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P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P)

 LYAM3_HUMAN             Reviewed;         830 AA.
P16109; Q5R344; Q8IVD1;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
22-NOV-2017, entry version 211.
RecName: Full=P-selectin;
AltName: Full=CD62 antigen-like family member P;
AltName: Full=Granule membrane protein 140;
Short=GMP-140;
AltName: Full=Leukocyte-endothelial cell adhesion molecule 3;
Short=LECAM3;
AltName: Full=Platelet activation dependent granule-external membrane protein;
Short=PADGEM;
AltName: CD_antigen=CD62P;
Flags: Precursor;
Name=SELP; Synonyms=GMRP, GRMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS ILE-274 AND
ASN-603.
PubMed=2466574; DOI=10.1016/0092-8674(89)90636-3;
Johnston G.I., Cook R.G., McEver R.P.;
"Cloning of GMP-140, a granule membrane protein of platelets and
endothelium: sequence similarity to proteins involved in cell adhesion
and inflammation.";
Cell 56:1033-1044(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-179; MET-209;
PHE-230; ILE-274; ASN-331; LEU-385; LYS-542; ASN-603; ALA-619;
VAL-631; VAL-640; ASN-661; SER-673 AND PRO-756.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-640.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-640.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
PALMITOYLATION AT CYS-807, AND STEAROYLATION AT CYS-807.
PubMed=7684381;
Fujimoto T., Stroud E., Whatley R.E., Prescott S.M., Muszbek L.,
Laposata M., McEver R.P.;
"P-selectin is acylated with palmitic acid and stearic acid at
cysteine 766 through a thioester linkage.";
J. Biol. Chem. 268:11394-11400(1993).
[6]
INTERACTION WITH SELPLG.
PubMed=7585949; DOI=10.1016/0092-8674(95)90173-6;
Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A.,
Shaw G.D.;
"A sulfated peptide segment at the amino terminus of PSGL-1 is
critical for P-selectin binding.";
Cell 83:323-331(1995).
[7]
INTERACTION WITH SELPLG, AND FUNCTION.
PubMed=7585950; DOI=10.1016/0092-8674(95)90174-4;
Pouyani T., Seed B.;
"PSGL-1 recognition of P-selectin is controlled by a tyrosine
sulfation consensus at the PSGL-1 amino terminus.";
Cell 83:333-343(1995).
[8]
INTERACTION WITH SELPLG.
PubMed=7559387; DOI=10.1074/jbc.270.39.22677;
Wilkins P.P., Moore K.L., McEver R.P., Cummings R.D.;
"Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required
for high affinity binding to P-selectin.";
J. Biol. Chem. 270:22677-22680(1995).
[9]
INTERACTION WITH SNX17.
PubMed=11237770; DOI=10.1006/bbrc.2001.4467;
Florian V., Schlueter T., Bohnensack R.;
"A new member of the sorting nexin family interacts with the C-
terminus of P-selectin.";
Biochem. Biophys. Res. Commun. 281:1045-1050(2001).
[10]
INTERACTION WITH SNX17.
PubMed=15769472; DOI=10.1016/j.jmb.2005.02.004;
Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V.,
Schreckenberger S., Hahn H., Bohnensack R.;
"Functions of sorting nexin 17 domains and recognition motif for P-
selectin trafficking.";
J. Mol. Biol. 347:813-825(2005).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-54.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[12]
INTERACTION WITH PODXL2.
PubMed=18606703; DOI=10.4049/jimmunol.181.2.1480;
Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D.;
"Endoglycan, a member of the CD34 family of sialomucins, is a ligand
for the vascular selectins.";
J. Immunol. 181:1480-1490(2008).
[13]
STRUCTURE BY NMR OF 160-199.
PubMed=8901515; DOI=10.1021/bi9610257;
Freedman S.J., Sanford D.G., Bachovchin W.W., Furie B.C., Baleja J.D.,
Furie B.;
"Structure and function of the epidermal growth factor domain of P-
selectin.";
Biochemistry 35:13733-13744(1996).
[14]
3D-STRUCTURE MODELING OF 42-161.
PubMed=7505680; DOI=10.1002/pro.5560021103;
Bajorath J., Stenkamp R., Aruffo A.;
"Knowledge-based model building of proteins: concepts and examples.";
Protein Sci. 2:1798-1810(1993).
[15]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-198 IN COMPLEX WITH
CALCIUM IONS AND SELPLG, SUBUNIT, AND DISULFIDE BONDS AT
60-CYS--CYS-158; 131-CYS--CYS-150; 163-CYS--CYS-183 AND
185-CYS--CYS-194.
PubMed=11081633; DOI=10.1016/S0092-8674(00)00138-0;
Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
"Insights into the molecular basis of leukocyte tethering and rolling
revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-
1.";
Cell 103:467-479(2000).
[16]
ERRATUM.
Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
Cell 105:971-971(2001).
[17]
VARIANTS ASN-331; ASN-603; VAL-640 AND PRO-756.
PubMed=9668170; DOI=10.1093/hmg/7.8.1277;
Herrmann S.M., Ricard S., Nicaud V., Mallet C., Evans A.,
Ruidavets J.B., Arveiler D., Luc G., Cambien F.;
"The P-selectin gene is highly polymorphic: reduced frequency of the
Pro715 allele carriers in patients with myocardial infarction.";
Hum. Mol. Genet. 7:1277-1284(1998).
[18]
VARIANTS MET-209; LEU-301; ASN-331; VAL-365; PHE-500; ASN-603; VAL-640
AND PRO-756.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[19]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[20]
ASSOCIATION OF VARIANT VAL-640 WITH SUSCEPTIBILITY TO ISCHSTR.
PubMed=14681304; DOI=10.1093/hmg/ddh039;
Zee R.Y.L., Cook N.R., Cheng S., Reynolds R., Erlich H.A.,
Lindpaintner K., Ridker P.M.;
"Polymorphism in the P-selectin and interleukin-4 genes as
determinants of stroke: a population-based, prospective genetic
analysis.";
Hum. Mol. Genet. 13:389-396(2004).
-!- FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds
to carbohydrates on neutrophils and monocytes. Mediates the
interaction of activated endothelial cells or platelets with
leukocytes. The ligand recognized is sialyl-Lewis X. Mediates
rapid rolling of leukocyte rolling over vascular surfaces during
the initial steps in inflammation through interaction with PSGL1.
{ECO:0000269|PubMed:7585950}.
-!- SUBUNIT: Interacts with SNX17. Interacts with PSGL1/SEPL and
PODXL2 and mediates neutrophil adhesion and leukocyte rolling.
This interaction requires the sialyl-Lewis X epitope of PSGL1 and
PODXL2, and specific tyrosine sulfation on PSGL1.
{ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:11237770,
ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:18606703,
ECO:0000269|PubMed:7559387, ECO:0000269|PubMed:7585949,
ECO:0000269|PubMed:7585950}.
-!- INTERACTION:
Q14242:SELPLG; NbExp=4; IntAct=EBI-1030170, EBI-1030190;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Stored in the alpha-granules of platelets and
Weibel-Palade bodies of endothelial cells. Upon cell activation by
agonists, P-selectin is transported rapidly to the cell surface.
-!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an
acute neurologic event leading to death of neural tissue of the
brain and resulting in loss of motor, sensory and/or cognitive
function. Ischemic strokes, resulting from vascular occlusion, is
considered to be a highly complex disease consisting of a group of
heterogeneous disorders with multiple genetic and environmental
risk factors. {ECO:0000269|PubMed:14681304}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/selp/";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=P-selectin;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_354";
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EMBL; M60234; AAA35910.1; -; Genomic_DNA.
EMBL; M60217; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60218; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60219; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60222; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60223; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60224; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60225; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60226; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60227; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60228; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60229; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60231; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60232; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M60233; AAA35910.1; JOINED; Genomic_DNA.
EMBL; M25322; AAA35911.1; -; mRNA.
EMBL; AF542391; AAN06828.1; -; Genomic_DNA.
EMBL; AL022146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z99572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW90851.1; -; Genomic_DNA.
CCDS; CCDS1282.1; -.
PIR; A30359; A30359.
RefSeq; NP_002996.2; NM_003005.3.
RefSeq; XP_005245492.1; XM_005245435.1.
RefSeq; XP_005245493.1; XM_005245436.3.
UniGene; Hs.73800; -.
PDB; 1FSB; NMR; -; A=160-199.
PDB; 1G1Q; X-ray; 2.40 A; A/B/C/D=42-198.
PDB; 1G1R; X-ray; 3.40 A; A/B/C/D=42-198.
PDB; 1G1S; X-ray; 1.90 A; A/B=42-198.
PDB; 1HES; X-ray; 3.00 A; P=813-830.
PDB; 1KJD; Model; -; A=42-161.
PDBsum; 1FSB; -.
PDBsum; 1G1Q; -.
PDBsum; 1G1R; -.
PDBsum; 1G1S; -.
PDBsum; 1HES; -.
PDBsum; 1KJD; -.
ProteinModelPortal; P16109; -.
SMR; P16109; -.
BioGrid; 112303; 9.
DIP; DIP-37667N; -.
ELM; P16109; -.
IntAct; P16109; 2.
STRING; 9606.ENSP00000263686; -.
BindingDB; P16109; -.
ChEMBL; CHEMBL5378; -.
DrugBank; DB06779; Dalteparin.
DrugBank; DB01109; Heparin.
DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DrugBank; DB08813; Nadroparin.
iPTMnet; P16109; -.
PhosphoSitePlus; P16109; -.
SwissPalm; P16109; -.
BioMuta; SELP; -.
DMDM; 215274139; -.
PaxDb; P16109; -.
PeptideAtlas; P16109; -.
PRIDE; P16109; -.
Ensembl; ENST00000263686; ENSP00000263686; ENSG00000174175.
GeneID; 6403; -.
KEGG; hsa:6403; -.
UCSC; uc001ggi.5; human.
CTD; 6403; -.
DisGeNET; 6403; -.
EuPathDB; HostDB:ENSG00000174175.16; -.
GeneCards; SELP; -.
HGNC; HGNC:10721; SELP.
HPA; CAB002145; -.
HPA; HPA002655; -.
HPA; HPA005990; -.
MalaCards; SELP; -.
MIM; 173610; gene+phenotype.
MIM; 601367; phenotype.
neXtProt; NX_P16109; -.
PharmGKB; PA35643; -.
eggNOG; ENOG410IS44; Eukaryota.
eggNOG; ENOG410Y5JF; LUCA.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P16109; -.
KO; K06496; -.
OrthoDB; EOG091G00VV; -.
PhylomeDB; P16109; -.
TreeFam; TF326910; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
SIGNOR; P16109; -.
EvolutionaryTrace; P16109; -.
GeneWiki; P-selectin; -.
GenomeRNAi; 6403; -.
PRO; PR:P16109; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000174175; -.
CleanEx; HS_SELP; -.
ExpressionAtlas; P16109; baseline and differential.
Genevisible; P16109; HS.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031092; C:platelet alpha granule membrane; IDA:MGI.
GO; GO:0031088; C:platelet dense granule membrane; TAS:Reactome.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0042806; F:fucose binding; IDA:BHF-UCL.
GO; GO:0043208; F:glycosphingolipid binding; TAS:BHF-UCL.
GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
GO; GO:0001530; F:lipopolysaccharide binding; IMP:BHF-UCL.
GO; GO:0070492; F:oligosaccharide binding; IDA:BHF-UCL.
GO; GO:0033691; F:sialic acid binding; IDA:BHF-UCL.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IC:BHF-UCL.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0010572; P:positive regulation of platelet activation; ISS:BHF-UCL.
GO; GO:0033623; P:regulation of integrin activation; IMP:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IC:BHF-UCL.
CDD; cd00033; CCP; 9.
CDD; cd03592; CLECT_selectins_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR033991; Selectin_CTLD.
InterPro; IPR002396; Selectin_superfamily.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 9.
PRINTS; PR00343; SELECTIN.
SMART; SM00032; CCP; 9.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57535; SSF57535; 9.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50923; SUSHI; 9.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Lectin; Lipoprotein; Membrane;
Palmitate; Polymorphism; Reference proteome; Repeat; Signal; Sushi;
Transmembrane; Transmembrane helix.
SIGNAL 1 41
CHAIN 42 830 P-selectin.
/FTId=PRO_0000017498.
TOPO_DOM 42 771 Extracellular. {ECO:0000255}.
TRANSMEM 772 795 Helical. {ECO:0000255}.
TOPO_DOM 796 830 Cytoplasmic. {ECO:0000255}.
DOMAIN 58 158 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 159 195 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 198 259 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 260 321 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 322 383 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 384 445 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 446 507 Sushi 5. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 508 569 Sushi 6. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 570 631 Sushi 7. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 640 701 Sushi 8. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 702 763 Sushi 9. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 821 830 Interaction with SNX17.
MOTIF 818 821 Endocytosis signal. {ECO:0000305}.
LIPID 807 807 S-palmitoyl cysteine; alternate.
{ECO:0000269|PubMed:7684381}.
LIPID 807 807 S-stearoyl cysteine; alternate.
{ECO:0000269|PubMed:7684381}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 411 411 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 665 665 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 716 716 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 723 723 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 741 741 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 158 {ECO:0000250}.
DISULFID 131 150 {ECO:0000250}.
DISULFID 163 174
DISULFID 168 183
DISULFID 185 194 {ECO:0000269|PubMed:11081633}.
DISULFID 200 244 {ECO:0000250}.
DISULFID 230 257 {ECO:0000250}.
DISULFID 262 306 {ECO:0000250}.
DISULFID 292 319 {ECO:0000250}.
DISULFID 324 368 {ECO:0000250}.
DISULFID 354 381 {ECO:0000250}.
DISULFID 386 430 {ECO:0000250}.
DISULFID 416 443 {ECO:0000250}.
DISULFID 448 492 {ECO:0000250}.
DISULFID 478 505 {ECO:0000250}.
DISULFID 510 554 {ECO:0000250}.
DISULFID 540 567 {ECO:0000250}.
DISULFID 572 616 {ECO:0000250}.
DISULFID 602 629 {ECO:0000250}.
DISULFID 642 686 {ECO:0000250}.
DISULFID 672 699 {ECO:0000250}.
DISULFID 704 748 {ECO:0000250}.
DISULFID 734 761 {ECO:0000250}.
VARIANT 179 179 G -> R (in dbSNP:rs3917718).
{ECO:0000269|Ref.2}.
/FTId=VAR_019381.
VARIANT 209 209 V -> M (in dbSNP:rs6125).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.2}.
/FTId=VAR_013910.
VARIANT 230 230 C -> F (in dbSNP:rs3917869).
{ECO:0000269|Ref.2}.
/FTId=VAR_019382.
VARIANT 274 274 T -> I (in dbSNP:rs3917724).
{ECO:0000269|PubMed:2466574,
ECO:0000269|Ref.2}.
/FTId=VAR_019383.
VARIANT 301 301 P -> L (in dbSNP:rs6124).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013911.
VARIANT 331 331 S -> N (in dbSNP:rs6131).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:9668170,
ECO:0000269|Ref.2}.
/FTId=VAR_004192.
VARIANT 365 365 M -> V (in dbSNP:rs6134).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013912.
VARIANT 385 385 S -> L (in dbSNP:rs3917742).
{ECO:0000269|Ref.2}.
/FTId=VAR_019384.
VARIANT 500 500 S -> F (in dbSNP:rs6130).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013913.
VARIANT 542 542 E -> K (in dbSNP:rs3917769).
{ECO:0000269|Ref.2}.
/FTId=VAR_019385.
VARIANT 603 603 D -> N (in dbSNP:rs6127).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:2466574,
ECO:0000269|PubMed:9668170,
ECO:0000269|Ref.2}.
/FTId=VAR_004193.
VARIANT 619 619 S -> A (in dbSNP:rs2228672).
{ECO:0000269|Ref.2}.
/FTId=VAR_019386.
VARIANT 631 631 G -> V (in dbSNP:rs3917812).
{ECO:0000269|Ref.2}.
/FTId=VAR_019387.
VARIANT 640 640 L -> V (associated with susceptibility to
ischemic stroke; dbSNP:rs6133).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:9668170,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_004194.
VARIANT 661 661 T -> N (in dbSNP:rs3917814).
{ECO:0000269|Ref.2}.
/FTId=VAR_019388.
VARIANT 673 673 N -> S (in dbSNP:rs3917815).
{ECO:0000269|Ref.2}.
/FTId=VAR_019389.
VARIANT 756 756 T -> P (reduced frequency in patients
with myocardial infarction;
dbSNP:rs6136).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:9668170,
ECO:0000269|Ref.2}.
/FTId=VAR_004195.
STRAND 43 46 {ECO:0000244|PDB:1G1S}.
HELIX 53 63 {ECO:0000244|PDB:1G1S}.
STRAND 64 67 {ECO:0000244|PDB:1G1S}.
HELIX 73 82 {ECO:0000244|PDB:1G1S}.
STRAND 90 97 {ECO:0000244|PDB:1G1S}.
STRAND 100 103 {ECO:0000244|PDB:1G1S}.
TURN 104 106 {ECO:0000244|PDB:1G1S}.
TURN 112 114 {ECO:0000244|PDB:1G1S}.
STRAND 131 134 {ECO:0000244|PDB:1G1S}.
STRAND 139 141 {ECO:0000244|PDB:1G1S}.
STRAND 145 148 {ECO:0000244|PDB:1G1S}.
STRAND 154 160 {ECO:0000244|PDB:1G1S}.
HELIX 167 170 {ECO:0000244|PDB:1G1S}.
STRAND 171 176 {ECO:0000244|PDB:1G1S}.
STRAND 178 185 {ECO:0000244|PDB:1G1S}.
STRAND 189 191 {ECO:0000244|PDB:1G1S}.
SEQUENCE 830 AA; 90834 MW; F53BC476AB6F70AC CRC64;
MANCQIAILY QRFQRVVFGI SQLLCFSALI SELTNQKEVA AWTYHYSTKA YSWNISRKYC
QNRYTDLVAI QNKNEIDYLN KVLPYYSSYY WIGIRKNNKT WTWVGTKKAL TNEAENWADN
EPNNKRNNED CVEIYIKSPS APGKWNDEHC LKKKHALCYT ASCQDMSCSK QGECLETIGN
YTCSCYPGFY GPECEYVREC GELELPQHVL MNCSHPLGNF SFNSQCSFHC TDGYQVNGPS
KLECLASGIW TNKPPQCLAA QCPPLKIPER GNMTCLHSAK AFQHQSSCSF SCEEGFALVG
PEVVQCTASG VWTAPAPVCK AVQCQHLEAP SEGTMDCVHP LTAFAYGSSC KFECQPGYRV
RGLDMLRCID SGHWSAPLPT CEAISCEPLE SPVHGSMDCS PSLRAFQYDT NCSFRCAEGF
MLRGADIVRC DNLGQWTAPA PVCQALQCQD LPVPNEARVN CSHPFGAFRY QSVCSFTCNE
GLLLVGASVL QCLATGNWNS VPPECQAIPC TPLLSPQNGT MTCVQPLGSS SYKSTCQFIC
DEGYSLSGPE RLDCTRSGRW TDSPPMCEAI KCPELFAPEQ GSLDCSDTRG EFNVGSTCHF
SCDNGFKLEG PNNVECTTSG RWSATPPTCK GIASLPTPGL QCPALTTPGQ GTMYCRHHPG
TFGFNTTCYF GCNAGFTLIG DSTLSCRPSG QWTAVTPACR AVKCSELHVN KPIAMNCSNL
WGNFSYGSIC SFHCLEGQLL NGSAQTACQE NGHWSTTVPT CQAGPLTIQE ALTYFGGAVA
STIGLIMGGT LLALLRKRFR QKDDGKCPLN PHSHLGTYGV FTNAAFDPSP


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