LYAM3_HUMAN
ID LYAM3_HUMAN Reviewed; 830 AA.
AC P16109; Q5R344; Q8IVD1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=P-selectin;
DE AltName: Full=CD62 antigen-like family member P;
DE AltName: Full=Granule membrane protein 140;
DE Short=GMP-140 {ECO:0000303|PubMed:2466574};
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 3;
DE Short=LECAM3;
DE AltName: Full=Platelet activation dependent granule-external membrane protein;
DE Short=PADGEM;
DE AltName: CD_antigen=CD62P;
DE Flags: Precursor;
GN Name=SELP; Synonyms=GMRP, GRMP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS ILE-274 AND ASN-603.
RX PubMed=2466574; DOI=10.1016/0092-8674(89)90636-3;
RA Johnston G.I., Cook R.G., McEver R.P.;
RT "Cloning of GMP-140, a granule membrane protein of platelets and
RT endothelium: sequence similarity to proteins involved in cell adhesion and
RT inflammation.";
RL Cell 56:1033-1044(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-179; MET-209; PHE-230;
RP ILE-274; ASN-331; LEU-385; LYS-542; ASN-603; ALA-619; VAL-631; VAL-640;
RP ASN-661; SER-673 AND PRO-756.
RG SeattleSNPs variation discovery resource;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-640.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-640.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PALMITOYLATION AT CYS-807, AND STEAROYLATION AT CYS-807.
RX PubMed=7684381; DOI=10.1016/s0021-9258(18)82137-8;
RA Fujimoto T., Stroud E., Whatley R.E., Prescott S.M., Muszbek L.,
RA Laposata M., McEver R.P.;
RT "P-selectin is acylated with palmitic acid and stearic acid at cysteine 766
RT through a thioester linkage.";
RL J. Biol. Chem. 268:11394-11400(1993).
RN [6]
RP INTERACTION WITH SELPLG.
RX PubMed=7585949; DOI=10.1016/0092-8674(95)90173-6;
RA Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A.,
RA Shaw G.D.;
RT "A sulfated peptide segment at the amino terminus of PSGL-1 is critical for
RT P-selectin binding.";
RL Cell 83:323-331(1995).
RN [7]
RP INTERACTION WITH SELPLG, AND FUNCTION.
RX PubMed=7585950; DOI=10.1016/0092-8674(95)90174-4;
RA Pouyani T., Seed B.;
RT "PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation
RT consensus at the PSGL-1 amino terminus.";
RL Cell 83:333-343(1995).
RN [8]
RP INTERACTION WITH SELPLG.
RX PubMed=7559387; DOI=10.1074/jbc.270.39.22677;
RA Wilkins P.P., Moore K.L., McEver R.P., Cummings R.D.;
RT "Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for
RT high affinity binding to P-selectin.";
RL J. Biol. Chem. 270:22677-22680(1995).
RN [9]
RP INTERACTION WITH SNX17.
RX PubMed=11237770; DOI=10.1006/bbrc.2001.4467;
RA Florian V., Schlueter T., Bohnensack R.;
RT "A new member of the sorting nexin family interacts with the C-terminus of
RT P-selectin.";
RL Biochem. Biophys. Res. Commun. 281:1045-1050(2001).
RN [10]
RP INTERACTION WITH SNX17.
RX PubMed=15769472; DOI=10.1016/j.jmb.2005.02.004;
RA Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V.,
RA Schreckenberger S., Hahn H., Bohnensack R.;
RT "Functions of sorting nexin 17 domains and recognition motif for P-selectin
RT trafficking.";
RL J. Mol. Biol. 347:813-825(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-54.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [12]
RP INTERACTION WITH PODXL2.
RX PubMed=18606703; DOI=10.4049/jimmunol.181.2.1480;
RA Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D.;
RT "Endoglycan, a member of the CD34 family of sialomucins, is a ligand for
RT the vascular selectins.";
RL J. Immunol. 181:1480-1490(2008).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-129.
RX PubMed=28011641; DOI=10.1074/jbc.m116.767186;
RA Mehta-D'souza P., Klopocki A.G., Oganesyan V., Terzyan S., Mather T.,
RA Li Z., Panicker S.R., Zhu C., McEver R.P.;
RT "Glycan Bound to the Selectin Low Affinity State Engages Glu-88 to
RT Stabilize the High Affinity State under Force.";
RL J. Biol. Chem. 292:2510-2518(2017).
RN [14]
RP STRUCTURE BY NMR OF 160-199.
RX PubMed=8901515; DOI=10.1021/bi9610257;
RA Freedman S.J., Sanford D.G., Bachovchin W.W., Furie B.C., Baleja J.D.,
RA Furie B.;
RT "Structure and function of the epidermal growth factor domain of P-
RT selectin.";
RL Biochemistry 35:13733-13744(1996).
RN [15]
RP 3D-STRUCTURE MODELING OF 42-161.
RX PubMed=7505680; DOI=10.1002/pro.5560021103;
RA Bajorath J., Stenkamp R., Aruffo A.;
RT "Knowledge-based model building of proteins: concepts and examples.";
RL Protein Sci. 2:1798-1810(1993).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-198 IN COMPLEX WITH CALCIUM
RP IONS AND SELPLG, SUBUNIT, AND DISULFIDE BONDS AT 60-CYS--CYS-158;
RP 131-CYS--CYS-150; 163-CYS--CYS-183 AND 185-CYS--CYS-194.
RX PubMed=11081633; DOI=10.1016/s0092-8674(00)00138-0;
RA Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
RT "Insights into the molecular basis of leukocyte tethering and rolling
RT revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1.";
RL Cell 103:467-479(2000).
RN [17]
RP ERRATUM OF PUBMED:11081633.
RA Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
RL Cell 105:971-971(2001).
RN [18]
RP VARIANTS ASN-331; ASN-603; VAL-640 AND PRO-756.
RX PubMed=9668170; DOI=10.1093/hmg/7.8.1277;
RA Herrmann S.M., Ricard S., Nicaud V., Mallet C., Evans A., Ruidavets J.B.,
RA Arveiler D., Luc G., Cambien F.;
RT "The P-selectin gene is highly polymorphic: reduced frequency of the Pro715
RT allele carriers in patients with myocardial infarction.";
RL Hum. Mol. Genet. 7:1277-1284(1998).
RN [19]
RP VARIANTS MET-209; LEU-301; ASN-331; VAL-365; PHE-500; ASN-603; VAL-640 AND
RP PRO-756.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [20]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [21]
RP ASSOCIATION OF VARIANT VAL-640 WITH SUSCEPTIBILITY TO ISCHSTR.
RX PubMed=14681304; DOI=10.1093/hmg/ddh039;
RA Zee R.Y.L., Cook N.R., Cheng S., Reynolds R., Erlich H.A., Lindpaintner K.,
RA Ridker P.M.;
RT "Polymorphism in the P-selectin and interleukin-4 genes as determinants of
RT stroke: a population-based, prospective genetic analysis.";
RL Hum. Mol. Genet. 13:389-396(2004).
CC -!- FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds to
CC carbohydrates on neutrophils and monocytes. Mediates the interaction of
CC activated endothelial cells or platelets with leukocytes. The ligand
CC recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte
CC rolling over vascular surfaces during the initial steps in inflammation
CC through interaction with SELPLG. {ECO:0000269|PubMed:11081633,
CC ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:7585950}.
CC -!- SUBUNIT: Interacts with SNX17. Interacts with SELPLG/PSGL1 and PODXL2
CC and mediates neutrophil adhesion and leukocyte rolling. This
CC interaction requires the sialyl-Lewis X epitope of SELPLG and PODXL2,
CC and specific tyrosine sulfation on SELPLG.
CC {ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:11237770,
CC ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:18606703,
CC ECO:0000269|PubMed:7559387, ECO:0000269|PubMed:7585949,
CC ECO:0000269|PubMed:7585950}.
CC -!- INTERACTION:
CC P16109; Q14242: SELPLG; NbExp=4; IntAct=EBI-1030170, EBI-1030190;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28011641};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:28011641}.
CC -!- TISSUE SPECIFICITY: Stored in the alpha-granules of platelets and
CC Weibel-Palade bodies of endothelial cells. Upon cell activation by
CC agonists, P-selectin is transported rapidly to the cell surface.
CC -!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute
CC neurologic event leading to death of neural tissue of the brain and
CC resulting in loss of motor, sensory and/or cognitive function. Ischemic
CC strokes, resulting from vascular occlusion, is considered to be a
CC highly complex disease consisting of a group of heterogeneous disorders
CC with multiple genetic and environmental risk factors.
CC {ECO:0000269|PubMed:14681304}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/selp/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=P-selectin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_354";
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DR EMBL; M60234; AAA35910.1; -; Genomic_DNA.
DR EMBL; M60217; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60218; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60219; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60222; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60223; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60224; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60225; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60226; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60227; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60228; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60229; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60231; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60232; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M60233; AAA35910.1; JOINED; Genomic_DNA.
DR EMBL; M25322; AAA35911.1; -; mRNA.
DR EMBL; AF542391; AAN06828.1; -; Genomic_DNA.
DR EMBL; AL022146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90851.1; -; Genomic_DNA.
DR CCDS; CCDS1282.1; -.
DR PIR; A30359; A30359.
DR RefSeq; NP_002996.2; NM_003005.3.
DR RefSeq; XP_005245492.1; XM_005245435.1.
DR RefSeq; XP_005245493.1; XM_005245436.3.
DR PDB; 1FSB; NMR; -; A=160-199.
DR PDB; 1G1Q; X-ray; 2.40 A; A/B/C/D=42-198.
DR PDB; 1G1R; X-ray; 3.40 A; A/B/C/D=42-198.
DR PDB; 1G1S; X-ray; 1.90 A; A/B=42-198.
DR PDB; 1HES; X-ray; 3.00 A; P=813-830.
DR PDBsum; 1FSB; -.
DR PDBsum; 1G1Q; -.
DR PDBsum; 1G1R; -.
DR PDBsum; 1G1S; -.
DR PDBsum; 1HES; -.
DR AlphaFoldDB; P16109; -.
DR SMR; P16109; -.
DR BioGRID; 112303; 10.
DR DIP; DIP-37667N; -.
DR ELM; P16109; -.
DR IntAct; P16109; 2.
DR STRING; 9606.ENSP00000263686; -.
DR BindingDB; P16109; -.
DR ChEMBL; CHEMBL5378; -.
DR DrugBank; DB15271; Crizanlizumab.
DR DrugBank; DB06779; Dalteparin.
DR DrugBank; DB01109; Heparin.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR DrugBank; DB08813; Nadroparin.
DR DrugCentral; P16109; -.
DR GuidetoPHARMACOLOGY; 3103; -.
DR UniLectin; P16109; -.
DR GlyConnect; 2095; 5 N-Linked glycans (3 sites).
DR GlyGen; P16109; 13 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; P16109; -.
DR PhosphoSitePlus; P16109; -.
DR SwissPalm; P16109; -.
DR BioMuta; SELP; -.
DR DMDM; 215274139; -.
DR jPOST; P16109; -.
DR MassIVE; P16109; -.
DR PaxDb; P16109; -.
DR PeptideAtlas; P16109; -.
DR PRIDE; P16109; -.
DR ProteomicsDB; 53287; -.
DR ABCD; P16109; 5 sequenced antibodies.
DR Antibodypedia; 794; 1238 antibodies from 44 providers.
DR DNASU; 6403; -.
DR Ensembl; ENST00000263686.11; ENSP00000263686.5; ENSG00000174175.17.
DR GeneID; 6403; -.
DR KEGG; hsa:6403; -.
DR UCSC; uc001ggi.5; human.
DR CTD; 6403; -.
DR DisGeNET; 6403; -.
DR GeneCards; SELP; -.
DR HGNC; HGNC:10721; SELP.
DR HPA; ENSG00000174175; Low tissue specificity.
DR MIM; 173610; gene+phenotype.
DR MIM; 601367; phenotype.
DR neXtProt; NX_P16109; -.
DR PharmGKB; PA35643; -.
DR VEuPathDB; HostDB:ENSG00000174175; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P16109; -.
DR OrthoDB; 445079at2759; -.
DR PhylomeDB; P16109; -.
DR TreeFam; TF326910; -.
DR PathwayCommons; P16109; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P16109; -.
DR SIGNOR; P16109; -.
DR BioGRID-ORCS; 6403; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; SELP; human.
DR EvolutionaryTrace; P16109; -.
DR GeneWiki; P-selectin; -.
DR GenomeRNAi; 6403; -.
DR Pharos; P16109; Tclin.
DR PRO; PR:P16109; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P16109; protein.
DR Bgee; ENSG00000174175; Expressed in right coronary artery and 127 other tissues.
DR ExpressionAtlas; P16109; baseline and differential.
DR Genevisible; P16109; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031092; C:platelet alpha granule membrane; IDA:MGI.
DR GO; GO:0031088; C:platelet dense granule membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0042806; F:fucose binding; IDA:BHF-UCL.
DR GO; GO:0043208; F:glycosphingolipid binding; TAS:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0001530; F:lipopolysaccharide binding; IMP:BHF-UCL.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0033691; F:sialic acid binding; IDA:BHF-UCL.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IC:BHF-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISS:BHF-UCL.
DR GO; GO:0033623; P:regulation of integrin activation; IMP:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IC:BHF-UCL.
DR CDD; cd00033; CCP; 9.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR IDEAL; IID00353; -.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR033991; Selectin_CTLD.
DR InterPro; IPR002396; Selectin_superfamily.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 9.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 9.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 9.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50923; SUSHI; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Disulfide bond;
KW EGF-like domain; Glycoprotein; Lectin; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Repeat; Signal; Sushi;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT CHAIN 42..830
FT /note="P-selectin"
FT /id="PRO_0000017498"
FT TOPO_DOM 42..771
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 772..795
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..158
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 159..195
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 198..259
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 260..321
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 322..383
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 384..445
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 446..507
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 508..569
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 570..631
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 640..701
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 702..763
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 821..830
FT /note="Interaction with SNX17"
FT MOTIF 818..821
FT /note="Endocytosis signal"
FT /evidence="ECO:0000305"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R"
FT BINDING 123
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1R"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1G1R"
FT BINDING 133
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1R"
FT BINDING 146
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1R"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R"
FT LIPID 807
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:7684381"
FT LIPID 807
FT /note="S-stearoyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:7684381"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..158
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R,
FT ECO:0007744|PDB:1G1S"
FT DISULFID 131..150
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R,
FT ECO:0007744|PDB:1G1S"
FT DISULFID 163..174
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R,
FT ECO:0007744|PDB:1G1S"
FT DISULFID 168..183
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R,
FT ECO:0007744|PDB:1G1S"
FT DISULFID 185..194
FT /evidence="ECO:0000269|PubMed:11081633,
FT ECO:0007744|PDB:1G1Q, ECO:0007744|PDB:1G1R,
FT ECO:0007744|PDB:1G1S"
FT DISULFID 200..244
FT /evidence="ECO:0000250"
FT DISULFID 230..257
FT /evidence="ECO:0000250"
FT DISULFID 262..306
FT /evidence="ECO:0000250"
FT DISULFID 292..319
FT /evidence="ECO:0000250"
FT DISULFID 324..368
FT /evidence="ECO:0000250"
FT DISULFID 354..381
FT /evidence="ECO:0000250"
FT DISULFID 386..430
FT /evidence="ECO:0000250"
FT DISULFID 416..443
FT /evidence="ECO:0000250"
FT DISULFID 448..492
FT /evidence="ECO:0000250"
FT DISULFID 478..505
FT /evidence="ECO:0000250"
FT DISULFID 510..554
FT /evidence="ECO:0000250"
FT DISULFID 540..567
FT /evidence="ECO:0000250"
FT DISULFID 572..616
FT /evidence="ECO:0000250"
FT DISULFID 602..629
FT /evidence="ECO:0000250"
FT DISULFID 642..686
FT /evidence="ECO:0000250"
FT DISULFID 672..699
FT /evidence="ECO:0000250"
FT DISULFID 704..748
FT /evidence="ECO:0000250"
FT DISULFID 734..761
FT /evidence="ECO:0000250"
FT VARIANT 179
FT /note="G -> R (in dbSNP:rs3917718)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019381"
FT VARIANT 209
FT /note="V -> M (in dbSNP:rs6125)"
FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.2"
FT /id="VAR_013910"
FT VARIANT 230
FT /note="C -> F (in dbSNP:rs3917869)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019382"
FT VARIANT 274
FT /note="T -> I (in dbSNP:rs3917724)"
FT /evidence="ECO:0000269|PubMed:2466574, ECO:0000269|Ref.2"
FT /id="VAR_019383"
FT VARIANT 301
FT /note="P -> L (in dbSNP:rs6124)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013911"
FT VARIANT 331
FT /note="S -> N (in dbSNP:rs6131)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:9668170, ECO:0000269|Ref.2"
FT /id="VAR_004192"
FT VARIANT 365
FT /note="M -> V (in dbSNP:rs6134)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013912"
FT VARIANT 385
FT /note="S -> L (in dbSNP:rs3917742)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019384"
FT VARIANT 500
FT /note="S -> F (in dbSNP:rs6130)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013913"
FT VARIANT 542
FT /note="E -> K (in dbSNP:rs3917769)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019385"
FT VARIANT 603
FT /note="D -> N (in dbSNP:rs6127)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:2466574, ECO:0000269|PubMed:9668170,
FT ECO:0000269|Ref.2"
FT /id="VAR_004193"
FT VARIANT 619
FT /note="S -> A (in dbSNP:rs2228672)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019386"
FT VARIANT 631
FT /note="G -> V (in dbSNP:rs3917812)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019387"
FT VARIANT 640
FT /note="L -> V (associated with susceptibility to ischemic
FT stroke; dbSNP:rs6133)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:9668170,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT /id="VAR_004194"
FT VARIANT 661
FT /note="T -> N (in dbSNP:rs3917814)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019388"
FT VARIANT 673
FT /note="N -> S (in dbSNP:rs3917815)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_019389"
FT VARIANT 756
FT /note="T -> P (reduced frequency in patients with
FT myocardial infarction; dbSNP:rs6136)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:9668170, ECO:0000269|Ref.2"
FT /id="VAR_004195"
FT MUTAGEN 129
FT /note="E->D: Impairs interaction with SELPLG. Abolishes
FT cell rolling on glycan ligands."
FT /evidence="ECO:0000269|PubMed:28011641"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1G1S"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1G1S"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1G1S"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1G1S"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1G1S"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:1G1S"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1G1S"
SQ 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
