LRP1_MOUSE
ID LRP1_MOUSE Reviewed; 4545 AA.
AC Q91ZX7; Q61291; Q920Y4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Prolow-density lipoprotein receptor-related protein 1 {ECO:0000305};
DE Short=LRP-1;
DE AltName: Full=Alpha-2-macroglobulin receptor;
DE Short=A2MR;
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 {ECO:0000312|MGI:MGI:96828};
GN Synonyms=A2mr {ECO:0000312|MGI:MGI:96828};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA47817.1}
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:CAA47817.1};
RX PubMed=8485155; DOI=10.1016/0167-4781(93)90244-8;
RA Van Leuven F., Stas L., Raymakers L., Overbergh L., De Strooper B.,
RA Hilliker C., Lorent K., Fias E., Umans L., Torrekens S., Serneels L.,
RA Moechars D., Van den Berghe H.;
RT "Molecular cloning and sequencing of the murine alpha-2-macroglobulin
RT receptor cDNA.";
RL Biochim. Biophys. Acta 1173:71-74(1993).
RN [2] {ECO:0000312|EMBL:AAL09567.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/J {ECO:0000312|EMBL:AAL09567.1}, and
RC CBA/J {ECO:0000312|EMBL:AAL09566.1};
RX PubMed=12151109; DOI=10.1016/s0167-4781(02)00419-0;
RA Smeijers L., Willems S., Lauwers A., Thiry E., van Leuven F.,
RA Roebroek A.J.M.;
RT "Functional expression of murine LRP1 requires correction of Lrp1 cDNA
RT sequences.";
RL Biochim. Biophys. Acta 1577:155-158(2002).
RN [3]
RP FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
RX PubMed=1618748; DOI=10.1016/s0021-9258(18)42291-0;
RA Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K.,
RA 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 [4]
RP INTERACTION WITH DAB2.
RX PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
RA Morris S.M., Cooper J.A.;
RT "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts
RT with AP-2.";
RL Traffic 2:111-123(2001).
RN [5] {ECO:0000305}
RP INTERACTION WITH MAFB.
RX PubMed=15135046; DOI=10.1016/j.febslet.2004.03.069;
RA Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M.,
RA Willnow T.E.;
RT "Low-density lipoprotein receptor-related protein interacts with MafB, a
RT regulator of hindbrain development.";
RL FEBS Lett. 565:23-27(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1423604; DOI=10.1016/0092-8674(92)90511-a;
RA Herz J., Clouthier D.E., Hammer R.E.;
RT "LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes
RT and is essential for embryo implantation.";
RL Cell 71:411-421(1992).
RN [7]
RP ERRATUM OF PUBMED:1423604.
RX PubMed=8490961; DOI=10.1016/0092-8674(93)90130-i;
RA Herz J., Couthier D.E., Hammer R.E.;
RL Cell 73:428-428(1993).
RN [8]
RP INTERACTION WITH MDK.
RX PubMed=10772929; DOI=10.1006/bbrc.2000.2549;
RA Muramatsu H., Zou K., Sakaguchi N., Ikematsu S., Sakuma S., Muramatsu T.;
RT "LDL receptor-related protein as a component of the midkine receptor.";
RL Biochem. Biophys. Res. Commun. 270:936-941(2000).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730; ASN-2128 AND ASN-3049.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-447.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP FUNCTION AS A RECEPTOR FOR CHOLIX TOXIN.
RX PubMed=18276581; DOI=10.1074/jbc.m710008200;
RA Jorgensen R., Purdy A.E., Fieldhouse R.J., Kimber M.S., Bartlett D.H.,
RA Merrill A.R.;
RT "Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae.";
RL J. Biol. Chem. 283:10671-10678(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2010, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP FUNCTION.
RX PubMed=32296178; DOI=10.1038/s41586-020-2156-5;
RA Rauch J.N., Luna G., Guzman E., Challis C., Sibih Y.E., Leshuk C.,
RA Hernandez I., Wegmann S., Hyman B.T., Gradinaru V., Kampmann M.,
RA Kosik K.S.;
RT "LRP1 is a master regulator of tau uptake and spread.";
RL Nature 580:381-385(2020).
CC -!- FUNCTION: Endocytic receptor involved in endocytosis and in
CC phagocytosis of apoptotic cells. Required for early embryonic
CC development (PubMed:1423604). Involved in cellular lipid homeostasis.
CC Involved in the plasma clearance of chylomicron remnants and activated
CC LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of
CC complexes between plasminogen activators and their endogenous
CC inhibitors. Acts as an alpha-2-macroglobulin receptor (By similarity).
CC Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as
CC well as its subsequent spread (PubMed:32296178). May modulate cellular
CC events, such as APP metabolism, kinase-dependent intracellular
CC signaling, neuronal calcium signaling as well as neurotransmission (By
CC similarity). {ECO:0000250|UniProtKB:Q07954, ECO:0000269|PubMed:1423604,
CC ECO:0000269|PubMed:32296178}.
CC -!- FUNCTION: (Microbial infection) Functions as a receptor for Vibrio
CC cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A.
CC {ECO:0000269|PubMed:1618748, ECO:0000269|PubMed:18276581}.
CC -!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a
CC non-covalently attached 515-kDa N-terminal subunit. Intracellular
CC domain interacts with MAFB (PubMed:15135046). Found in a complex with
CC PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17, PID1/PCLI1, PDGF and
CC CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1 (By
CC similarity). Can weakly interact (via NPXY motif) with DAB2 (via PID
CC domain); the interaction is enhanced by tyrosine phosphorylation of the
CC NPXY motif (PubMed:11247302). Interacts with MDK; promotes neuronal
CC survival (PubMed:10772929). Interacts with LRPAP1; this interaction is
CC followed by rapid internalization. Interacts with uPA/PLAU and
CC PAI1/SERPINE1, either individually or in complex with each other,
CC leading to rapid endocytosis; this interaction is abolished in the
CC presence of LRPAP1/RAP. Also interacts with tPA/PLAT alone or in
CC complex with SERPINE1. Interacts with the urokinase receptor PLAUR;
CC this interaction leads to PLAUR internalization and is impaired in the
CC presence of SORL1. Interacts with PDGFB. Interacts with TAU/MAPT,
CC leading to endocytosis; this interaction is reduced in the presence of
CC LRPAP1/RAP (By similarity). {ECO:0000250|UniProtKB:Q07954,
CC ECO:0000269|PubMed:10772929, ECO:0000269|PubMed:11247302,
CC ECO:0000269|PubMed:15135046}.
CC -!- INTERACTION:
CC Q91ZX7; P97318: Dab1; NbExp=2; IntAct=EBI-300955, EBI-81680;
CC Q91ZX7; Q62108: Dlg4; NbExp=4; IntAct=EBI-300955, EBI-300895;
CC Q91ZX7; P48356: Lepr; NbExp=2; IntAct=EBI-300955, EBI-2257257;
CC Q91ZX7; Q9WVI9: Mapk8ip1; NbExp=2; IntAct=EBI-300955, EBI-74515;
CC Q91ZX7; Q9ERE9: Mapk8ip2; NbExp=2; IntAct=EBI-300955, EBI-74576;
CC -!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
CC 1 85 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07954}.
CC Membrane, coated pit {ECO:0000250|UniProtKB:Q07954}.
CC -!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
CC 1 515 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q07954};
CC Extracellular side {ECO:0000250|UniProtKB:Q07954}. Membrane, coated pit
CC {ECO:0000250|UniProtKB:Q07954}.
CC -!- SUBCELLULAR LOCATION: Golgi outpost {ECO:0000250|UniProtKB:G3V928}.
CC Cytoplasm, cytoskeleton, microtubule organizing center
CC {ECO:0000250|UniProtKB:G3V928}. Note=Localizes to the postsynaptic
CC Golgi apparatus region, also named Golgi outpost, which shapes dendrite
CC morphology by functioning as sites of acentrosomal microtubule
CC nucleation. {ECO:0000250|UniProtKB:G3V928}.
CC -!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
CC 1 intracellular domain]: Cytoplasm {ECO:0000250|UniProtKB:Q07954}.
CC Nucleus {ECO:0000250|UniProtKB:Q07954}. Note=After cleavage, the
CC intracellular domain (LRPICD) is detected both in the cytoplasm and in
CC the nucleus. {ECO:0000250|UniProtKB:Q07954}.
CC -!- PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues upon stimulation with PDGF.
CC Tyrosine phosphorylation promotes interaction with SHC1 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515
CC kDa large extracellular domain (LRP-515) that remains non-covalently
CC associated. Gamma-secretase-dependent cleavage of LRP-85 releases the
CC intracellular domain from the membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q07954}.
CC -!- DISRUPTION PHENOTYPE: Death during early embryogenesis around 14 dpc.
CC {ECO:0000269|PubMed:1423604}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000255}.
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DR EMBL; X67469; CAA47817.1; ALT_SEQ; mRNA.
DR EMBL; AF367720; AAL09566.1; -; mRNA.
DR EMBL; AF369477; AAL09567.1; -; Genomic_DNA.
DR EMBL; AF369389; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369390; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369391; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369392; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369393; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369394; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369395; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369396; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369397; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369398; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369399; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369400; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369401; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369402; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369403; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369404; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369405; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369406; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369407; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369408; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369409; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369410; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369411; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369412; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369413; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369414; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369415; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369416; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369417; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369418; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369419; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369420; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369421; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369422; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369423; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369424; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369425; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369426; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369427; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369428; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369429; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369430; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369431; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369432; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369433; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369434; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369435; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369436; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369437; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369438; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369439; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369440; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369441; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369442; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369443; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369444; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369445; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369446; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369447; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369448; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369449; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369450; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369451; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369452; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369453; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369454; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369455; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369456; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369457; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369458; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369459; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369460; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369461; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369462; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369463; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369464; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369465; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369466; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369467; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369468; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369469; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369470; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369471; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369472; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369473; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369474; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369475; AAL09567.1; JOINED; Genomic_DNA.
DR EMBL; AF369476; AAL09567.1; JOINED; Genomic_DNA.
DR CCDS; CCDS24245.1; -.
DR PIR; S25111; S25111.
DR RefSeq; NP_032538.2; NM_008512.2.
DR SMR; Q91ZX7; -.
DR BioGRID; 201201; 24.
DR ComplexPortal; CPX-4461; Prolow-density lipoprotein receptor-related protein 1 complex.
DR CORUM; Q91ZX7; -.
DR DIP; DIP-47785N; -.
DR IntAct; Q91ZX7; 10.
DR MINT; Q91ZX7; -.
DR STRING; 10090.ENSMUSP00000044004; -.
DR GlyConnect; 2611; 35 N-Linked glycans (30 sites).
DR GlyGen; Q91ZX7; 51 sites, 33 N-linked glycans (30 sites).
DR iPTMnet; Q91ZX7; -.
DR PhosphoSitePlus; Q91ZX7; -.
DR SwissPalm; Q91ZX7; -.
DR CPTAC; non-CPTAC-3838; -.
DR jPOST; Q91ZX7; -.
DR MaxQB; Q91ZX7; -.
DR PaxDb; Q91ZX7; -.
DR PeptideAtlas; Q91ZX7; -.
DR PRIDE; Q91ZX7; -.
DR ProteomicsDB; 252676; -.
DR DNASU; 16971; -.
DR GeneID; 16971; -.
DR KEGG; mmu:16971; -.
DR UCSC; uc007hjx.1; mouse.
DR CTD; 4035; -.
DR MGI; MGI:96828; Lrp1.
DR eggNOG; KOG1215; Eukaryota.
DR InParanoid; Q91ZX7; -.
DR OrthoDB; 1606at2759; -.
DR PhylomeDB; Q91ZX7; -.
DR TreeFam; TF315253; -.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 16971; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Lrp1; mouse.
DR PRO; PR:Q91ZX7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91ZX7; protein.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0032593; C:insulin-responsive compartment; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0062136; C:low-density lipoprotein receptor complex; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0016964; F:alpha-2 macroglobulin receptor activity; ISS:UniProtKB.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; IMP:ARUK-UCL.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISO:MGI.
DR GO; GO:0015026; F:coreceptor activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0097242; P:amyloid-beta clearance; IMP:BHF-UCL.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IDA:ARUK-UCL.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IDA:ARUK-UCL.
DR GO; GO:0035909; P:aorta morphogenesis; IMP:BHF-UCL.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
DR GO; GO:0002265; P:astrocyte activation involved in immune response; IGI:ARUK-UCL.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0044242; P:cellular lipid catabolic process; ISO:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0061642; P:chemoattraction of axon; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IMP:BHF-UCL.
DR GO; GO:0007041; P:lysosomal transport; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; IMP:BHF-UCL.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IMP:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:BHF-UCL.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IMP:ARUK-UCL.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:1904109; P:positive regulation of cholesterol import; ISO:MGI.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:ComplexPortal.
DR GO; GO:0048694; P:positive regulation of collateral sprouting of injured axon; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0032370; P:positive regulation of lipid transport; IMP:BHF-UCL.
DR GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0051222; P:positive regulation of protein transport; ISO:MGI.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; ISO:MGI.
DR GO; GO:1904300; P:positive regulation of transcytosis; IMP:ARUK-UCL.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:BHF-UCL.
DR GO; GO:0032374; P:regulation of cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0032429; P:regulation of phospholipase A2 activity; IMP:BHF-UCL.
DR GO; GO:1905109; P:regulation of pulmonary blood vessel remodeling; IMP:BHF-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; IMP:ARUK-UCL.
DR CDD; cd00112; LDLa; 31.
DR Gene3D; 2.120.10.30; -; 8.
DR Gene3D; 4.10.400.10; -; 30.
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; 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; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 30.
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 Acetylation; Calcium; Cell membrane; Coated pit; Cytoplasm; Cytoskeleton;
KW Developmental protein; Disulfide bond; EGF-like domain; Endocytosis;
KW Glycoprotein; Golgi apparatus; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..4545
FT /note="Prolow-density lipoprotein receptor-related protein
FT 1"
FT /id="PRO_0000273273"
FT CHAIN 20..?3944
FT /note="Low-density lipoprotein receptor-related protein 1
FT 515 kDa subunit"
FT /id="PRO_0000302753"
FT CHAIN ?3945..4545
FT /note="Low-density lipoprotein receptor-related protein 1
FT 85 kDa subunit"
FT /id="PRO_0000302754"
FT CHAIN ?4442..4545
FT /note="Low-density lipoprotein receptor-related protein 1
FT intracellular domain"
FT /id="PRO_0000302755"
FT TOPO_DOM 20..4424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4425..4445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4446..4545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..67
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 71..111
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 112..150
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 151..190
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 293..335
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 336..379
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255"
FT REPEAT 380..423
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255"
FT DOMAIN 475..521
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 572..614
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255"
FT REPEAT 615..660
FT /note="LDL-receptor class B 5"
FT /evidence="ECO:0000255"
FT REPEAT 661..711
FT /note="LDL-receptor class B 6"
FT /evidence="ECO:0000255"
FT REPEAT 712..755
FT /note="LDL-receptor class B 7"
FT /evidence="ECO:0000255"
FT DOMAIN 804..844
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 853..893
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 894..934
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 935..974
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 975..1014
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1014..1054
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1061..1100
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1103..1143
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1144..1183
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1184..1223
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1224..1263
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1310..1356
FT /note="LDL-receptor class B 8"
FT /evidence="ECO:0000255"
FT REPEAT 1357..1399
FT /note="LDL-receptor class B 9"
FT /evidence="ECO:0000255"
FT REPEAT 1400..1446
FT /note="LDL-receptor class B 10"
FT /evidence="ECO:0000255"
FT REPEAT 1447..1491
FT /note="LDL-receptor class B 11"
FT /evidence="ECO:0000255"
FT REPEAT 1492..1532
FT /note="LDL-receptor class B 12"
FT /evidence="ECO:0000255"
FT DOMAIN 1537..1580
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1628..1670
FT /note="LDL-receptor class B 13"
FT /evidence="ECO:0000255"
FT REPEAT 1671..1714
FT /note="LDL-receptor class B 14"
FT /evidence="ECO:0000255"
FT REPEAT 1715..1754
FT /note="LDL-receptor class B 15"
FT /evidence="ECO:0000255"
FT REPEAT 1755..1799
FT /note="LDL-receptor class B 16"
FT /evidence="ECO:0000255"
FT DOMAIN 1847..1888
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1935..1977
FT /note="LDL-receptor class B 17"
FT /evidence="ECO:0000255"
FT REPEAT 1978..2020
FT /note="LDL-receptor class B 18"
FT /evidence="ECO:0000255"
FT REPEAT 2021..2064
FT /note="LDL-receptor class B 19"
FT /evidence="ECO:0000255"
FT REPEAT 2065..2108
FT /note="LDL-receptor class B 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2156..2196
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2254..2295
FT /note="LDL-receptor class B 21"
FT /evidence="ECO:0000255"
FT REPEAT 2296..2344
FT /note="LDL-receptor class B 22"
FT /evidence="ECO:0000255"
FT REPEAT 2345..2389
FT /note="LDL-receptor class B 23"
FT /evidence="ECO:0000255"
FT REPEAT 2390..2432
FT /note="LDL-receptor class B 24"
FT /evidence="ECO:0000255"
FT REPEAT 2433..2474
FT /note="LDL-receptor class B 25"
FT /evidence="ECO:0000255"
FT DOMAIN 2479..2519
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2523..2564
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2565..2603
FT /note="LDL-receptor class A 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2604..2642
FT /note="LDL-receptor class A 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2643..2691
FT /note="LDL-receptor class A 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2695..2733
FT /note="LDL-receptor class A 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2733..2772
FT /note="LDL-receptor class A 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2773..2815
FT /note="LDL-receptor class A 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2817..2856
FT /note="LDL-receptor class A 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2857..2900
FT /note="LDL-receptor class A 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2903..2941
FT /note="LDL-receptor class A 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2942..2982
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2983..3023
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3070..3114
FT /note="LDL-receptor class B 26"
FT /evidence="ECO:0000255"
FT REPEAT 3115..3157
FT /note="LDL-receptor class B 27"
FT /evidence="ECO:0000255"
FT REPEAT 3158..3201
FT /note="LDL-receptor class B 28"
FT /evidence="ECO:0000255"
FT REPEAT 3202..3244
FT /note="LDL-receptor class B 29"
FT /evidence="ECO:0000255"
FT REPEAT 3245..3285
FT /note="LDL-receptor class B 30"
FT /evidence="ECO:0000255"
FT DOMAIN 3291..3332
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3333..3372
FT /note="LDL-receptor class A 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3373..3411
FT /note="LDL-receptor class A 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3412..3451
FT /note="LDL-receptor class A 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3452..3492
FT /note="LDL-receptor class A 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3493..3534
FT /note="LDL-receptor class A 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3535..3573
FT /note="LDL-receptor class A 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3574..3612
FT /note="LDL-receptor class A 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3612..3650
FT /note="LDL-receptor class A 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3653..3693
FT /note="LDL-receptor class A 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3694..3734
FT /note="LDL-receptor class A 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3740..3779
FT /note="LDL-receptor class A 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3782..3824
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3825..3862
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3913..3955
FT /note="LDL-receptor class B 31"
FT /evidence="ECO:0000255"
FT REPEAT 3971..4013
FT /note="LDL-receptor class B 32"
FT /evidence="ECO:0000255"
FT REPEAT 4014..4057
FT /note="LDL-receptor class B 33"
FT /evidence="ECO:0000255"
FT REPEAT 4058..4102
FT /note="LDL-receptor class B 34"
FT /evidence="ECO:0000255"
FT DOMAIN 4148..4184
FT /note="EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4197..4233
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4233..4269
FT /note="EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4269..4305
FT /note="EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4305..4341
FT /note="EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4341..4376
FT /note="EGF-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4374..4410
FT /note="EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4446..4545
FT /note="Interaction with MAFB"
FT /evidence="ECO:0000269|PubMed:15135046"
FT MOTIF 3941..3944
FT /note="Recognition site for proteolytical processing"
FT /evidence="ECO:0000255"
FT MOTIF 4503..4508
FT /note="NPXY motif"
FT BINDING 872
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 875
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 877
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 879
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 885
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 886
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1033
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1036
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1038
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1040
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1046
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1047
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1081
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1084
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1086
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1088
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1094
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1095
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 2010
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 4461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4508
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1051
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 2473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 3090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..41
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 35..54
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 48..65
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 73..86
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 80..99
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 93..109
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 116..125
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 121..134
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 136..149
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 155..165
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 161..174
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 176..189
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 479..494
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 490..505
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 507..520
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 808..819
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 815..828
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 830..843
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 855..867
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT DISULFID 862..880
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT DISULFID 874..891
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT DISULFID 896..908
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 903..921
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 915..932
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 937..949
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 944..962
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 956..972
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 977..990
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 985..1003
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 997..1012
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1016..1028
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1023..1041
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1035..1052
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1063..1076
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT DISULFID 1070..1089
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT DISULFID 1083..1098
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT DISULFID 1105..1119
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1113..1132
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1126..1141
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1146..1160
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1153..1173
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1167..1183
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1186..1197
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1193..1207
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1209..1222
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1228..1238
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1234..1247
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1249..1262
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1541..1554
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1550..1564
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1566..1579
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1851..1862
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1858..1872
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 1874..1887
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2160..2171
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2167..2181
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2183..2195
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2483..2494
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2490..2504
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2506..2518
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2525..2538
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2533..2551
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2545..2562
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2567..2579
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2574..2592
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2586..2601
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2606..2618
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2613..2631
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2625..2640
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2645..2667
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2661..2680
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2674..2689
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2697..2709
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2704..2722
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2716..2731
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2735..2747
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2742..2760
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2754..2770
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2775..2788
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2782..2801
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2795..2813
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2819..2831
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2826..2844
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2838..2854
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2859..2871
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2866..2885
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2879..2898
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2905..2918
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2913..2931
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2925..2940
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2945..2957
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2953..2966
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2968..2981
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2987..2997
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 2993..3006
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3008..3022
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3295..3306
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3302..3316
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3318..3331
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3335..3347
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3342..3360
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3354..3370
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3375..3387
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3382..3400
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3394..3409
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3414..3427
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3421..3440
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3434..3449
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3454..3467
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3461..3480
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3474..3490
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3495..3508
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3502..3521
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3515..3532
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3537..3549
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3544..3562
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3556..3571
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3576..3588
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3583..3601
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3595..3610
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3614..3626
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3621..3639
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3633..3648
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3655..3667
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3662..3680
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3674..3691
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3696..3710
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3704..3723
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3717..3732
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3742..3755
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3750..3768
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3762..3777
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3786..3799
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3793..3808
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3810..3823
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3829..3839
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3835..3848
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 3850..3861
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4152..4161
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4157..4170
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4172..4183
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4201..4211
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4205..4221
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4223..4232
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4237..4247
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4241..4257
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4259..4268
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4273..4283
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4277..4293
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4295..4304
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4309..4319
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4313..4329
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4331..4340
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4345..4353
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4348..4364
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4366..4375
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4378..4388
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4382..4398
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DISULFID 4400..4409
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT CONFLICT 2642
FT /note="A -> T (in Ref. 2; AAL09567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4545 AA; 504742 MW; 9904CF5DF5EE333E CRC64;
MLTPPLLLLL PLLSALVSGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG ERDCPDGSDE
APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM DGSDEGAHCR ELRANCSRMG
CQHHCVPTPS GPTCYCNSSF QLQADGKTCK DFDECSVYGT CSQLCTNTDG SFTCGCVEGY
LLQPDNRSCK AKNEPVDRPP VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN
ETVCWVHVGD SAAQTQLKCA RMPGLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD
IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE RCDMDGQNRT
KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK GRQTIIQGIL IEHLYGLTVF
ENYLYATNSD NANTQQKTSV IRVNRFNSTE YQVVTRVDKG GALHIYHQRR QPRVRSHACE
NDQYGKPGGC SDICLLANSH KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR
GMDMGAKVPD EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD
GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH PRAIVVDPLN
GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL WPNGLSLDIP AGRLYWVDAF
YDRIETILLN GTDRKIVYEG PELNHAFGLC HHGNYLFWTE YRSGSVYRLE RGVAGAPPTV
TLLRSERPPI FEIRMYDAQQ QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDTDG
VTCLANPSYV PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR
FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI PISWTCDLDD
DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND NDCGDNSDEA GCSHSCSSTQ
FKCNSGRCIP EHWTCDGDND CGDYSDETHA NCTNQATRPP GGCHSDEFQC RLDGLCIPLR
WRCDGDTDCM DSSDEKSCEG VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN
CEALACRPPS HPCANNTSVC LPPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA
PGEGIVCSCP LGMELGSDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY EGWVLEPDGE
SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT IALDFHLSQS ALYWTDVVED
KIYRGKLLDN GALTSFEVVI QYGLATPEGL AVDWIAGNIY WVESNLDQIE VAKLDGTLRT
TLLAGDIEHP RAIALDPRDG ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL
TVDYLEKRIL WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN
TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC SHLCLINYNR
TVSCACPHLM KLHKDNTTCY EFKKFLLYAR QMEIRGVDLD APYYNYIISF TVPDIDNVTV
LDYDAREQRV YWSDVRTQAI KRAFINGTGV ETVVSADLPN AHGLAVDWVS RNLFWTSYDT
NKKQINVARL DGSFKNAVVQ GLEQPHGLVV HPLRGKLYWT DGDNISMANM DGSNHTLLFS
GQKGPVGLAI DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL
WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP CSVNNGDCSQ
LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE GIRGIPLDPN DKSDALVPVS
GTSLAVGIDF HAENDTIYWV DMGLSTISRA KRDQTWREDV VTNGIGRVEG IAVDWIAGNI
YWTDQGFDVI EVARLNGSFR YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD
GTERVVLVNV SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF
SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN RDRQKGTNVC
AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG YLLYSERTIL KSIHLSDERN
LNAPVQPFED PEHMKNVIAL AFDYRAGTSP GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV
ENVGSVEGLA YHRGWDTLYW TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL
DECQNLMFWT NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD
KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV GSDMKLLRVD
IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG HVNCSCRGGR ILQEDFTCRA
VNSSCRAQDE FECANGECIS FSLTCDGVSH CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV
SNMLWCNGVD DCGDGSDEIP CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC
SATDCSSYFR LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN
YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK QWLCDGSDDC
GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD CTDGADESVT AGCLYNSTCD
DREFMCQNRL CIPKHFVCDH DRDCADGSDE SPECEYPTCG PNEFRCANGR CLSSRQWECD
GENDCHDHSD EAPKNPHCTS PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC
HVNECLSRKL SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADLDECSTT FPCSQLCINT
HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY TLLKQGLNNA
VALDFDYREQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT GLSNPDGLAV DWVGGNLYWC
DKGRDTIEVS KLNGAYRTVL VSSGLREPRA LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG
RSIIVDTKIT WPNGLTVDYV TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL
FEDYVYWTDW ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG
GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF WWKCDTEDDC
GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC QDNSDEANCD IHVCLPSQFK
CTNTNRCIPG IFRCNGQDNC GDGEDERDCP EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC
VDGSDEPANC TQMTCGVDEF RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY
QFRCKNNRCV PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD
CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT GVRTCPLDEF
QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CARFICPPNR PFRCKNDRVC LWIGRQCDGV
DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC RNQRCLSSSL RCNMFDDCGD GSDEEDCSID
PKLTSCATNA SMCGDEARCV RTEKAAYCAC RSGFHTVPGQ PGCQDINECL RFGTCSQLCN
NTKGGHLCSC ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQTFQGDES
VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV THLNISGLKM
PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM IDEPHAIVVD PLRGTMYWSD
WGNHPKIETA AMDGTLRETL VQDNIQWPTG LAVDYHNERL YWADAKLSVI GSIRLNGTDP
IVAADSKRGL SHPFSIDVFE DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY
HQHKQPEVTN PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT
CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS PSGMPTCRCP
TGFTGPKCTA QVCAGYCSNN STCTVNQGNQ PQCRCLPGFL GDRCQYRQCS GFCENFGTCQ
MAADGSRQCR CTVYFEGPRC EVNKCSRCLQ GACVVNKQTG DVTCNCTDGR VAPSCLTCID
HCSNGGSCTM NSKMMPECQC PPHMTGPRCE EQVVSQQQPG HMASILIPLL LLLLLLLVAG
VVFWYKRRVR GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP
TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA
