GenomeNet

Database: UniProt
Entry: P16109
LinkDB: P16109
Original site: P16109 
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   13-FEB-2019, entry version 217.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS ILE-274 AND
RP   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
RT   and inflammation.";
RL   Cell 56:1033-1044(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-179; MET-209;
RP   PHE-230; ILE-274; ASN-331; LEU-385; LYS-542; ASN-603; ALA-619;
RP   VAL-631; VAL-640; 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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;
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
RT   cysteine 766 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
RT   critical for 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
RT   sulfation 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
RT   for 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-
RT   terminus of 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-
RT   selectin 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
RT   for 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
RP   CALCIUM IONS AND SELPLG, SUBUNIT, AND DISULFIDE BONDS AT
RP   60-CYS--CYS-158; 131-CYS--CYS-150; 163-CYS--CYS-183 AND
RP   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-
RT   1.";
RL   Cell 103:467-479(2000).
RN   [17]
RP   ERRATUM.
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.,
RA   Ruidavets J.B., Arveiler D., Luc G., Cambien F.;
RT   "The P-selectin gene is highly polymorphic: reduced frequency of the
RT   Pro715 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
RP   AND 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
RT   of human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [20]
RP   ERRATUM.
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.,
RA   Lindpaintner K., Ridker P.M.;
RT   "Polymorphism in the P-selectin and interleukin-4 genes as
RT   determinants of stroke: a population-based, prospective genetic
RT   analysis.";
RL   Hum. Mol. Genet. 13:389-396(2004).
CC   -!- FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds
CC       to carbohydrates on neutrophils and monocytes. Mediates the
CC       interaction of activated endothelial cells or platelets with
CC       leukocytes. The ligand recognized is sialyl-Lewis X. Mediates
CC       rapid rolling of leukocyte rolling over vascular surfaces during
CC       the initial steps in inflammation through interaction with SELPLG.
CC       {ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:28011641,
CC       ECO:0000269|PubMed:7585950}.
CC   -!- SUBUNIT: Interacts with SNX17. Interacts with SELPLG/PSGL1 and
CC       PODXL2 and mediates neutrophil adhesion and leukocyte rolling.
CC       This interaction requires the sialyl-Lewis X epitope of SELPLG and
CC       PODXL2, 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       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
CC       acute neurologic event leading to death of neural tissue of the
CC       brain and resulting in loss of motor, sensory and/or cognitive
CC       function. Ischemic strokes, resulting from vascular occlusion, is
CC       considered to be a highly complex disease consisting of a group of
CC       heterogeneous disorders with multiple genetic and environmental
CC       risk factors. {ECO:0000269|PubMed:14681304}. Note=Disease
CC       susceptibility is associated with variations affecting the gene
CC       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";
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   UniGene; Hs.73800; -.
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   PDB; 1KJD; Model; -; A=42-161.
DR   PDBsum; 1FSB; -.
DR   PDBsum; 1G1Q; -.
DR   PDBsum; 1G1R; -.
DR   PDBsum; 1G1S; -.
DR   PDBsum; 1HES; -.
DR   PDBsum; 1KJD; -.
DR   ProteinModelPortal; P16109; -.
DR   SMR; P16109; -.
DR   BioGrid; 112303; 9.
DR   DIP; DIP-37667N; -.
DR   ELM; P16109; -.
DR   IntAct; P16109; 2.
DR   STRING; 9606.ENSP00000263686; -.
DR   BindingDB; P16109; -.
DR   ChEMBL; CHEMBL5378; -.
DR   DrugBank; DB06779; Dalteparin.
DR   DrugBank; DB01109; Heparin.
DR   DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR   DrugBank; DB08813; Nadroparin.
DR   UniLectin; P16109; -.
DR   iPTMnet; P16109; -.
DR   PhosphoSitePlus; P16109; -.
DR   SwissPalm; P16109; -.
DR   BioMuta; SELP; -.
DR   DMDM; 215274139; -.
DR   jPOST; P16109; -.
DR   PaxDb; P16109; -.
DR   PeptideAtlas; P16109; -.
DR   PRIDE; P16109; -.
DR   ProteomicsDB; 53287; -.
DR   Ensembl; ENST00000263686; ENSP00000263686; ENSG00000174175.
DR   GeneID; 6403; -.
DR   KEGG; hsa:6403; -.
DR   UCSC; uc001ggi.5; human.
DR   CTD; 6403; -.
DR   DisGeNET; 6403; -.
DR   EuPathDB; HostDB:ENSG00000174175.16; -.
DR   GeneCards; SELP; -.
DR   HGNC; HGNC:10721; SELP.
DR   HPA; CAB002145; -.
DR   HPA; HPA002655; -.
DR   HPA; HPA005990; -.
DR   MalaCards; SELP; -.
DR   MIM; 173610; gene+phenotype.
DR   MIM; 601367; phenotype.
DR   neXtProt; NX_P16109; -.
DR   PharmGKB; PA35643; -.
DR   eggNOG; ENOG410IS44; Eukaryota.
DR   eggNOG; ENOG410Y5JF; LUCA.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   InParanoid; P16109; -.
DR   KO; K06496; -.
DR   OrthoDB; 445079at2759; -.
DR   PhylomeDB; P16109; -.
DR   TreeFam; TF326910; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   SIGNOR; P16109; -.
DR   EvolutionaryTrace; P16109; -.
DR   GeneWiki; P-selectin; -.
DR   GenomeRNAi; 6403; -.
DR   PRO; PR:P16109; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000174175; Expressed in 136 organ(s), highest expression level in adrenal gland.
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; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR   GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR   GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
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: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   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; IPR013032; EGF-like_CS.
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;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Lectin; Lipoprotein; Membrane; Metal-binding; Palmitate; Polymorphism;
KW   Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     41
FT   CHAIN        42    830       P-selectin.
FT                                /FTId=PRO_0000017498.
FT   TOPO_DOM     42    771       Extracellular. {ECO:0000255}.
FT   TRANSMEM    772    795       Helical. {ECO:0000255}.
FT   TOPO_DOM    796    830       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       58    158       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      159    195       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      198    259       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      260    321       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      322    383       Sushi 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      384    445       Sushi 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      446    507       Sushi 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      508    569       Sushi 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      570    631       Sushi 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      640    701       Sushi 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      702    763       Sushi 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      821    830       Interaction with SNX17.
FT   MOTIF       818    821       Endocytosis signal. {ECO:0000305}.
FT   METAL       121    121       Calcium. {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000269|PubMed:11081633}.
FT   METAL       123    123       Calcium. {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000269|PubMed:11081633}.
FT   METAL       124    124       Calcium. {ECO:0000244|PDB:1G1R}.
FT   METAL       146    146       Calcium. {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000269|PubMed:11081633}.
FT   METAL       147    147       Calcium. {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000269|PubMed:11081633}.
FT   BINDING     123    123       Carbohydrate. {ECO:0000244|PDB:1G1R,
FT                                ECO:0000269|PubMed:11081633}.
FT   BINDING     133    133       Carbohydrate. {ECO:0000244|PDB:1G1R,
FT                                ECO:0000269|PubMed:11081633}.
FT   BINDING     146    146       Carbohydrate. {ECO:0000244|PDB:1G1R,
FT                                ECO:0000269|PubMed:11081633}.
FT   LIPID       807    807       S-palmitoyl cysteine; alternate.
FT                                {ECO:0000269|PubMed:7684381}.
FT   LIPID       807    807       S-stearoyl cysteine; alternate.
FT                                {ECO:0000269|PubMed:7684381}.
FT   CARBOHYD     54     54       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16263699}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    180    180       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    219    219       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    411    411       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    460    460       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    518    518       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    665    665       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    716    716       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    723    723       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    741    741       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     60    158       {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000244|PDB:1G1S,
FT                                ECO:0000269|PubMed:11081633}.
FT   DISULFID    131    150       {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000244|PDB:1G1S,
FT                                ECO:0000269|PubMed:11081633}.
FT   DISULFID    163    174       {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000244|PDB:1G1S,
FT                                ECO:0000269|PubMed:11081633}.
FT   DISULFID    168    183       {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000244|PDB:1G1S,
FT                                ECO:0000269|PubMed:11081633}.
FT   DISULFID    185    194       {ECO:0000244|PDB:1G1Q,
FT                                ECO:0000244|PDB:1G1R,
FT                                ECO:0000244|PDB:1G1S,
FT                                ECO:0000269|PubMed:11081633}.
FT   DISULFID    200    244       {ECO:0000250}.
FT   DISULFID    230    257       {ECO:0000250}.
FT   DISULFID    262    306       {ECO:0000250}.
FT   DISULFID    292    319       {ECO:0000250}.
FT   DISULFID    324    368       {ECO:0000250}.
FT   DISULFID    354    381       {ECO:0000250}.
FT   DISULFID    386    430       {ECO:0000250}.
FT   DISULFID    416    443       {ECO:0000250}.
FT   DISULFID    448    492       {ECO:0000250}.
FT   DISULFID    478    505       {ECO:0000250}.
FT   DISULFID    510    554       {ECO:0000250}.
FT   DISULFID    540    567       {ECO:0000250}.
FT   DISULFID    572    616       {ECO:0000250}.
FT   DISULFID    602    629       {ECO:0000250}.
FT   DISULFID    642    686       {ECO:0000250}.
FT   DISULFID    672    699       {ECO:0000250}.
FT   DISULFID    704    748       {ECO:0000250}.
FT   DISULFID    734    761       {ECO:0000250}.
FT   VARIANT     179    179       G -> R (in dbSNP:rs3917718).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019381.
FT   VARIANT     209    209       V -> M (in dbSNP:rs6125).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_013910.
FT   VARIANT     230    230       C -> F (in dbSNP:rs3917869).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019382.
FT   VARIANT     274    274       T -> I (in dbSNP:rs3917724).
FT                                {ECO:0000269|PubMed:2466574,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019383.
FT   VARIANT     301    301       P -> L (in dbSNP:rs6124).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_013911.
FT   VARIANT     331    331       S -> N (in dbSNP:rs6131).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:9668170,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_004192.
FT   VARIANT     365    365       M -> V (in dbSNP:rs6134).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_013912.
FT   VARIANT     385    385       S -> L (in dbSNP:rs3917742).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019384.
FT   VARIANT     500    500       S -> F (in dbSNP:rs6130).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_013913.
FT   VARIANT     542    542       E -> K (in dbSNP:rs3917769).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019385.
FT   VARIANT     603    603       D -> N (in dbSNP:rs6127).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:2466574,
FT                                ECO:0000269|PubMed:9668170,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_004193.
FT   VARIANT     619    619       S -> A (in dbSNP:rs2228672).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019386.
FT   VARIANT     631    631       G -> V (in dbSNP:rs3917812).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019387.
FT   VARIANT     640    640       L -> V (associated with susceptibility to
FT                                ischemic stroke; dbSNP:rs6133).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:16710414,
FT                                ECO:0000269|PubMed:9668170,
FT                                ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
FT                                /FTId=VAR_004194.
FT   VARIANT     661    661       T -> N (in dbSNP:rs3917814).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019388.
FT   VARIANT     673    673       N -> S (in dbSNP:rs3917815).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019389.
FT   VARIANT     756    756       T -> P (reduced frequency in patients
FT                                with myocardial infarction;
FT                                dbSNP:rs6136).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:9668170,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_004195.
FT   MUTAGEN     129    129       E->D: Impairs interaction with SELPLG.
FT                                Abolishes cell rolling on glycan ligands.
FT                                {ECO:0000269|PubMed:28011641}.
FT   STRAND       43     46       {ECO:0000244|PDB:1G1S}.
FT   HELIX        53     63       {ECO:0000244|PDB:1G1S}.
FT   STRAND       64     67       {ECO:0000244|PDB:1G1S}.
FT   HELIX        73     82       {ECO:0000244|PDB:1G1S}.
FT   STRAND       90     97       {ECO:0000244|PDB:1G1S}.
FT   STRAND      100    103       {ECO:0000244|PDB:1G1S}.
FT   TURN        104    106       {ECO:0000244|PDB:1G1S}.
FT   TURN        112    114       {ECO:0000244|PDB:1G1S}.
FT   STRAND      131    134       {ECO:0000244|PDB:1G1S}.
FT   STRAND      139    141       {ECO:0000244|PDB:1G1S}.
FT   STRAND      145    148       {ECO:0000244|PDB:1G1S}.
FT   STRAND      154    160       {ECO:0000244|PDB:1G1S}.
FT   HELIX       167    170       {ECO:0000244|PDB:1G1S}.
FT   STRAND      171    176       {ECO:0000244|PDB:1G1S}.
FT   STRAND      178    185       {ECO:0000244|PDB:1G1S}.
FT   STRAND      189    191       {ECO:0000244|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
//
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