ID SELPL_HUMAN Reviewed; 412 AA. AC Q14242; A8K2Y0; B4DQC3; B7Z5C7; J3KMX6; Q12775; Q6GTW7; Q8N7J7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 146. DE RecName: Full=P-selectin glycoprotein ligand 1; DE Short=PSGL-1; DE AltName: Full=Selectin P ligand; DE AltName: CD_antigen=CD162; DE Flags: Precursor; GN Name=SELPLG; 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]. RC TISSUE=Placenta; RX PubMed=7541799; DOI=10.1074/jbc.270.27.16470; RA Veldman G.M., Bean K.M., Cumming D.A., Eddy R.L., Sait S.N.J., RA Shows T.B.; RT "Genomic organization and chromosomal localization of the gene RT encoding human P-selectin glycoprotein ligand."; RL J. Biol. Chem. 270:16470-16475(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 132-GLN--ALA-141 RP DEL. RX PubMed=7505206; DOI=10.1016/0092-8674(93)90327-M; RA Sako D., Chang X.J., Barone K.M., Vachino G., White H.M., Shaw G., RA Veldman G.M., Bean K.M., Ahern T.J., Furie B., Cumming D.A., RA Larsen G.R.; RT "Expression cloning of a functional glycoprotein ligand for P- RT selectin."; RL Cell 75:1179-1186(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND RP VARIANTS ILE-62 AND 132-GLN--ALA-141 DEL. RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-62 AND SER-246. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP 132-GLN--ALA-141 DEL. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 350-355 AND 390-396, INTERACTION WITH SELP AND RP SELE, STRUCTURE OF CARBOHYDRATE, SUBUNIT, AND SIALIC ACID CONTENT. RC TISSUE=Neutrophil; RX PubMed=7521878; RA Moore K.L., Eaton S.F., Lyons D.E., Lichenstein H.S., Cummings R.D., RA McEver R.P.; RT "The P-selectin glycoprotein ligand from human neutrophils displays RT sialylated, fucosylated, O-linked poly-N-acetyllactosamine."; RL J. Biol. Chem. 269:23318-23327(1994). RN [8] RP SULFATION, INTERACTION WITH SELP, AND MUTAGENESIS OF 46-TYR--ASP-52. 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 [9] RP SULFATION, INTERACTION WITH SELP, AND MUTAGENESIS OF TYR-46; TYR-48; RP TYR-51 AND THR-57. 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 [10] RP SULFATION, AND INTERACTION WITH SELP. 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 [11] RP STRUCTURE OF O-LINKED CARBOHYDRATES. RX PubMed=8702529; DOI=10.1074/jbc.271.31.18732; RA Wilkins P.P., McEver R.P., Cummings R.D.; RT "Structures of the O-glycans on P-selectin glycoprotein ligand-1 from RT HL-60 cells."; RL J. Biol. Chem. 271:18732-18742(1996). RN [12] RP INTERACTION WITH SELP, DISULFIDE BOND AT CYS-320, AND MUTAGENESIS OF RP CYS-320. RX PubMed=10713099; DOI=10.1074/jbc.275.11.7839; RA Epperson T.K., Patel K.D., McEver R.P., Cummings R.D.; RT "Noncovalent association of P-selectin glycoprotein ligand-1 and RT minimal determinants for binding to P-selectin."; RL J. Biol. Chem. 275:7839-7853(2000). RN [13] RP INTERACTION WITH SELE AND SELP, SULFATION, AND FUNCTION. RX PubMed=11566773; DOI=10.1016/S0006-3495(01)75850-X; RA Rodgers S.D., Camphausen R.T., Hammer D.A.; RT "Tyrosine sulfation enhances but is not required for PSGL-1 rolling RT adhesion on P-selectin."; RL Biophys. J. 81:2001-2009(2001). RN [14] RP INTERACTION WITH MSN AND SYK. RX PubMed=12387735; DOI=10.1016/S1074-7613(02)00420-X; RA Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A., RA Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J., RA Sanchez-Madrid F.; RT "ITAM-based interaction of ERM proteins with Syk mediates signaling by RT the leukocyte adhesion receptor PSGL-1."; RL Immunity 17:401-412(2002). RN [15] RP INTERACTION WITH SELL, FUNCTION, AND MUTAGENESIS OF THR-44; TYR-48; RP TYR-51 AND THR-57. RX PubMed=12403782; DOI=10.1074/jbc.M204360200; RA Bernimoulin M.P., Zeng X.-L., Abbal C., Giraud S., Martinez M., RA Michielin O., Schapira M., Spertini O.; RT "Molecular basis of leukocyte rolling on PSGL-1. Predominant role of RT core-2 O-glycans and of tyrosine sulfate residue 51."; RL J. Biol. Chem. 278:37-47(2003). RN [16] RP INTERACTION WITH SELL, SULFATION, AND GLYCOSYLATION. RX PubMed=12736247; DOI=10.1074/jbc.M303551200; RA Leppaenen A., Yago T., Otto V.I., McEver R.P., Cummings R.D.; RT "Model glycosulfopeptides from P-selectin glycoprotein ligand-1 RT require tyrosine sulfation and a core 2-branched O-glycan to bind to RT L-selectin."; RL J. Biol. Chem. 278:26391-26400(2003). RN [17] RP INTERACTION WITH SNX20. RX PubMed=18196517; DOI=10.1002/eji.200737777; RA Schaff U.Y., Shih H.H., Lorenz M., Sako D., Kriz R., Milarski K., RA Bates B., Tchernychev B., Shaw G.D., Simon S.I.; RT "SLIC-1/sorting nexin 20: a novel sorting nexin that directs RT subcellular distribution of PSGL-1."; RL Eur. J. Immunol. 38:550-564(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [19] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBTEROVIRUS 71 RP CAPSID PROTEINS. RX PubMed=19543284; DOI=10.1038/nm.1961; RA Nishimura Y., Shimojima M., Tano Y., Miyamura T., Wakita T., RA Shimizu H.; RT "Human P-selectin glycoprotein ligand-1 is a functional receptor for RT enterovirus 71."; RL Nat. Med. 15:794-797(2009). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-68 IN COMPLEX WITH SELE RP AND SELP LECTIN/EGF DOMAINS, SULFATION AT TYR-46; TYR-48 AND TYR-51, RP GLYCOSYLATION AT THR-57, AND PYROGLUTAMATE FORMATION AT GLN-42. 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 [21] RP ERRATUM. RA Somers W.S., Tang J., Shaw G.D., Camphausen R.T.; RL Cell 105:971-971(2001). CC -!- FUNCTION: A SLe(x)-type proteoglycan, which through high affinity, CC calcium-dependent interactions with E-, P- and L-selectins, CC mediates rapid rolling of leukocytes over vascular surfaces during CC the initial steps in inflammation. Critical for the initial CC leukocyte capture. {ECO:0000269|PubMed:11566773, CC ECO:0000269|PubMed:12403782}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for enterovirus CC 71. {ECO:0000269|PubMed:19543284}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Interaction with P-, E- and CC L-selectins, through their lectin/EGF domains, is required for CC promoting recruitment and rolling of leukocytes. These CC interactions require sialyl Lewis X glycan modification but there CC is a differing dependence for tyrosine sulfations. Sulfation on CC Tyr-51 of PSGL1 is most important for high affinity L- CC selectin/SELL binding while P-selectin/SELP requires sulfation on CC Tyr-48. E-selectin/SELE binds with much lower affinity and CC requires the sLe(x) epitope, but apparantly not tyrosine CC sulfation. Dimerization appears not to be required for P- CC selectin/SELP binding. Interacts with SNX20. Interacts with MSN CC and SYK; mediates the activation of SYK by SELPLG. (Microbial CC infection) Interacts with enterovirus 71 capsid proteins CC (PubMed:19543284). {ECO:0000269|PubMed:10713099, CC ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:11566773, CC ECO:0000269|PubMed:12387735, ECO:0000269|PubMed:12403782, CC ECO:0000269|PubMed:12736247, ECO:0000269|PubMed:18196517, CC ECO:0000269|PubMed:19543284, ECO:0000269|PubMed:7521878, CC ECO:0000269|PubMed:7559387, ECO:0000269|PubMed:7585949, CC ECO:0000269|PubMed:7585950}. CC -!- INTERACTION: CC Q7Z614:SNX20; NbExp=5; IntAct=EBI-1030190, EBI-744896; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14242-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14242-2; Sequence=VSP_044827; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed on neutrophils, monocytes and most CC lymphocytes. CC -!- PTM: Displays complex, core-2, sialylated and fucosylated O-linked CC oligosaccharides, at least some of which appear to contain poly-N- CC acetyllactosamine with varying degrees of substitution. Mainly CC disialylated or neutral forms of the core-2 tetrasaccharide, CC Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN CC ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains CC about 14% fucose with alpha-1,3 linkage present in two forms: One CC species is a disialylated, monofucosylated glycan, and the other, CC a monosialylated, trifucosylated glycan with a polylactosamine CC backbone. The fucosylated forms carry the Lewis antigen and are CC important for interaction with selectins and for functioning in CC leukocyte rolling. The modification containing the sialyl Lewis X CC glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation. CC {ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:12736247}. CC -!- PTM: Sulfation, in conjunction with the SLe(x)-containing glycan, CC is necessary for P- and L-selectin binding. High affinity P- CC selectin binding has a preferred requirement for the isomer CC sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding CC requires predominantly sulfation on Tyr-51 with sulfation on Tyr- CC 48 playing only a minor role. These sulfations play an important CC role in L- and P-selectin-mediated neutrophil recruitment, and CC leukocyte rolling. {ECO:0000269|PubMed:11081633}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=P-selectin glycoprotein ligand CC 1 entry; CC URL="https://en.wikipedia.org/wiki/P-selectin_glycoprotein_ligand-1"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/selplg/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U25956; AAA74577.1; -; Genomic_DNA. DR EMBL; U02297; AAC50061.1; -; mRNA. DR EMBL; AK098315; BAC05283.1; -; mRNA. DR EMBL; AK290395; BAF83084.1; -; mRNA. DR EMBL; AK298738; BAG60885.1; -; mRNA. DR EMBL; AK298742; BAH12863.1; -; mRNA. DR EMBL; AY331789; AAP81163.1; -; Genomic_DNA. DR EMBL; AC007569; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008119; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC029782; AAH29782.1; -; mRNA. DR CCDS; CCDS31895.2; -. [Q14242-1] DR CCDS; CCDS55881.1; -. [Q14242-2] DR PIR; A57468; A57468. DR RefSeq; NP_001193538.1; NM_001206609.1. [Q14242-2] DR RefSeq; NP_002997.2; NM_003006.4. [Q14242-1] DR RefSeq; XP_005269133.1; XM_005269076.2. DR UniGene; Hs.591014; -. DR PDB; 1G1S; X-ray; 1.90 A; C/D=42-60. DR PDBsum; 1G1S; -. DR ProteinModelPortal; Q14242; -. DR BioGrid; 112304; 6. DR DIP; DIP-37668N; -. DR IntAct; Q14242; 7. DR STRING; 9606.ENSP00000228463; -. DR BindingDB; Q14242; -. DR ChEMBL; CHEMBL3301394; -. DR PhosphoSite; Q14242; -. DR UniCarbKB; Q14242; -. DR BioMuta; SELPLG; -. DR DMDM; 2498904; -. DR MaxQB; Q14242; -. DR PaxDb; Q14242; -. DR PRIDE; Q14242; -. DR DNASU; 6404; -. DR Ensembl; ENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2] DR Ensembl; ENST00000550948; ENSP00000447752; ENSG00000110876. [Q14242-1] DR GeneID; 6404; -. DR KEGG; hsa:6404; -. DR UCSC; uc001tni.3; human. [Q14242-1] DR CTD; 6404; -. DR GeneCards; SELPLG; -. DR H-InvDB; HIX0010969; -. DR HGNC; HGNC:10722; SELPLG. DR HPA; CAB002431; -. DR MIM; 600738; gene. DR neXtProt; NX_Q14242; -. DR PharmGKB; PA35644; -. DR eggNOG; ENOG410JASD; Eukaryota. DR eggNOG; ENOG410Y5S5; LUCA. DR GeneTree; ENSGT00440000039754; -. DR HOGENOM; HOG000013048; -. DR HOVERGEN; HBG061628; -. DR InParanoid; Q14242; -. DR KO; K06544; -. DR OMA; NYSPTEM; -. DR OrthoDB; EOG7CVPZ8; -. DR PhylomeDB; Q14242; -. DR TreeFam; TF337792; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR ChiTaRS; SELPLG; human. DR EvolutionaryTrace; Q14242; -. DR GeneWiki; P-selectin_glycoprotein_ligand-1; -. DR GenomeRNAi; 6404; -. DR NextBio; 24882; -. DR PMAP-CutDB; A8K2Y0; -. DR PRO; PR:Q14242; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; Q14242; -. DR CleanEx; HS_SELPLG; -. DR ExpressionAtlas; Q14242; baseline and differential. DR Genevisible; Q14242; HS. DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0001931; C:uropod; IDA:UniProtKB. DR GO; GO:0005102; F:receptor binding; NAS:ProtInc. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:MGI. DR GO; GO:0050902; P:leukocyte adhesive activation; ISS:UniProtKB. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl. DR InterPro; IPR026195; PSGL-1. DR PANTHER; PTHR17384; PTHR17384; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; KW Cleavage on pair of basic residues; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; Membrane; KW Polymorphism; Pyrrolidone carboxylic acid; Receptor; KW Reference proteome; Repeat; Sialic acid; Signal; Sulfation; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 17 {ECO:0000255}. FT PROPEP 18 41 FT /FTId=PRO_0000022302. FT CHAIN 42 412 P-selectin glycoprotein ligand 1. FT /FTId=PRO_0000022303. FT TOPO_DOM 18 320 Extracellular. {ECO:0000255}. FT TRANSMEM 321 341 Helical. {ECO:0000255}. FT TOPO_DOM 342 412 Cytoplasmic. {ECO:0000255}. FT REPEAT 122 131 1. FT REPEAT 132 141 2. FT REPEAT 142 151 3. FT REPEAT 162 171 4. FT REPEAT 182 191 5. FT REPEAT 192 201 6. FT REPEAT 202 211 7. FT REPEAT 212 221 8. FT REPEAT 222 231 9. FT REPEAT 232 241 10. FT REPEAT 242 251 11. FT REPEAT 252 261 12. FT REGION 122 261 12 X 10 AA tandem repeats. FT MOD_RES 42 42 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:11081633}. FT MOD_RES 46 46 Sulfotyrosine. FT {ECO:0000269|PubMed:11081633}. FT MOD_RES 48 48 Sulfotyrosine. FT {ECO:0000269|PubMed:11081633}. FT MOD_RES 51 51 Sulfotyrosine. FT {ECO:0000269|PubMed:11081633}. FT CARBOHYD 57 57 O-linked (GalNAc...). FT {ECO:0000269|PubMed:11081633}. FT CARBOHYD 65 65 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 111 111 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 302 302 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 320 320 Interchain. FT {ECO:0000269|PubMed:10713099}. FT VAR_SEQ 1 1 M -> MAVGASGLEGDKMAGAM (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_044827. FT VARIANT 62 62 M -> I (in dbSNP:rs2228315). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|Ref.4}. FT /FTId=VAR_019156. FT VARIANT 132 141 Missing (in short form; not an FT alternative splicing; dbSNP:rs63748999). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:7505206}. FT /FTId=VAR_005611. FT VARIANT 246 246 P -> S (in dbSNP:rs8179142). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_019157. FT MUTAGEN 44 44 T->A: No effect on L-selectin binding nor FT neutrophil rolling. FT {ECO:0000269|PubMed:12403782}. FT MUTAGEN 46 52 YEYLDYD->FEFLDFE: No sulfation. Almost FT complete loss of P-selectin binding. No FT effect on E-selectin binding. FT {ECO:0000269|PubMed:7585949}. FT MUTAGEN 46 51 YEYLDY->FEFLDF: No sulfation. Almost FT complete loss of P-selectin binding. No FT effect on E-selectin binding. FT MUTAGEN 46 46 Y->F: Binding L-selectin reduced by 20%, FT neutrophil recruitment reduced by 30%, FT and lymphocyte rolling reduced by 32%; FT when associated with F-48. Binding L- FT selectin reduced by 86%, neutrophil FT recruitment reduced by 75%, and FT lymphocyte rolling reduced by 69%; when FT associated with F-51. Binding L-selectin FT reduced by 89%, and neutrophil FT recruitment reduced by 90%; when FT associated with F-48 and F-51. Binding of FT L-selectin reduced by 91%; when FT associated with F-48; F-51 and A-57. FT {ECO:0000269|PubMed:7585950}. FT MUTAGEN 48 48 Y->F: Binding L-selectin reduced by 20%, FT neutrophil recruitment reduced by 30%, FT and lymphocyte rolling reduced by 32%; FT when associated with F-46. Binding L- FT lectin reduced by 31%, neutrophil FT recruitment reduced by 52%, and FT lymphocyte rolling reduced by 52%; when FT associated with F-51. Binding L-selectin FT reduced by 89%, and neutrophil FT recruitment reduced by 90%; when FT associated with F-46 and F-51. Binding of FT L-selectin reduced by 91%; when FT associated with F-46; F-51 and A-57. FT {ECO:0000269|PubMed:12403782, FT ECO:0000269|PubMed:7585950}. FT MUTAGEN 51 51 Y->F: Binding L-selectin reduced by 86%, FT neutrophil recruitment reduced by 75% FT and, lymphocyte rolling reduced by 69%; FT when associated with F-46. Binding L- FT selectin reduced by 31%, neutrophil FT recruitment reduced by 52%, and FT lymphocyte rolling reduced by 52%; when FT associated with F-48; Binding L-selectin FT reduced by 89%, and neutrophil FT recruitment reduced by 90%; when FT associated with F-46 and F-48. Binding of FT L-selectin reduced by 91%; when FT associated with F-46; F-48 and A-57. FT {ECO:0000269|PubMed:12403782, FT ECO:0000269|PubMed:7585950}. FT MUTAGEN 57 57 T->A: No E- nor P-selectin binding, and FT very little neutrophil rolling. Binding FT of L-selectin reduced by 91%; when FT associated with F-46; F-48 and F-51. FT {ECO:0000269|PubMed:12403782, FT ECO:0000269|PubMed:7585950}. FT MUTAGEN 320 320 C->A,S: No dimer formation. No effect on FT P-selectin binding. FT {ECO:0000269|PubMed:10713099}. FT CONFLICT 23 39 Missing (in Ref. 3; BAC05283). FT {ECO:0000305}. FT CONFLICT 50 50 D -> E (in Ref. 3; BAC05283). FT {ECO:0000305}. FT CONFLICT 219 219 M -> T (in Ref. 3; BAC05283). FT {ECO:0000305}. FT CONFLICT 222 222 Q -> R (in Ref. 3; BAH12863). FT {ECO:0000305}. FT CONFLICT 396 396 P -> A (in Ref. 3; BAC05283). FT {ECO:0000305}. FT TURN 51 53 {ECO:0000244|PDB:1G1S}. SQ SEQUENCE 412 AA; 43201 MW; A92A2A902DC9963A CRC64; MPLQLLLLLI LLGPGNSLQL WDTWADEAEK ALGPLLARDR RQATEYEYLD YDFLPETEPP EMLRNSTDTT PLTGPGTPES TTVEPAARRS TGLDAGGAVT ELTTELANMG NLSTDSAAME IQTTQPAATE AQTTQPVPTE AQTTPLAATE AQTTRLTATE AQTTPLAATE AQTTPPAATE AQTTQPTGLE AQTTAPAAME AQTTAPAAME AQTTPPAAME AQTTQTTAME AQTTAPEATE AQTTQPTATE AQTTPLAAME ALSTEPSATE ALSMEPTTKR GLFIPFSVSS VTHKGIPMAA SNLSVNYPVG APDHISVKQC LLAILILALV ATIFFVCTVV LAVRLSRKGH MYPVRNYSPT EMVCISSLLP DGGEGPSATA NGGLSKAKSP GLTPEPREDR EGDDLTLHSF LP //