SELPL_HUMAN
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 03-AUG-2022, entry version 190.
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/";
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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; 7.
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 GlyGen; Q14242; 5 sites, 9 O-linked glycans (1 site).
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; Q14242; -.
DR PeptideAtlas; Q14242; -.
DR PRIDE; Q14242; -.
DR ProteomicsDB; 59939; -. [Q14242-1]
DR ABCD; Q14242; 1 sequenced antibody.
DR Antibodypedia; 3720; 1085 antibodies from 40 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 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; 1055530at2759; -.
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; 15 hits in 1082 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 179 other tissues.
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: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:0030097; P:hemopoiesis; IBA:GO_Central.
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; PTHR17384; 1.
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 F-
FT 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 F-
FT 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 F-
FT 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
