT   DISULFID   3353   3369       {ECO:0000250}.
FT   DISULFID   3374   3386       {ECO:0000250}.
FT   DISULFID   3381   3399       {ECO:0000250}.
FT   DISULFID   3393   3408       {ECO:0000250}.
FT   DISULFID   3413   3426       {ECO:0000250}.
FT   DISULFID   3420   3439       {ECO:0000250}.
FT   DISULFID   3433   3448       {ECO:0000250}.
FT   DISULFID   3453   3466       {ECO:0000250}.
FT   DISULFID   3460   3479       {ECO:0000250}.
FT   DISULFID   3473   3489       {ECO:0000250}.
FT   DISULFID   3494   3507       {ECO:0000250}.
FT   DISULFID   3501   3520       {ECO:0000250}.
FT   DISULFID   3514   3531       {ECO:0000250}.
FT   DISULFID   3536   3548       {ECO:0000250}.
FT   DISULFID   3543   3561       {ECO:0000250}.
FT   DISULFID   3555   3570       {ECO:0000250}.
FT   DISULFID   3575   3587       {ECO:0000250}.
FT   DISULFID   3582   3600       {ECO:0000250}.
FT   DISULFID   3594   3609       {ECO:0000250}.
FT   DISULFID   3613   3625       {ECO:0000250}.
FT   DISULFID   3620   3638       {ECO:0000250}.
FT   DISULFID   3632   3647       {ECO:0000250}.
FT   DISULFID   3654   3666       {ECO:0000250}.
FT   DISULFID   3661   3679       {ECO:0000250}.
FT   DISULFID   3673   3690       {ECO:0000250}.
FT   DISULFID   3695   3709       {ECO:0000250}.
FT   DISULFID   3703   3722       {ECO:0000250}.
FT   DISULFID   3716   3731       {ECO:0000250}.
FT   DISULFID   3741   3754       {ECO:0000250}.
FT   DISULFID   3749   3767       {ECO:0000250}.
FT   DISULFID   3761   3776       {ECO:0000250}.
FT   DISULFID   3785   3798       {ECO:0000250}.
FT   DISULFID   3792   3807       {ECO:0000250}.
FT   DISULFID   3809   3822       {ECO:0000250}.
FT   DISULFID   3828   3838       {ECO:0000250}.
FT   DISULFID   3834   3847       {ECO:0000250}.
FT   DISULFID   3849   3860       {ECO:0000250}.
FT   DISULFID   4151   4160       {ECO:0000250}.
FT   DISULFID   4156   4169       {ECO:0000250}.
FT   DISULFID   4171   4182       {ECO:0000250}.
FT   DISULFID   4200   4210       {ECO:0000250}.
FT   DISULFID   4204   4220       {ECO:0000250}.
FT   DISULFID   4222   4231       {ECO:0000250}.
FT   DISULFID   4236   4246       {ECO:0000250}.
FT   DISULFID   4240   4256       {ECO:0000250}.
FT   DISULFID   4258   4267       {ECO:0000250}.
FT   DISULFID   4272   4282       {ECO:0000250}.
FT   DISULFID   4276   4292       {ECO:0000250}.
FT   DISULFID   4294   4303       {ECO:0000250}.
FT   DISULFID   4308   4318       {ECO:0000250}.
FT   DISULFID   4312   4328       {ECO:0000250}.
FT   DISULFID   4330   4339       {ECO:0000250}.
FT   DISULFID   4344   4352       {ECO:0000250}.
FT   DISULFID   4347   4363       {ECO:0000250}.
FT   DISULFID   4365   4374       {ECO:0000250}.
FT   DISULFID   4377   4387       {ECO:0000250}.
FT   DISULFID   4381   4397       {ECO:0000250}.
FT   DISULFID   4399   4408       {ECO:0000250}.
FT   VAR_SEQ     281    292       HVEQMAIDWLTG -> LCVFSKSQQEMG (in isoform
FT                                2). {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056919.
FT   VAR_SEQ     293   4544       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056920.
FT   VARIANT     166    166       N -> D (in dbSNP:rs2306691).
FT                                /FTId=VAR_021885.
FT   VARIANT     217    217       A -> V (in dbSNP:rs1800127).
FT                                /FTId=VAR_014725.
FT   VARIANT     869    869       E -> K (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs1207947902).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035994.
FT   VARIANT    1245   1245       K -> R (in KPA; reduced alpha-2
FT                                macroglobulin receptor activity; reduced
FT                                protein abundance; dbSNP:rs483353013).
FT                                {ECO:0000269|PubMed:26142438}.
FT                                /FTId=VAR_077982.
FT   VARIANT    2059   2059       V -> L (in dbSNP:rs2229278).
FT                                /FTId=VAR_029181.
FT   VARIANT    2080   2080       D -> N (in dbSNP:rs34577247).
FT                                /FTId=VAR_047525.
FT   VARIANT    2900   2900       Q -> P (in dbSNP:rs7397167).
FT                                {ECO:0000269|PubMed:3266596,
FT                                ECO:0000269|PubMed:9782078,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_047526.
FT   VARIANT    3258   3258       H -> Q (found in a patient with severe
FT                                mental retardation, seizures, stereotypic
FT                                behavior, high pain threshold and sleep
FT                                disturbances).
FT                                {ECO:0000269|PubMed:23033978}.
FT                                /FTId=VAR_069388.
FT   VARIANT    3760   3760       R -> H (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs569866427).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035995.
FT   VARIANT    4536   4536       E -> G (in dbSNP:rs17357542).
FT                                /FTId=VAR_047527.
FT   MUTAGEN    4460   4460       T->A: Strongly reduced phosphorylation
FT                                and loss of interaction with SHC1; when
FT                                associated with A-4517; A-4520 and A-
FT                                4523. {ECO:0000269|PubMed:15272003}.
FT   MUTAGEN    4470   4473       NPTY->APTA: No effect on tyrosine
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:11854294}.
FT   MUTAGEN    4470   4470       N->A: No effect on interaction with
FT                                GULP1. {ECO:0000269|PubMed:11729193}.
FT   MUTAGEN    4472   4472       T->A: No detectable effect on
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:15272003}.
FT   MUTAGEN    4504   4507       NPVY->APVA: Loss of tyrosine
FT                                phosphorylation. Abolishes interaction
FT                                with SHC1 and GULP1.
FT                                {ECO:0000269|PubMed:11854294}.
FT   MUTAGEN    4504   4504       N->A: Loss of interaction with GULP1.
FT                                {ECO:0000269|PubMed:11729193}.
FT   MUTAGEN    4517   4517       S->A: Strongly reduced phosphorylation
FT                                and loss of interaction with SHC1; when
FT                                associated with A-4460; A-4520 and A-
FT                                4523. {ECO:0000269|PubMed:15272003}.
FT   MUTAGEN    4520   4520       S->A: Strongly reduced phosphorylation
FT                                and loss of interaction with SHC1; when
FT                                associated with A-4460; A-4517 and A-
FT                                4523. {ECO:0000269|PubMed:15272003}.
FT   MUTAGEN    4523   4523       S->A: Strongly reduced phosphorylation
FT                                and loss of interaction with SHC1; when
FT                                associated with A-4460; A-4517 and A-
FT                                4520. {ECO:0000269|PubMed:15272003}.
FT   CONFLICT    685    685       D -> G (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1743   1743       G -> S (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   2871   2872       LS -> IA (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   3036   3036       R -> M (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   TURN        853    857       {ECO:0000244|PDB:1D2L}.
FT   STRAND      859    861       {ECO:0000244|PDB:1D2L}.
FT   TURN        862    864       {ECO:0000244|PDB:1D2L}.
FT   STRAND      865    867       {ECO:0000244|PDB:1D2L}.
FT   HELIX       869    871       {ECO:0000244|PDB:1D2L}.
FT   STRAND      874    876       {ECO:0000244|PDB:1D2L}.
FT   TURN        878    881       {ECO:0000244|PDB:1D2L}.
FT   STRAND      934    936       {ECO:0000244|PDB:2FYJ}.
FT   STRAND      940    942       {ECO:0000244|PDB:2FYJ}.
FT   TURN        944    946       {ECO:0000244|PDB:2FYL}.
FT   STRAND      948    950       {ECO:0000244|PDB:2FYJ}.
FT   STRAND      953    956       {ECO:0000244|PDB:2FYJ}.
FT   STRAND      958    961       {ECO:0000244|PDB:2FYJ}.
FT   TURN        964    968       {ECO:0000244|PDB:2FYJ}.
FT   TURN        969    971       {ECO:0000244|PDB:2FYL}.
FT   STRAND      974    976       {ECO:0000244|PDB:2FYJ}.
FT   STRAND      978    983       {ECO:0000244|PDB:2FYJ}.
FT   TURN        985    987       {ECO:0000244|PDB:2FYL}.
FT   STRAND      989    991       {ECO:0000244|PDB:2FYJ}.
FT   STRAND      995   1000       {ECO:0000244|PDB:2FYJ}.
FT   STRAND     1003   1007       {ECO:0000244|PDB:2FYJ}.
FT   STRAND     1009   1011       {ECO:0000244|PDB:2FYL}.
FT   STRAND     1013   1015       {ECO:0000244|PDB:1J8E}.
FT   STRAND     1019   1021       {ECO:0000244|PDB:1J8E}.
FT   STRAND     1027   1029       {ECO:0000244|PDB:1J8E}.
FT   HELIX      1030   1032       {ECO:0000244|PDB:1J8E}.
FT   STRAND     1035   1037       {ECO:0000244|PDB:1J8E}.
FT   STRAND     1040   1043       {ECO:0000244|PDB:1J8E}.
FT   HELIX      1044   1046       {ECO:0000244|PDB:1J8E}.
FT   HELIX      1048   1051       {ECO:0000244|PDB:1J8E}.
FT   TURN       1070   1072       {ECO:0000244|PDB:1CR8}.
FT   HELIX      1078   1080       {ECO:0000244|PDB:1CR8}.
FT   STRAND     1081   1085       {ECO:0000244|PDB:1CR8}.
FT   STRAND     1088   1091       {ECO:0000244|PDB:1CR8}.
FT   TURN       1092   1096       {ECO:0000244|PDB:1CR8}.
FT   STRAND     2778   2781       {ECO:0000244|PDB:2KNX}.
FT   TURN       2782   2785       {ECO:0000244|PDB:2KNX}.
FT   STRAND     2786   2789       {ECO:0000244|PDB:2KNX}.
FT   TURN       2790   2794       {ECO:0000244|PDB:2KNX}.
FT   STRAND     2795   2797       {ECO:0000244|PDB:2KNX}.
FT   STRAND     2800   2803       {ECO:0000244|PDB:2KNY}.
FT   HELIX      2804   2806       {ECO:0000244|PDB:2KNX}.
FT   HELIX      2808   2810       {ECO:0000244|PDB:2KNX}.
FT   STRAND     2813   2816       {ECO:0000244|PDB:2KNY}.
SQ   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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