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 27-MAR-2024, entry version 199. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., Shows T.B.; RT "Genomic organization and chromosomal localization of the gene encoding RT 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 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., Larsen G.R.; RT "Expression cloning of a functional glycoprotein ligand for P-selectin."; RL Cell 75:1179-1186(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., 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., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., 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., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA 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 project: RT 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 SELE, RP STRUCTURE OF CARBOHYDRATE, SUBUNIT, AND SIALIC ACID CONTENT. RC TISSUE=Neutrophil; RX PubMed=7521878; DOI=10.1016/s0021-9258(17)31656-3; 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 critical for RT P-selectin binding."; RL Cell 83:323-331(1995). RN [9] RP SULFATION, INTERACTION WITH SELP, AND MUTAGENESIS OF TYR-46; TYR-48; TYR-51 RP 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 sulfation RT 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 for RT 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 HL-60 RT 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 minimal RT 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 the RT 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; TYR-51 RP 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 core-2 RT 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 require RT tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin."; RL J. Biol. Chem. 278:26391-26400(2003). RN [17] RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SSL5 (MICROBIAL INFECTION). RX PubMed=17132726; DOI=10.1182/blood-2006-06-015461; RA Bestebroer J., Poppelier M.J., Ulfman L.H., Lenting P.J., Denis C.V., RA van Kessel K.P., van Strijp J.A., de Haas C.J.; RT "Staphylococcal superantigen-like 5 binds PSGL-1 and inhibits P-selectin- RT mediated neutrophil rolling."; RL Blood 109:2936-2943(2007). RN [18] RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SSL11 (MICROBIAL INFECTION). RX PubMed=18045383; DOI=10.1111/j.1365-2958.2007.05989.x; RA Chung M.C., Wines B.D., Baker H., Langley R.J., Baker E.N., Fraser J.D.; RT "The crystal structure of staphylococcal superantigen-like protein 11 in RT complex with sialyl Lewis X reveals the mechanism for cell binding and RT immune inhibition."; RL Mol. Microbiol. 66:1342-1355(2007). RN [19] 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., Bates B., RA Tchernychev B., Shaw G.D., Simon S.I.; RT "SLIC-1/sorting nexin 20: a novel sorting nexin that directs subcellular RT distribution of PSGL-1."; RL Eur. J. Immunol. 38:550-564(2008). RN [20] 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 [21] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBTEROVIRUS 71 CAPSID RP PROTEINS (MICROBIAL INFECTION). RX PubMed=19543284; DOI=10.1038/nm.1961; RA Nishimura Y., Shimojima M., Tano Y., Miyamura T., Wakita T., 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-406 AND SER-409, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP INTERACTION WITH HAVCR1. RX PubMed=24703780; DOI=10.1016/j.immuni.2014.03.004; RA Angiari S., Donnarumma T., Rossi B., Dusi S., Pietronigro E., Zenaro E., RA Della Bianca V., Toffali L., Piacentino G., Budui S., Rennert P., Xiao S., RA Laudanna C., Casasnovas J.M., Kuchroo V.K., Constantin G.; RT "TIM-1 glycoprotein binds the adhesion receptor P-selectin and mediates T RT cell trafficking during inflammation and autoimmunity."; RL Immunity 40:542-553(2014). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-68 IN COMPLEX WITH SELE AND RP 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-1."; RL Cell 103:467-479(2000). RN [25] RP ERRATUM OF PUBMED:11081633. RA Somers W.S., Tang J., Shaw G.D., Camphausen R.T.; RL Cell 105:971-971(2001). RN [26] RP VARIANT MET-249. RX PubMed=25102098; DOI=10.1038/jhg.2014.71; RA Saitsu H., Tohyama J., Walsh T., Kato M., Kobayashi Y., Lee M., RA Tsurusaki Y., Miyake N., Goto Y., Nishino I., Ohtake A., King M.C., RA Matsumoto N.; RT "A girl with West syndrome and autistic features harboring a de novo RT TBL1XR1 mutation."; RL J. Hum. Genet. 59:581-583(2014). CC -!- FUNCTION: A SLe(x)-type proteoglycan, which through high affinity, CC calcium-dependent interactions with E-, P- and L-selectins, mediates CC rapid rolling of leukocytes over vascular surfaces during the initial CC steps in inflammation. Critical for the initial leukocyte capture. CC {ECO:0000269|PubMed:11566773, ECO:0000269|PubMed:12403782}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for enterovirus 71. CC {ECO:0000269|PubMed:19543284}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Interaction with P-, E- and L- CC selectins, through their lectin/EGF domains, is required for promoting CC recruitment and rolling of leukocytes. These interactions require CC sialyl Lewis X glycan modification but there is a differing dependence CC for tyrosine sulfations. Sulfation on Tyr-51 of PSGL1 is most important CC for high affinity L-selectin/SELL binding while P-selectin/SELP CC requires sulfation on Tyr-48. E-selectin/SELE binds with much lower CC affinity and requires the sLe(x) epitope, but apparently not tyrosine CC sulfation. Dimerization appears not to be required for P-selectin/SELP CC binding. Interacts with SNX20. Interacts with MSN and SYK; mediates the CC activation of SYK by SELPLG. Interacts with HAVCR1 (PubMed:24703780). CC {ECO:0000269|PubMed:10713099, ECO:0000269|PubMed:11081633, CC ECO:0000269|PubMed:11566773, ECO:0000269|PubMed:12387735, CC ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:12736247, CC ECO:0000269|PubMed:18196517, ECO:0000269|PubMed:24703780, CC ECO:0000269|PubMed:7521878, ECO:0000269|PubMed:7559387, CC ECO:0000269|PubMed:7585949, ECO:0000269|PubMed:7585950}. CC -!- SUBUNIT: (Microbial infection) Interacts with enterovirus 71 capsid CC proteins. {ECO:0000269|PubMed:19543284}. CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus CC proteins SSL5 and SSL11; these interactions prevent SELPLG-mediated CC neutrophil rolling. {ECO:0000269|PubMed:18045383, CC ECO:0000269|PubMed:19543284}. CC -!- INTERACTION: CC Q14242; P16109: SELP; NbExp=4; IntAct=EBI-1030190, EBI-1030170; CC Q14242; Q7Z614: SNX20; NbExp=5; IntAct=EBI-1030190, EBI-744896; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane 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 -!- 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 ratio CC is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% CC fucose with alpha-1,3 linkage present in two forms: One species is a CC disialylated, monofucosylated glycan, and the other, a monosialylated, CC trifucosylated glycan with a polylactosamine backbone. The fucosylated CC forms carry the Lewis antigen and are important for interaction with CC selectins and for functioning in leukocyte rolling. The modification CC containing the sialyl Lewis X glycan is on Thr-57. No sulfated O- CC glycans. Some N-glycosylation. {ECO:0000269|PubMed:11081633, CC ECO:0000269|PubMed:12736247}. CC -!- PTM: Sulfation, in conjunction with the SLe(x)-containing glycan, is CC necessary for P- and L-selectin binding. High affinity P-selectin CC binding has a preferred requirement for the isomer sulfated on both CC Tyr-48 and Tyr-51, whereas L-selectin binding requires predominantly CC sulfation on Tyr-51 with sulfation on Tyr-48 playing only a minor role. CC These sulfations play an important role in L- and P-selectin-mediated CC neutrophil recruitment, and leukocyte rolling. CC {ECO:0000269|PubMed:11081633}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=P-selectin glycoprotein ligand 1 CC 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 PDB; 1G1S; X-ray; 1.90 A; C/D=42-60. DR PDBsum; 1G1S; -. DR AlphaFoldDB; Q14242; -. DR SMR; Q14242; -. DR BioGRID; 112304; 9. DR DIP; DIP-37668N; -. DR IntAct; Q14242; 7. DR STRING; 9606.ENSP00000228463; -. DR BindingDB; Q14242; -. DR ChEMBL; CHEMBL4183; -. DR DrugBank; DB16698; Neihulizumab. DR GlyConnect; 520; 6 O-Linked glycans. DR GlyCosmos; Q14242; 4 sites, 9 glycans. DR GlyGen; Q14242; 12 sites, 10 O-linked glycans (8 sites). DR iPTMnet; Q14242; -. DR PhosphoSitePlus; Q14242; -. DR BioMuta; SELPLG; -. DR DMDM; 2498904; -. DR EPD; Q14242; -. DR jPOST; Q14242; -. DR MassIVE; Q14242; -. DR MaxQB; Q14242; -. DR PaxDb; 9606-ENSP00000228463; -. DR PeptideAtlas; Q14242; -. DR ProteomicsDB; 59939; -. [Q14242-1] DR ABCD; Q14242; 1 sequenced antibody. DR Antibodypedia; 3720; 1226 antibodies from 41 providers. DR DNASU; 6404; -. DR Ensembl; ENST00000228463.6; ENSP00000228463.6; ENSG00000110876.10. [Q14242-2] DR Ensembl; ENST00000550948.2; ENSP00000447752.1; ENSG00000110876.10. [Q14242-1] DR GeneID; 6404; -. DR KEGG; hsa:6404; -. DR MANE-Select; ENST00000550948.2; ENSP00000447752.1; NM_003006.4; NP_002997.2. DR UCSC; uc001tni.4; human. [Q14242-1] DR AGR; HGNC:10722; -. DR CTD; 6404; -. DR DisGeNET; 6404; -. DR GeneCards; SELPLG; -. DR HGNC; HGNC:10722; SELPLG. DR HPA; ENSG00000110876; Tissue enhanced (lymphoid). DR MIM; 600738; gene. DR neXtProt; NX_Q14242; -. DR OpenTargets; ENSG00000110876; -. DR PharmGKB; PA35644; -. DR VEuPathDB; HostDB:ENSG00000110876; -. DR eggNOG; ENOG502S8ZU; Eukaryota. DR GeneTree; ENSGT00440000039754; -. DR HOGENOM; CLU_061579_0_0_1; -. DR InParanoid; Q14242; -. DR OMA; HTYPVRN; -. DR OrthoDB; 5324753at2759; -. DR PhylomeDB; Q14242; -. DR TreeFam; TF337792; -. DR PathwayCommons; Q14242; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR SignaLink; Q14242; -. DR SIGNOR; Q14242; -. DR BioGRID-ORCS; 6404; 18 hits in 1164 CRISPR screens. DR ChiTaRS; SELPLG; human. DR EvolutionaryTrace; Q14242; -. DR GeneWiki; P-selectin_glycoprotein_ligand-1; -. DR GenomeRNAi; 6404; -. DR Pharos; Q14242; Tbio. DR PRO; PR:Q14242; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q14242; Protein. DR Bgee; ENSG00000110876; Expressed in granulocyte and 181 other cell types or tissues. DR ExpressionAtlas; Q14242; baseline and differential. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0044853; C:plasma membrane raft; IDA:CAFA. DR GO; GO:0001931; C:uropod; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; NAS:ProtInc. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. 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; IDA:CAFA. DR GO; GO:0050901; P:leukocyte tethering or rolling; IDA:CAFA. DR IDEAL; IID00352; -. DR InterPro; IPR026195; PSGL-1. DR PANTHER; PTHR17384:SF7; P-SELECTIN GLYCOPROTEIN LIGAND 1; 1. DR PANTHER; PTHR17384; P-SELECTIN GLYCOPROTEIN LIGAND-1; 1. DR Genevisible; Q14242; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry; KW Host-virus interaction; Membrane; Phosphoprotein; KW Pyrrolidone carboxylic acid; Receptor; Reference proteome; Repeat; KW Sialic acid; Signal; Sulfation; Transmembrane; Transmembrane helix. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT PROPEP 18..41 FT /id="PRO_0000022302" FT CHAIN 42..412 FT /note="P-selectin glycoprotein ligand 1" FT /id="PRO_0000022303" FT TOPO_DOM 18..320 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 321..341 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 342..412 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 122..131 FT /note="1" FT REPEAT 132..141 FT /note="2" FT REPEAT 142..151 FT /note="3" FT REPEAT 162..171 FT /note="4" FT REPEAT 182..191 FT /note="5" FT REPEAT 192..201 FT /note="6" FT REPEAT 202..211 FT /note="7" FT REPEAT 212..221 FT /note="8" FT REPEAT 222..231 FT /note="9" FT REPEAT 232..241 FT /note="10" FT REPEAT 242..251 FT /note="11" FT REPEAT 252..261 FT /note="12" FT REGION 56..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 122..261 FT /note="12 X 10 AA tandem repeats" FT REGION 125..146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 166..252 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 374..412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 62..87 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 392..406 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 42 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:11081633" FT MOD_RES 46 FT /note="Sulfotyrosine" FT /evidence="ECO:0000269|PubMed:11081633" FT MOD_RES 48 FT /note="Sulfotyrosine" FT /evidence="ECO:0000269|PubMed:11081633" FT MOD_RES 51 FT /note="Sulfotyrosine" FT /evidence="ECO:0000269|PubMed:11081633" FT MOD_RES 406 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 57 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:11081633" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 320 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:10713099" FT VAR_SEQ 1 FT /note="M -> MAVGASGLEGDKMAGAM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044827" FT VARIANT 62 FT /note="M -> I (in dbSNP:rs2228315)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4" FT /id="VAR_019156" FT VARIANT 132..141 FT /note="Missing (in short form; not an alternative splicing; FT dbSNP:rs63748999)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7505206" FT /id="VAR_005611" FT VARIANT 246 FT /note="P -> S (in dbSNP:rs8179142)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_019157" FT VARIANT 249 FT /note="T -> M (in dbSNP:rs756234416)" FT /evidence="ECO:0000269|PubMed:25102098" FT /id="VAR_076761" FT MUTAGEN 44 FT /note="T->A: No effect on L-selectin binding nor neutrophil FT rolling." FT /evidence="ECO:0000269|PubMed:12403782" FT MUTAGEN 46..52 FT /note="YEYLDYD->FEFLDFE: No sulfation. Almost complete loss FT of P-selectin binding. No effect on E-selectin binding." FT /evidence="ECO:0000269|PubMed:7585949" FT MUTAGEN 46..51 FT /note="YEYLDY->FEFLDF: No sulfation. Almost complete loss FT of P-selectin binding. No effect on E-selectin binding." FT MUTAGEN 46 FT /note="Y->F: Binding L-selectin reduced by 20%, neutrophil FT recruitment reduced by 30%, and lymphocyte rolling reduced FT by 32%; when associated with F-48. Binding L-selectin FT reduced by 86%, neutrophil recruitment reduced by 75%, and FT lymphocyte rolling reduced by 69%; when associated with FT F-51. Binding L-selectin reduced by 89%, and neutrophil FT recruitment reduced by 90%; when associated with F-48 and FT F-51. Binding of L-selectin reduced by 91%; when associated FT with F-48; F-51 and A-57." FT /evidence="ECO:0000269|PubMed:7585950" FT MUTAGEN 48 FT /note="Y->F: Binding L-selectin reduced by 20%, neutrophil FT recruitment reduced by 30%, and lymphocyte rolling reduced FT by 32%; when associated with F-46. Binding L-lectin reduced FT by 31%, neutrophil recruitment reduced by 52%, and FT lymphocyte rolling reduced by 52%; when associated with FT F-51. Binding L-selectin reduced by 89%, and neutrophil FT recruitment reduced by 90%; when associated with F-46 and FT F-51. Binding of L-selectin reduced by 91%; when associated FT with F-46; F-51 and A-57." FT /evidence="ECO:0000269|PubMed:12403782, FT ECO:0000269|PubMed:7585950" FT MUTAGEN 51 FT /note="Y->F: Binding L-selectin reduced by 86%, neutrophil FT recruitment reduced by 75% and, lymphocyte rolling reduced FT by 69%; when associated with F-46. Binding L-selectin FT reduced by 31%, neutrophil recruitment reduced by 52%, and FT lymphocyte rolling reduced by 52%; when associated with FT F-48; Binding L-selectin reduced by 89%, and neutrophil FT recruitment reduced by 90%; when associated with F-46 and FT F-48. Binding of L-selectin reduced by 91%; when associated FT with F-46; F-48 and A-57." FT /evidence="ECO:0000269|PubMed:12403782, FT ECO:0000269|PubMed:7585950" FT MUTAGEN 57 FT /note="T->A: No E- nor P-selectin binding, and very little FT neutrophil rolling. Binding of L-selectin reduced by 91%; FT when associated with F-46; F-48 and F-51." FT /evidence="ECO:0000269|PubMed:12403782, FT ECO:0000269|PubMed:7585950" FT MUTAGEN 320 FT /note="C->A,S: No dimer formation. No effect on P-selectin FT binding." FT /evidence="ECO:0000269|PubMed:10713099" FT CONFLICT 23..39 FT /note="Missing (in Ref. 3; BAC05283)" FT /evidence="ECO:0000305" FT CONFLICT 50 FT /note="D -> E (in Ref. 3; BAC05283)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="M -> T (in Ref. 3; BAC05283)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="Q -> R (in Ref. 3; BAH12863)" FT /evidence="ECO:0000305" FT CONFLICT 396 FT /note="P -> A (in Ref. 3; BAC05283)" FT /evidence="ECO:0000305" FT TURN 51..53 FT /evidence="ECO:0007829|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 //