ID LRP1_HUMAN Reviewed; 4544 AA. AC Q07954; Q2PP12; Q8IVG8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 10-AUG-2010, entry version 119. DE RecName: Full=Prolow-density lipoprotein receptor-related protein 1; DE Short=LRP-1; DE AltName: Full=Alpha-2-macroglobulin receptor; 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]. RC TISSUE=Liver; RX MEDLINE=89210795; 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 MEDLINE=95203893; 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]. RX MEDLINE=99000832; 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]. 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], AND VARIANT GLN-2900. 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 [GENOMIC DNA] OF 1-11. RX MEDLINE=90089395; 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 [7] 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 [8] 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 [9] RP PROTEOLYTIC PROCESSING. RX MEDLINE=90269210; 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 [10] RP FUNCTION. RX MEDLINE=91092405; 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 [11] 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 [12] 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 betwenn RT LRP and the PDGF."; RL J. Biol. Chem. 277:15499-15506(2002). RN [13] 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 [14] 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 [15] RP FUNCTION. RX PubMed=12713657; RA May P., Herz J.; RT "LDL receptor-related proteins in neurodevelopment."; RL Traffic 4:291-301(2003). RN [16] 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 [17] 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 [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-2127 AND RP ASN-3048, AND MASS SPECTROMETRY. 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 [19] 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 [20] 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, AND RP MASS SPECTROMETRY. 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 [21] RP STRUCTURE BY NMR OF 1059-1100 IN COMPLEX WITH CALCIUM IONS, AND RP DISULFIDE BONDS. RX MEDLINE=99253972; 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 [22] RP STRUCTURE BY NMR OF 851-893 IN COMPLEX WITH CALCIUM IONS, AND RP DISULFIDE BONDS. RX MEDLINE=20119280; 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 [23] 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 [24] 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 [25] 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). 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. CC -!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit CC and a non-covalently attached 515-kDa amino-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. 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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the LDLR family. CC -!- SIMILARITY: Contains 22 EGF-like domains. CC -!- SIMILARITY: Contains 31 LDL-receptor class A domains. CC -!- SIMILARITY: Contains 34 LDL-receptor class B repeats. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; X15424; CAA33464.1; -; Genomic_DNA. DR EMBL; Y18524; CAD57169.1; -; Genomic_DNA. DR IPI; IPI00020557; -. DR PIR; S02392; S02392. DR RefSeq; NP_002323.2; -. 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=1012-1054. 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 IntAct; Q07954; 2. DR MINT; MINT-5004471; -. DR STRING; Q07954; -. DR PhosphoSite; Q07954; -. DR PRIDE; Q07954; -. DR Ensembl; ENST00000243077; ENSP00000243077; ENSG00000123384; Homo sapiens. DR GeneID; 4035; -. DR KEGG; hsa:4035; -. DR UCSC; uc001snd.1; human. DR CTD; 4035; -. DR GeneCards; GC12P057497; -. DR GeneCards; GC12P057522; -. DR H-InvDB; HIX0026381; -. DR HGNC; HGNC:6692; LRP1. DR HPA; CAB018621; -. DR HPA; HPA022903; -. DR MIM; 107770; gene. DR PharmGKB; PA142671549; -. DR eggNOG; prNOG15949; -. DR HOGENOM; HBG378855; -. DR HOVERGEN; HBG006292; -. DR InParanoid; Q07954; -. DR Pathway_Interaction_DB; amb2_neutrophils_pathway; amb2 Integrin signaling. DR Pathway_Interaction_DB; pdgfrbpathway; PDGFR-beta signaling pathway. DR DrugBank; DB00009; Alteplase. DR DrugBank; DB00029; Anistreplase. DR DrugBank; DB00025; Antihemophilic Factor. DR DrugBank; DB00102; Becaplermin. DR DrugBank; DB00100; Coagulation Factor IX. DR DrugBank; DB00031; Tenecteplase. DR NextBio; 15806; -. DR ArrayExpress; Q07954; -. DR Bgee; Q07954; -. DR CleanEx; HS_LRP1; -. DR Genevestigator; Q07954; -. DR GermOnline; ENSG00000123384; Homo sapiens. DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005624; C:membrane fraction; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc. DR GO; GO:0005319; F:lipid transporter activity; TAS:ProtInc. DR GO; GO:0008034; F:lipoprotein binding; TAS:ProtInc. DR GO; GO:0070325; F:lipoprotein receptor binding; IC:BHF-UCL. DR GO; GO:0032403; F:protein complex binding; IDA:BHF-UCL. DR GO; GO:0004872; F:receptor activity; TAS:ProtInc. DR GO; GO:0043277; P:apoptotic cell clearance; ISS:BHF-UCL. DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc. DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0030178; P:negative regulation of Wnt receptor signali...; ISS:BHF-UCL. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:BHF-UCL. DR GO; GO:0032429; P:regulation of phospholipase A2 activity; ISS:BHF-UCL. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR006210; EGF-like. DR InterPro; IPR013032; EGF-like_reg_CS. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR000742; EGF_3. DR InterPro; IPR001881; EGF_Ca-bd. DR InterPro; IPR013091; EGF_Ca-bd_2. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR000033; LDL_rcpt_classB_YWTD_rpt. DR Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 8. DR Pfam; PF07645; EGF_CA; 2. DR Pfam; PF00058; Ldl_recept_b; 16. DR SMART; SM00181; EGF; 18. DR SMART; SM00179; EGF_CA; 3. DR SMART; SM00135; LY; 35. 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; Calcium; Cell membrane; Coated pit; Complete proteome; KW Cytoplasm; Developmental protein; Direct protein sequencing; KW Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Membrane; KW Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 19 Potential. 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 (Potential). FT TRANSMEM 4420 4444 Helical; (Potential). FT TOPO_DOM 4445 4544 Cytoplasmic (Potential). FT DOMAIN 25 66 LDL-receptor class A 1. FT DOMAIN 70 110 LDL-receptor class A 2. FT DOMAIN 111 149 EGF-like 1. FT DOMAIN 150 189 EGF-like 2; calcium-binding (Potential). 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. 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. FT DOMAIN 852 892 LDL-receptor class A 3. FT DOMAIN 893 933 LDL-receptor class A 4. FT DOMAIN 934 973 LDL-receptor class A 5. FT DOMAIN 974 1013 LDL-receptor class A 6. FT DOMAIN 1013 1053 LDL-receptor class A 7. FT DOMAIN 1060 1099 LDL-receptor class A 8. FT DOMAIN 1102 1142 LDL-receptor class A 9. FT DOMAIN 1143 1182 LDL-receptor class A 10. FT DOMAIN 1183 1222 EGF-like 5. FT DOMAIN 1223 1262 EGF-like 6. 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. 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. 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. 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. FT DOMAIN 2522 2563 LDL-receptor class A 11. FT DOMAIN 2564 2602 LDL-receptor class A 12. FT DOMAIN 2603 2641 LDL-receptor class A 13. FT DOMAIN 2642 2690 LDL-receptor class A 14. FT DOMAIN 2694 2732 LDL-receptor class A 15. FT DOMAIN 2732 2771 LDL-receptor class A 16. FT DOMAIN 2772 2814 LDL-receptor class A 17. FT DOMAIN 2816 2855 LDL-receptor class A 18. FT DOMAIN 2856 2899 LDL-receptor class A 19. FT DOMAIN 2902 2940 LDL-receptor class A 20. FT DOMAIN 2941 2981 EGF-like 11. FT DOMAIN 2982 3022 EGF-like 12; calcium-binding (Potential). 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. FT DOMAIN 3332 3371 LDL-receptor class A 21. FT DOMAIN 3372 3410 LDL-receptor class A 22. FT DOMAIN 3411 3450 LDL-receptor class A 23. FT DOMAIN 3451 3491 LDL-receptor class A 24. FT DOMAIN 3492 3533 LDL-receptor class A 25. FT DOMAIN 3534 3572 LDL-receptor class A 26. FT DOMAIN 3573 3611 LDL-receptor class A 27. FT DOMAIN 3611 3649 LDL-receptor class A 28. FT DOMAIN 3652 3692 LDL-receptor class A 29. FT DOMAIN 3693 3733 LDL-receptor class A 30. FT DOMAIN 3739 3778 LDL-receptor class A 31. FT DOMAIN 3781 3823 EGF-like 14. FT DOMAIN 3824 3861 EGF-like 15. 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. FT DOMAIN 4196 4232 EGF-like 17. FT DOMAIN 4232 4268 EGF-like 18. FT DOMAIN 4268 4304 EGF-like 19. FT DOMAIN 4304 4340 EGF-like 20. FT DOMAIN 4340 4375 EGF-like 21. FT DOMAIN 4373 4409 EGF-like 22. FT REGION 4445 4544 Interaction with MAFB (By similarity). FT MOTIF 3940 3943 Recognition site for proteolytical FT processing (Potential). FT MOTIF 4502 4507 Endocytosis signal (Potential). 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 4460 4460 Phosphothreonine (Probable). FT MOD_RES 4507 4507 Phosphotyrosine. FT MOD_RES 4517 4517 Phosphoserine (Probable). FT MOD_RES 4520 4520 Phosphoserine (Probable). FT MOD_RES 4523 4523 Phosphoserine (Probable). FT MOD_RES 4524 4524 Phosphothreonine (By similarity). FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential). FT CARBOHYD 136 136 N-linked (GlcNAc...) (Potential). FT CARBOHYD 185 185 N-linked (GlcNAc...) (Potential). FT CARBOHYD 239 239 N-linked (GlcNAc...) (Potential). FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential). FT CARBOHYD 357 357 N-linked (GlcNAc...) (Potential). FT CARBOHYD 446 446 N-linked (GlcNAc...). FT CARBOHYD 729 729 N-linked (GlcNAc...). FT CARBOHYD 928 928 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1050 1050 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1154 1154 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1155 1155 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1195 1195 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1218 1218 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1511 1511 N-linked (GlcNAc...). FT CARBOHYD 1558 1558 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1575 1575 N-linked (GlcNAc...). FT CARBOHYD 1616 1616 N-linked (GlcNAc...). FT CARBOHYD 1645 1645 N-linked (GlcNAc...). FT CARBOHYD 1723 1723 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1733 1733 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1763 1763 N-linked (GlcNAc...). FT CARBOHYD 1825 1825 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1933 1933 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1995 1995 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2048 2048 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2117 2117 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2127 2127 N-linked (GlcNAc...). FT CARBOHYD 2472 2472 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2502 2502 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2521 2521 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2539 2539 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2601 2601 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2620 2620 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2638 2638 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2815 2815 N-linked (GlcNAc...). FT CARBOHYD 2905 2905 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3048 3048 N-linked (GlcNAc...). FT CARBOHYD 3089 3089 N-linked (GlcNAc...). FT CARBOHYD 3264 3264 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3333 3333 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3488 3488 N-linked (GlcNAc...). FT CARBOHYD 3662 3662 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3788 3788 N-linked (GlcNAc...). FT CARBOHYD 3839 3839 N-linked (GlcNAc...) (Potential). FT CARBOHYD 3953 3953 N-linked (GlcNAc...). FT CARBOHYD 4075 4075 N-linked (GlcNAc...). FT CARBOHYD 4125 4125 N-linked (GlcNAc...). FT CARBOHYD 4179 4179 N-linked (GlcNAc...) (Potential). FT CARBOHYD 4278 4278 N-linked (GlcNAc...) (Potential). FT CARBOHYD 4279 4279 N-linked (GlcNAc...) (Potential). FT CARBOHYD 4364 4364 N-linked (GlcNAc...) (Potential). FT DISULFID 27 40 By similarity. FT DISULFID 34 53 By similarity. FT DISULFID 47 64 By similarity. FT DISULFID 72 85 By similarity. FT DISULFID 79 98 By similarity. FT DISULFID 92 108 By similarity. FT DISULFID 115 124 By similarity. FT DISULFID 120 133 By similarity. FT DISULFID 135 148 By similarity. FT DISULFID 154 164 By similarity. FT DISULFID 160 173 By similarity. FT DISULFID 175 188 By similarity. FT DISULFID 478 493 By similarity. FT DISULFID 489 504 By similarity. FT DISULFID 506 519 By similarity. FT DISULFID 807 818 By similarity. FT DISULFID 814 827 By similarity. FT DISULFID 829 842 By similarity. FT DISULFID 854 866 FT DISULFID 861 879 FT DISULFID 873 890 FT DISULFID 895 907 By similarity. FT DISULFID 902 920 By similarity. FT DISULFID 914 931 By similarity. 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 By similarity. FT DISULFID 1112 1131 By similarity. FT DISULFID 1125 1140 By similarity. FT DISULFID 1145 1159 By similarity. FT DISULFID 1152 1172 By similarity. FT DISULFID 1166 1182 By similarity. FT DISULFID 1185 1196 By similarity. FT DISULFID 1192 1206 By similarity. FT DISULFID 1208 1221 By similarity. FT DISULFID 1227 1237 By similarity. FT DISULFID 1233 1246 By similarity. FT DISULFID 1248 1261 By similarity. FT DISULFID 1540 1553 By similarity. FT DISULFID 1549 1563 By similarity. FT DISULFID 1565 1578 By similarity. FT DISULFID 1850 1861 By similarity. FT DISULFID 1857 1871 By similarity. FT DISULFID 1873 1886 By similarity. FT DISULFID 2159 2170 By similarity. FT DISULFID 2166 2180 By similarity. FT DISULFID 2182 2194 By similarity. FT DISULFID 2482 2493 By similarity. FT DISULFID 2489 2503 By similarity. FT DISULFID 2505 2517 By similarity. FT DISULFID 2524 2537 By similarity. FT DISULFID 2532 2550 By similarity. FT DISULFID 2544 2561 By similarity. FT DISULFID 2566 2578 By similarity. FT DISULFID 2573 2591 By similarity. FT DISULFID 2585 2600 By similarity. FT DISULFID 2605 2617 By similarity. FT DISULFID 2612 2630 By similarity. FT DISULFID 2624 2639 By similarity. FT DISULFID 2644 2666 By similarity. FT DISULFID 2660 2679 By similarity. FT DISULFID 2673 2688 By similarity. FT DISULFID 2696 2708 By similarity. FT DISULFID 2703 2721 By similarity. FT DISULFID 2715 2730 By similarity. FT DISULFID 2734 2746 By similarity. FT DISULFID 2741 2759 By similarity. FT DISULFID 2753 2769 By similarity. FT DISULFID 2774 2787 By similarity. FT DISULFID 2781 2800 By similarity. FT DISULFID 2794 2812 By similarity. FT DISULFID 2818 2830 By similarity. FT DISULFID 2825 2843 By similarity. FT DISULFID 2837 2853 By similarity. FT DISULFID 2858 2870 By similarity. FT DISULFID 2865 2884 By similarity. FT DISULFID 2878 2897 By similarity. FT DISULFID 2904 2917 By similarity. FT DISULFID 2912 2930 By similarity. FT DISULFID 2924 2939 By similarity. FT DISULFID 2944 2956 By similarity. FT DISULFID 2952 2965 By similarity. FT DISULFID 2967 2980 By similarity. FT DISULFID 2986 2996 By similarity. FT DISULFID 2992 3005 By similarity. FT DISULFID 3007 3021 By similarity. FT DISULFID 3294 3305 By similarity. FT DISULFID 3301 3315 By similarity. FT DISULFID 3317 3330 By similarity. FT DISULFID 3334 3346 By similarity. FT DISULFID 3341 3359 By similarity. FT DISULFID 3353 3369 By similarity. FT DISULFID 3374 3386 By similarity. FT DISULFID 3381 3399 By similarity. FT DISULFID 3393 3408 By similarity. FT DISULFID 3413 3426 By similarity. FT DISULFID 3420 3439 By similarity. FT DISULFID 3433 3448 By similarity. FT DISULFID 3453 3466 By similarity. FT DISULFID 3460 3479 By similarity. FT DISULFID 3473 3489 By similarity. FT DISULFID 3494 3507 By similarity. FT DISULFID 3501 3520 By similarity. FT DISULFID 3514 3531 By similarity. FT DISULFID 3536 3548 By similarity. FT DISULFID 3543 3561 By similarity. FT DISULFID 3555 3570 By similarity. FT DISULFID 3575 3587 By similarity. FT DISULFID 3582 3600 By similarity. FT DISULFID 3594 3609 By similarity. FT DISULFID 3613 3625 By similarity. FT DISULFID 3620 3638 By similarity. FT DISULFID 3632 3647 By similarity. FT DISULFID 3654 3666 By similarity. FT DISULFID 3661 3679 By similarity. FT DISULFID 3673 3690 By similarity. FT DISULFID 3695 3709 By similarity. FT DISULFID 3703 3722 By similarity. FT DISULFID 3716 3731 By similarity. FT DISULFID 3741 3754 By similarity. FT DISULFID 3749 3767 By similarity. FT DISULFID 3761 3776 By similarity. FT DISULFID 3785 3798 By similarity. FT DISULFID 3792 3807 By similarity. FT DISULFID 3809 3822 By similarity. FT DISULFID 3828 3838 By similarity. FT DISULFID 3834 3847 By similarity. FT DISULFID 3849 3860 By similarity. FT DISULFID 4151 4160 By similarity. FT DISULFID 4156 4169 By similarity. FT DISULFID 4171 4182 By similarity. FT DISULFID 4200 4210 By similarity. FT DISULFID 4204 4220 By similarity. FT DISULFID 4222 4231 By similarity. FT DISULFID 4236 4246 By similarity. FT DISULFID 4240 4256 By similarity. FT DISULFID 4258 4267 By similarity. FT DISULFID 4272 4282 By similarity. FT DISULFID 4276 4292 By similarity. FT DISULFID 4294 4303 By similarity. FT DISULFID 4308 4318 By similarity. FT DISULFID 4312 4328 By similarity. FT DISULFID 4330 4339 By similarity. FT DISULFID 4344 4352 By similarity. FT DISULFID 4347 4363 By similarity. FT DISULFID 4365 4374 By similarity. FT DISULFID 4377 4387 By similarity. FT DISULFID 4381 4397 By similarity. FT DISULFID 4399 4408 By similarity. 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). FT /FTId=VAR_035994. 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 P -> Q (in dbSNP:rs7397167). FT /FTId=VAR_047526. FT VARIANT 3760 3760 R -> H (in a colorectal cancer sample; FT somatic mutation). 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. FT MUTAGEN 4470 4473 NPTY->APTA: No effect on tyrosine FT phosphorylation. FT MUTAGEN 4470 4470 N->A: No effect on interaction with FT GULP1. FT MUTAGEN 4472 4472 T->A: No detectable effect on FT phosphorylation. FT MUTAGEN 4504 4507 NPVY->APVA: Loss of tyrosine FT phosphorylation. Abolishes interaction FT with SHC1 and GULP1. FT MUTAGEN 4504 4504 N->A: Loss of interaction with GULP1. 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. 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. 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. FT CONFLICT 685 685 D -> G (in Ref. 8; AA sequence). FT CONFLICT 1743 1743 G -> S (in Ref. 8; AA sequence). FT CONFLICT 2871 2872 LS -> IA (in Ref. 8; AA sequence). FT CONFLICT 3036 3036 R -> M (in Ref. 8; AA sequence). FT TURN 853 857 FT STRAND 859 861 FT TURN 862 864 FT STRAND 865 867 FT HELIX 869 871 FT STRAND 874 876 FT TURN 878 881 FT STRAND 934 936 FT STRAND 940 942 FT STRAND 948 950 FT STRAND 953 956 FT STRAND 958 961 FT TURN 964 968 FT STRAND 974 976 FT STRAND 978 983 FT STRAND 989 991 FT STRAND 995 1000 FT STRAND 1003 1007 FT STRAND 1013 1015 FT STRAND 1019 1021 FT STRAND 1027 1029 FT HELIX 1030 1032 FT STRAND 1035 1037 FT STRAND 1040 1043 FT HELIX 1044 1046 FT HELIX 1048 1051 FT TURN 1070 1072 FT HELIX 1078 1080 FT STRAND 1081 1085 FT STRAND 1088 1091 FT TURN 1092 1096 SQ SEQUENCE 4544 AA; 504575 MW; 90C534835A7D0A3B 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 APKNPHCTSP 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 //