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Cation-independent mannose-6-phosphate receptor (CI Man-6-P receptor) (CI-MPR) (M6PR) (300 kDa mannose 6-phosphate receptor) (MPR 300) (Insulin-like growth factor 2 receptor) (Insulin-like growth factor II receptor) (IGF-II receptor) (M6P/IGF2 receptor) (M6P/IGF2R) (CD antigen CD222)

 MPRI_MOUSE              Reviewed;        2483 AA.
Q07113; Q61822; Q6LED1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 162.
RecName: Full=Cation-independent mannose-6-phosphate receptor;
Short=CI Man-6-P receptor;
Short=CI-MPR;
Short=M6PR;
AltName: Full=300 kDa mannose 6-phosphate receptor;
Short=MPR 300;
AltName: Full=Insulin-like growth factor 2 receptor;
AltName: Full=Insulin-like growth factor II receptor;
Short=IGF-II receptor;
AltName: Full=M6P/IGF2 receptor;
Short=M6P/IGF2R;
AltName: CD_antigen=CD222;
Flags: Precursor;
Name=Igf2r;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8188212; DOI=10.1006/geno.1994.1021;
Szebenyi G., Rotwein P.;
"The mouse insulin-like growth factor II/cation-independent mannose 6-
phosphate (IGF-II/MPR) receptor gene: molecular cloning and genomic
organization.";
Genomics 19:120-129(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=8194771; DOI=10.1016/0378-1119(94)90282-8;
Ludwig T., Tenscher K., Remmler J., Hoflack B., Lobel P.;
"Cloning and sequencing of cDNAs encoding the full-length mouse
mannose 6-phosphate/insulin-like growth factor II receptor.";
Gene 142:311-312(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 AND 93-106.
STRAIN=129, and C57BL/6J;
PubMed=8462104; DOI=10.1016/0092-8674(93)90160-R;
Stoger R., Kubicka P., Liu C.G., Kafri T., Razin A., Cedar H.,
Barlow D.P.;
"Maternal-specific methylation of the imprinted mouse Igf2r locus
identifies the expressed locus as carrying the imprinting signal.";
Cell 73:61-71(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
STRAIN=129/Sv;
PubMed=8584025; DOI=10.1210/mend.9.11.8584025;
Liu Z., Mittanck D.W., Kim S., Rotwein P.;
"Control of insulin-like growth factor-II/mannose 6-phosphate receptor
gene transcription by proximal promoter elements.";
Mol. Endocrinol. 9:1477-1487(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 435-488.
TISSUE=Liver;
PubMed=1848553;
Szebenyi G., Rotwein P.;
"Differential regulation of mannose 6-phosphate receptors and their
ligands during the myogenic development of C2 cells.";
J. Biol. Chem. 266:5534-5539(1991).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1625-2045.
STRAIN=C57BL/6J;
Matzner U.;
Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2249-2483.
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=8226743;
Chen H.J., Remmler J., Delaney J.C., Messner D.J., Lobel P.;
"Mutational analysis of the cation-independent mannose 6-
phosphate/insulin-like growth factor II receptor. A consensus casein
kinase II site followed by 2 leucines near the carboxyl terminus is
important for intracellular targeting of lysosomal enzymes.";
J. Biol. Chem. 268:22338-22346(1993).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2471 AND SER-2476, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1532.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-740; ASN-1532 AND
ASN-1750.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401; SER-2471 AND
SER-2476, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2417, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Acts as a positive regulator of T-cell coactivation, by
binding DPP4 (By similarity). Transport of phosphorylated
lysosomal enzymes from the Golgi complex and the cell surface to
lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind
specifically to mannose-6-phosphate receptors in the Golgi
apparatus and the resulting receptor-ligand complex is transported
to an acidic prelyosomal compartment where the low pH mediates the
dissociation of the complex. This receptor also binds IGF2.
{ECO:0000250}.
-!- SUBUNIT: Interacts with DPP4; the interaction is direct. Binds
GGA1, GGA2 and GGA3. Binds HA-I and HA-II plasma membrane adapters
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I
membrane protein.
-!- DOMAIN: Contains 15 repeating units of approximately 147 AA
harboring four disulfide bonds each. The most highly conserved
region within the repeat consists of a stretch of 13 AA that
contains cysteines at both ends.
-!- SIMILARITY: Belongs to the MRL1/IGF2R family. {ECO:0000305}.
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EMBL; L22143; AAA39320.1; -; Genomic_DNA.
EMBL; L22096; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22097; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22098; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22099; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22100; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22101; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22102; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22103; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22104; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22105; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22106; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22107; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22108; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22109; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22110; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22111; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22112; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22113; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22114; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22115; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22116; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22117; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22118; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22119; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22120; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22121; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22122; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22123; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22124; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22125; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22126; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22127; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22128; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22129; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22130; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22131; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22132; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22133; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22134; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22135; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22136; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22137; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22138; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22139; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22140; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22141; AAA39320.1; JOINED; Genomic_DNA.
EMBL; L22142; AAA39320.1; JOINED; Genomic_DNA.
EMBL; U04710; AAA19568.1; -; mRNA.
EMBL; L06445; AAA37921.1; -; Genomic_DNA.
EMBL; L06446; AAA37922.1; -; Genomic_DNA.
EMBL; U26348; AAA98844.1; -; Genomic_DNA.
EMBL; M58586; AAA39483.1; -; Genomic_DNA.
EMBL; X60389; CAA42940.1; -; mRNA.
EMBL; L19500; AAA16037.1; -; mRNA.
CCDS; CCDS37436.1; -.
PIR; A49617; A49617.
PIR; I48922; I48922.
RefSeq; NP_034645.2; NM_010515.2.
UniGene; Mm.26553; -.
UniGene; Mm.486511; -.
ProteinModelPortal; Q07113; -.
SMR; Q07113; -.
BioGrid; 200550; 2.
IntAct; Q07113; 6.
MINT; MINT-200350; -.
STRING; 10090.ENSMUSP00000024599; -.
iPTMnet; Q07113; -.
PhosphoSitePlus; Q07113; -.
SwissPalm; Q07113; -.
EPD; Q07113; -.
MaxQB; Q07113; -.
PaxDb; Q07113; -.
PeptideAtlas; Q07113; -.
PRIDE; Q07113; -.
Ensembl; ENSMUST00000024599; ENSMUSP00000024599; ENSMUSG00000023830.
GeneID; 16004; -.
KEGG; mmu:16004; -.
UCSC; uc008aky.1; mouse.
CTD; 3482; -.
MGI; MGI:96435; Igf2r.
eggNOG; KOG4504; Eukaryota.
eggNOG; ENOG410ZWHP; LUCA.
GeneTree; ENSGT00390000013943; -.
HOGENOM; HOG000113638; -.
HOVERGEN; HBG000334; -.
InParanoid; Q07113; -.
KO; K06564; -.
OMA; VDCQVTD; -.
OrthoDB; EOG091G116D; -.
PhylomeDB; Q07113; -.
TreeFam; TF328963; -.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
PRO; PR:Q07113; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023830; -.
CleanEx; MM_IGF2R; -.
ExpressionAtlas; Q07113; baseline and differential.
Genevisible; Q07113; MM.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030118; C:clathrin coat; IEA:Ensembl.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
GO; GO:0004930; F:G-protein coupled receptor activity; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005520; F:insulin-like growth factor binding; IPI:MGI.
GO; GO:0031995; F:insulin-like growth factor II binding; IEA:Ensembl.
GO; GO:0005537; F:mannose binding; IDA:MGI.
GO; GO:0051219; F:phosphoprotein binding; ISS:UniProtKB.
GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
CDD; cd00062; FN2; 1.
Gene3D; 2.70.130.10; -; 15.
InterPro; IPR000479; CIMR.
InterPro; IPR000562; FN_type2_col-bd.
InterPro; IPR013806; Kringle-like.
InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom.
Pfam; PF00878; CIMR; 14.
Pfam; PF00040; fn2; 1.
SMART; SM01404; CIMR; 14.
SMART; SM00059; FN2; 1.
SUPFAM; SSF50911; SSF50911; 16.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Disulfide bond; Glycoprotein;
Lysosome; Membrane; Methylation; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 2483 Cation-independent mannose-6-phosphate
receptor.
/FTId=PRO_0000019230.
TOPO_DOM 36 2295 Lumenal. {ECO:0000255}.
TRANSMEM 2296 2316 Helical. {ECO:0000255}.
TOPO_DOM 2317 2483 Cytoplasmic. {ECO:0000255}.
REPEAT 35 184 1.
REPEAT 185 339 2.
REPEAT 340 484 3.
REPEAT 485 637 4.
REPEAT 638 776 5.
REPEAT 777 943 6.
REPEAT 945 1092 7.
REPEAT 1093 1236 8.
REPEAT 1237 1377 9.
REPEAT 1378 1525 10.
REPEAT 1526 1659 11.
REPEAT 1660 1813 12.
REPEAT 1814 2001 13.
DOMAIN 1891 1937 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 2002 2130 14.
REPEAT 2158 2282 15.
MOD_RES 2342 2342 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11717}.
MOD_RES 2401 2401 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 2417 2417 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 2471 2471 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 2476 2476 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 537 537 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 575 575 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 620 620 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 740 740 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 864 864 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 944 944 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1157 1157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1239 1239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1305 1305 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1358 1358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1423 1423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1532 1532 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CARBOHYD 1649 1649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1750 1750 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 1809 1809 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2078 2078 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2129 2129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 64 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 72 79 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 112 144 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 129 156 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 169 207 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 223 230 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 270 301 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 283 313 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 323 361 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 369 377 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 415 449 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 429 461 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 621 658 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 666 673 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 724 753 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1509 1546 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1552 1559 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1591 1627 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1607 1639 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1645 1688 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1699 1706 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1743 1776 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1759 1788 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1797 1832 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1843 1849 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1886 1968 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1896 1920 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1910 1935 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1950 1980 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1987 2022 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 2032 2039 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 2075 2106 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 2089 2118 {ECO:0000255|PROSITE-ProRule:PRU00479}.
CONFLICT 10 11 PS -> RP (in Ref. 2). {ECO:0000305}.
CONFLICT 13 13 Missing (in Ref. 2). {ECO:0000305}.
CONFLICT 209 209 D -> V (in Ref. 2; AAA19568).
{ECO:0000305}.
CONFLICT 456 457 DT -> VS (in Ref. 2). {ECO:0000305}.
CONFLICT 1626 1631 TCTLFF -> GSTFFS (in Ref. 6; CAA42940).
{ECO:0000305}.
CONFLICT 1694 1695 MH -> TC (in Ref. 6; CAA42940).
{ECO:0000305}.
CONFLICT 1699 1699 C -> R (in Ref. 6; CAA42940).
{ECO:0000305}.
CONFLICT 1759 1759 C -> Y (in Ref. 2; AAA19568).
{ECO:0000305}.
CONFLICT 2028 2028 G -> V (in Ref. 6; CAA42940).
{ECO:0000305}.
CONFLICT 2032 2032 C -> S (in Ref. 6; CAA42940).
{ECO:0000305}.
SEQUENCE 2483 AA; 273815 MW; 8F64F6189FD05CD1 CRC64;
MRAVQLGPVP SGPRVALLPP LLLLLLLAAA GSAQAQAVDL DALCSYTWEA VDSKNNAVYK
INVCGNVGIS SCGPTSAICM CDLKTENCRS VGDSLLRSSA RSLLEFNTTM GCQPSDSQHR
IQTSITFLCG KTLGTPEFVT ATDCVHYFEW RTTAACKKDI FKADKEVPCY AFDDKLQKHD
LNPLIKLNGG YLVDDSDPDT SLFINVCRDI DSLRDPSTQL RVCPAGTAAC LLKGNQAFDV
GRPKEGLKLL SKDRLVLTYV KEEGEKPDFC NGHSPAVTVT FVCPSERREG TIPKLTAKSN
CRYEVEWITE YACHRDYLQS ESCSLSSEQH DITIDLSPLA QYGGSPYVSD GREYTFFINV
CGDTKVSLCN NKEAAVCQEK KADSTQVKIA GRHQNQTLRY SDGDLTLIYS GGDECSSGFQ
RMSVINFECN KTAGKDGRGE PVFTGEVDCT YFFTWDTKYA CIKEKEDLLC GAINGKKRYD
LSVLARHSES EQNWEAVDGS QAESEKYFFI NVCHRVLQEG KARNCPEDAA VCAVDKNGSK
NLGKFVSSPT KEKGHIQLSY TDGDDCGSDK KISTNITLVC KPGDLESAPV LRAARSDGCF
YEFEWHTAAA CVLSKTEGEN CTVLDAQAGF SFDLSLLTKK NGAYKVETEK YDFYINVCGP
VSMDPCQSNS GACQVAKSGK SWNLGLSSTK LTYYDGMIQL SYRNGTPYNN EKHTPRATLI
TFLCDRDAGV GFPEYQEEDN STYNFRWYTS YACPEEPLEC MVTDPSMMEQ YDLSSLVKSE
GGSGGNWYAM ENSREHVTRR KYYLNVCRPL NPVPGCDRYA SACQMKYENH EGSLAETVSI
SNLGVAKIGP VVEESGSLLL EYVNGSACTT SDGQLTTYST RIHLVCGRGF MNSHPIFTFN
WECVVSFLWN TEAACPIQTI TETDQACSIR DPSSGFVFNL SPLNDSAQGH VVLGIGKTFV
FNICGAMPAC GTVAGKPAYG CEAETQIEDI KDLRPQRPVG MERSLQLSAE GFLTLTYKGS
SPSDRGTAFI IRFICNDDIY PGAPKFLHQD IDSTRGIRNT YFEFETALAC TPSLVDCQVT
DPAGNEYDLS ALSMVRKPWT AVDTSAYGKR RHFYLSVCNP LPYIPGCHGI ALGSCMVSED
NSFNLGVVQI SPQATGNGSL SILYVNGDRC GDQRFSTRIV FECAQTSGSP MFQFVNNCEY
VFVWRTVEAC PVIREEGDNC QVKDPRHGNL YDLKPLGLND TIVSVGEYTY YLRVCGKLSS
DVCSAHDGSK AVSSCQEKKG PQGFQKVAGL LSQKLTFENG LLKMNYTGGD TCHKVYQRST
TIYFYCDRTT QKPVFLKETS DCSYMFEWRT QYACPPFNVT ECSVQDAAGN SIDLSSLSRY
SDNWEAVTRT GATEHYLINV CKSLSPHAGT EPCPPEAAVC LLNGSKPVNL GKVRDGPQWT
DGVTVLQYVD GDLCPDKIRR RSTIIRFTCS DNQVNSRPLF ISAVQDCEYT FSWPTPSACP
VKSNTHDDCQ VTNPSTGHLF DLSSLSGRAG INASYSEKGL VFMSICEENE NCGPGVGACF
GQTRISVGKA SKRLSYKDQV LQLVYENGSP CPSLSDLRYK SVISFVCRPE AGPTNRPMLI
SLDKQTCTLF FSWHTPLACE QATECTVRNG SSIIDLSPLI HRTGGYEAYD ESEDDTSDTT
PDFYINICQP LNPMHGVPCP AGASVCKVPV DGPPIDIGRV TGPPIFNPVA NEVYLNFESS
THCLADRYMN YTSLITFHCK RGVSMGTPKL IRTNDCDFVF EWETPIVCPD EVKTQGCAVT
DEQLLYSFNL TSLSTSTFKV TRDARTYSIG VCTAAAGLGQ EGCKDGGVCL LSGNKGASFG
RLASMQLDYR HQDEAVILSY VNGDPCPPET DDGEPCVFPF IYKGKSYDEC VLEGRAKLWC
SKTANYDRDH EWGFCRQTNS YRMSAIIFTC DESEDIGRPQ VFSEDRGCEV TFEWKTKVVC
PPKKMECKFV QKHKTYDLRL LSSLTGSWDF VHEGNSYFIN LCQRVYKGPL DCSERASICK
KSATGQVQVL GLVHTQKLEV IDETVIVTYS KGYPCGGNKT ASSVIELTCA KTVGRPAFKR
FDSVSCTYYF YWYSRAACAV RPQEVTMVNG TLTNPVTGKS FSLGEIYFKL FSASGDMRTN
GDNYLYEIQL SSITSSSYPA CAGANICQVK PNDQHFSRKV GTSDMTKYYV QDGDLDVVFT
SSSKCGKDKT KSVSSTIFFH CDPLVKDGIP EFSHETADCQ YLFSWYTSAV CPLGVDFEDE
SAGPEYKGLS ERSQAVGAVL SLLLVALTGC LLALLLHKKE RRETVINKLT SCCRRSSGVS
YKYSKVSKEE ETDENETEWL MEEIQVPAPR LGKDGQENGH ITTKAVKAEA LSSLHGDDQD
SEDEVLTVPE VKVHSGRGAE VESSQPLRNP QRKVLKEREG ERLGLVRGEK ARKGKFRPGQ
RKPTAPAKLV SFHDDSDEDL LHI


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