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P-selectin glycoprotein ligand 1 (PSGL-1) (Selectin P ligand) (CD antigen CD162)

 SELPL_HUMAN             Reviewed;         412 AA.
Q14242; A8K2Y0; B4DQC3; B7Z5C7; J3KMX6; Q12775; Q6GTW7; Q8N7J7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 163.
RecName: Full=P-selectin glycoprotein ligand 1;
Short=PSGL-1;
AltName: Full=Selectin P ligand;
AltName: CD_antigen=CD162;
Flags: Precursor;
Name=SELPLG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=7541799; DOI=10.1074/jbc.270.27.16470;
Veldman G.M., Bean K.M., Cumming D.A., Eddy R.L., Sait S.N.J.,
Shows T.B.;
"Genomic organization and chromosomal localization of the gene
encoding human P-selectin glycoprotein ligand.";
J. Biol. Chem. 270:16470-16475(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 132-GLN--ALA-141
DEL.
PubMed=7505206; DOI=10.1016/0092-8674(93)90327-M;
Sako D., Chang X.J., Barone K.M., Vachino G., White H.M., Shaw G.,
Veldman G.M., Bean K.M., Ahern T.J., Furie B., Cumming D.A.,
Larsen G.R.;
"Expression cloning of a functional glycoprotein ligand for P-
selectin.";
Cell 75:1179-1186(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS ILE-62 AND 132-GLN--ALA-141 DEL.
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-62 AND SER-246.
SeattleSNPs variation discovery resource;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
132-GLN--ALA-141 DEL.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 350-355 AND 390-396, INTERACTION WITH SELP AND
SELE, STRUCTURE OF CARBOHYDRATE, SUBUNIT, AND SIALIC ACID CONTENT.
TISSUE=Neutrophil;
PubMed=7521878;
Moore K.L., Eaton S.F., Lyons D.E., Lichenstein H.S., Cummings R.D.,
McEver R.P.;
"The P-selectin glycoprotein ligand from human neutrophils displays
sialylated, fucosylated, O-linked poly-N-acetyllactosamine.";
J. Biol. Chem. 269:23318-23327(1994).
[8]
SULFATION, INTERACTION WITH SELP, AND MUTAGENESIS OF 46-TYR--ASP-52.
PubMed=7585949; DOI=10.1016/0092-8674(95)90173-6;
Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A.,
Shaw G.D.;
"A sulfated peptide segment at the amino terminus of PSGL-1 is
critical for P-selectin binding.";
Cell 83:323-331(1995).
[9]
SULFATION, INTERACTION WITH SELP, AND MUTAGENESIS OF TYR-46; TYR-48;
TYR-51 AND THR-57.
PubMed=7585950; DOI=10.1016/0092-8674(95)90174-4;
Pouyani T., Seed B.;
"PSGL-1 recognition of P-selectin is controlled by a tyrosine
sulfation consensus at the PSGL-1 amino terminus.";
Cell 83:333-343(1995).
[10]
SULFATION, AND INTERACTION WITH SELP.
PubMed=7559387; DOI=10.1074/jbc.270.39.22677;
Wilkins P.P., Moore K.L., McEver R.P., Cummings R.D.;
"Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required
for high affinity binding to P-selectin.";
J. Biol. Chem. 270:22677-22680(1995).
[11]
STRUCTURE OF O-LINKED CARBOHYDRATES.
PubMed=8702529; DOI=10.1074/jbc.271.31.18732;
Wilkins P.P., McEver R.P., Cummings R.D.;
"Structures of the O-glycans on P-selectin glycoprotein ligand-1 from
HL-60 cells.";
J. Biol. Chem. 271:18732-18742(1996).
[12]
INTERACTION WITH SELP, DISULFIDE BOND AT CYS-320, AND MUTAGENESIS OF
CYS-320.
PubMed=10713099; DOI=10.1074/jbc.275.11.7839;
Epperson T.K., Patel K.D., McEver R.P., Cummings R.D.;
"Noncovalent association of P-selectin glycoprotein ligand-1 and
minimal determinants for binding to P-selectin.";
J. Biol. Chem. 275:7839-7853(2000).
[13]
INTERACTION WITH SELE AND SELP, SULFATION, AND FUNCTION.
PubMed=11566773; DOI=10.1016/S0006-3495(01)75850-X;
Rodgers S.D., Camphausen R.T., Hammer D.A.;
"Tyrosine sulfation enhances but is not required for PSGL-1 rolling
adhesion on P-selectin.";
Biophys. J. 81:2001-2009(2001).
[14]
INTERACTION WITH MSN AND SYK.
PubMed=12387735; DOI=10.1016/S1074-7613(02)00420-X;
Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A.,
Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J.,
Sanchez-Madrid F.;
"ITAM-based interaction of ERM proteins with Syk mediates signaling by
the leukocyte adhesion receptor PSGL-1.";
Immunity 17:401-412(2002).
[15]
INTERACTION WITH SELL, FUNCTION, AND MUTAGENESIS OF THR-44; TYR-48;
TYR-51 AND THR-57.
PubMed=12403782; DOI=10.1074/jbc.M204360200;
Bernimoulin M.P., Zeng X.-L., Abbal C., Giraud S., Martinez M.,
Michielin O., Schapira M., Spertini O.;
"Molecular basis of leukocyte rolling on PSGL-1. Predominant role of
core-2 O-glycans and of tyrosine sulfate residue 51.";
J. Biol. Chem. 278:37-47(2003).
[16]
INTERACTION WITH SELL, SULFATION, AND GLYCOSYLATION.
PubMed=12736247; DOI=10.1074/jbc.M303551200;
Leppaenen A., Yago T., Otto V.I., McEver R.P., Cummings R.D.;
"Model glycosulfopeptides from P-selectin glycoprotein ligand-1
require tyrosine sulfation and a core 2-branched O-glycan to bind to
L-selectin.";
J. Biol. Chem. 278:26391-26400(2003).
[17]
INTERACTION WITH SNX20.
PubMed=18196517; DOI=10.1002/eji.200737777;
Schaff U.Y., Shih H.H., Lorenz M., Sako D., Kriz R., Milarski K.,
Bates B., Tchernychev B., Shaw G.D., Simon S.I.;
"SLIC-1/sorting nexin 20: a novel sorting nexin that directs
subcellular distribution of PSGL-1.";
Eur. J. Immunol. 38:550-564(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBTEROVIRUS 71
CAPSID PROTEINS.
PubMed=19543284; DOI=10.1038/nm.1961;
Nishimura Y., Shimojima M., Tano Y., Miyamura T., Wakita T.,
Shimizu H.;
"Human P-selectin glycoprotein ligand-1 is a functional receptor for
enterovirus 71.";
Nat. Med. 15:794-797(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-406 AND SER-409, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-68 IN COMPLEX WITH SELE
AND SELP LECTIN/EGF DOMAINS, SULFATION AT TYR-46; TYR-48 AND TYR-51,
GLYCOSYLATION AT THR-57, AND PYROGLUTAMATE FORMATION AT GLN-42.
PubMed=11081633; DOI=10.1016/S0092-8674(00)00138-0;
Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
"Insights into the molecular basis of leukocyte tethering and rolling
revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-
1.";
Cell 103:467-479(2000).
[22]
ERRATUM.
Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
Cell 105:971-971(2001).
[23]
VARIANT MET-249.
PubMed=25102098; DOI=10.1038/jhg.2014.71;
Saitsu H., Tohyama J., Walsh T., Kato M., Kobayashi Y., Lee M.,
Tsurusaki Y., Miyake N., Goto Y., Nishino I., Ohtake A., King M.C.,
Matsumoto N.;
"A girl with West syndrome and autistic features harboring a de novo
TBL1XR1 mutation.";
J. Hum. Genet. 59:581-583(2014).
-!- FUNCTION: A SLe(x)-type proteoglycan, which through high affinity,
calcium-dependent interactions with E-, P- and L-selectins,
mediates rapid rolling of leukocytes over vascular surfaces during
the initial steps in inflammation. Critical for the initial
leukocyte capture. {ECO:0000269|PubMed:11566773,
ECO:0000269|PubMed:12403782}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for enterovirus
71. {ECO:0000269|PubMed:19543284}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interaction with P-, E- and
L-selectins, through their lectin/EGF domains, is required for
promoting recruitment and rolling of leukocytes. These
interactions require sialyl Lewis X glycan modification but there
is a differing dependence for tyrosine sulfations. Sulfation on
Tyr-51 of PSGL1 is most important for high affinity L-
selectin/SELL binding while P-selectin/SELP requires sulfation on
Tyr-48. E-selectin/SELE binds with much lower affinity and
requires the sLe(x) epitope, but apparantly not tyrosine
sulfation. Dimerization appears not to be required for P-
selectin/SELP binding. Interacts with SNX20. Interacts with MSN
and SYK; mediates the activation of SYK by SELPLG.
{ECO:0000269|PubMed:10713099, ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:11566773, ECO:0000269|PubMed:12387735,
ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:12736247,
ECO:0000269|PubMed:18196517, ECO:0000269|PubMed:7521878,
ECO:0000269|PubMed:7559387, ECO:0000269|PubMed:7585949,
ECO:0000269|PubMed:7585950}.
-!- SUBUNIT: (Microbial infection) Interacts with enterovirus 71
capsid proteins. {ECO:0000269|PubMed:19543284}.
-!- INTERACTION:
P16109:SELP; NbExp=4; IntAct=EBI-1030190, EBI-1030170;
Q7Z614:SNX20; NbExp=5; IntAct=EBI-1030190, EBI-744896;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14242-1; Sequence=Displayed;
Name=2;
IsoId=Q14242-2; Sequence=VSP_044827;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed on neutrophils, monocytes and most
lymphocytes.
-!- PTM: Displays complex, core-2, sialylated and fucosylated O-linked
oligosaccharides, at least some of which appear to contain poly-N-
acetyllactosamine with varying degrees of substitution. Mainly
disialylated or neutral forms of the core-2 tetrasaccharide,
Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN
ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains
about 14% fucose with alpha-1,3 linkage present in two forms: One
species is a disialylated, monofucosylated glycan, and the other,
a monosialylated, trifucosylated glycan with a polylactosamine
backbone. The fucosylated forms carry the Lewis antigen and are
important for interaction with selectins and for functioning in
leukocyte rolling. The modification containing the sialyl Lewis X
glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation.
{ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:12736247}.
-!- PTM: Sulfation, in conjunction with the SLe(x)-containing glycan,
is necessary for P- and L-selectin binding. High affinity P-
selectin binding has a preferred requirement for the isomer
sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding
requires predominantly sulfation on Tyr-51 with sulfation on Tyr-
48 playing only a minor role. These sulfations play an important
role in L- and P-selectin-mediated neutrophil recruitment, and
leukocyte rolling. {ECO:0000269|PubMed:11081633}.
-!- WEB RESOURCE: Name=Wikipedia; Note=P-selectin glycoprotein ligand
1 entry;
URL="https://en.wikipedia.org/wiki/P-selectin_glycoprotein_ligand-1";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/selplg/";
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EMBL; U25956; AAA74577.1; -; Genomic_DNA.
EMBL; U02297; AAC50061.1; -; mRNA.
EMBL; AK098315; BAC05283.1; -; mRNA.
EMBL; AK290395; BAF83084.1; -; mRNA.
EMBL; AK298738; BAG60885.1; -; mRNA.
EMBL; AK298742; BAH12863.1; -; mRNA.
EMBL; AY331789; AAP81163.1; -; Genomic_DNA.
EMBL; AC007569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029782; AAH29782.1; -; mRNA.
CCDS; CCDS31895.2; -. [Q14242-1]
CCDS; CCDS55881.1; -. [Q14242-2]
PIR; A57468; A57468.
RefSeq; NP_001193538.1; NM_001206609.1. [Q14242-2]
RefSeq; NP_002997.2; NM_003006.4. [Q14242-1]
UniGene; Hs.591014; -.
PDB; 1G1S; X-ray; 1.90 A; C/D=42-60.
PDBsum; 1G1S; -.
ProteinModelPortal; Q14242; -.
SMR; Q14242; -.
BioGrid; 112304; 6.
DIP; DIP-37668N; -.
IntAct; Q14242; 7.
STRING; 9606.ENSP00000228463; -.
BindingDB; Q14242; -.
ChEMBL; CHEMBL4183; -.
GlyConnect; 520; -.
iPTMnet; Q14242; -.
PhosphoSitePlus; Q14242; -.
UniCarbKB; Q14242; -.
BioMuta; SELPLG; -.
DMDM; 2498904; -.
EPD; Q14242; -.
MaxQB; Q14242; -.
PaxDb; Q14242; -.
PeptideAtlas; Q14242; -.
PRIDE; Q14242; -.
DNASU; 6404; -.
Ensembl; ENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2]
Ensembl; ENST00000550948; ENSP00000447752; ENSG00000110876. [Q14242-1]
GeneID; 6404; -.
KEGG; hsa:6404; -.
UCSC; uc001tni.4; human. [Q14242-1]
CTD; 6404; -.
DisGeNET; 6404; -.
EuPathDB; HostDB:ENSG00000110876.9; -.
GeneCards; SELPLG; -.
H-InvDB; HIX0010969; -.
HGNC; HGNC:10722; SELPLG.
HPA; CAB002431; -.
MIM; 600738; gene.
neXtProt; NX_Q14242; -.
OpenTargets; ENSG00000110876; -.
PharmGKB; PA35644; -.
eggNOG; ENOG410JASD; Eukaryota.
eggNOG; ENOG410Y5S5; LUCA.
GeneTree; ENSGT00440000039754; -.
HOGENOM; HOG000013048; -.
HOVERGEN; HBG061628; -.
InParanoid; Q14242; -.
KO; K06544; -.
OMA; NYSPTEM; -.
OrthoDB; EOG091G0BCI; -.
PhylomeDB; Q14242; -.
TreeFam; TF337792; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
SIGNOR; Q14242; -.
ChiTaRS; SELPLG; human.
EvolutionaryTrace; Q14242; -.
GeneWiki; P-selectin_glycoprotein_ligand-1; -.
GenomeRNAi; 6404; -.
PMAP-CutDB; A8K2Y0; -.
PRO; PR:Q14242; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000110876; -.
CleanEx; HS_SELPLG; -.
ExpressionAtlas; Q14242; baseline and differential.
Genevisible; Q14242; HS.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IDA:CAFA.
GO; GO:0001931; C:uropod; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; NAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0071354; P:cellular response to interleukin-6; IDA:MGI.
GO; GO:0050902; P:leukocyte adhesive activation; ISS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; IDA:CAFA.
GO; GO:0050901; P:leukocyte tethering or rolling; IDA:CAFA.
InterPro; IPR026195; PSGL-1.
PANTHER; PTHR17384; PTHR17384; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Membrane;
Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid; Receptor;
Reference proteome; Repeat; Sialic acid; Signal; Sulfation;
Transmembrane; Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 41
/FTId=PRO_0000022302.
CHAIN 42 412 P-selectin glycoprotein ligand 1.
/FTId=PRO_0000022303.
TOPO_DOM 18 320 Extracellular. {ECO:0000255}.
TRANSMEM 321 341 Helical. {ECO:0000255}.
TOPO_DOM 342 412 Cytoplasmic. {ECO:0000255}.
REPEAT 122 131 1.
REPEAT 132 141 2.
REPEAT 142 151 3.
REPEAT 162 171 4.
REPEAT 182 191 5.
REPEAT 192 201 6.
REPEAT 202 211 7.
REPEAT 212 221 8.
REPEAT 222 231 9.
REPEAT 232 241 10.
REPEAT 242 251 11.
REPEAT 252 261 12.
REGION 122 261 12 X 10 AA tandem repeats.
MOD_RES 42 42 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:11081633}.
MOD_RES 46 46 Sulfotyrosine.
{ECO:0000269|PubMed:11081633}.
MOD_RES 48 48 Sulfotyrosine.
{ECO:0000269|PubMed:11081633}.
MOD_RES 51 51 Sulfotyrosine.
{ECO:0000269|PubMed:11081633}.
MOD_RES 406 406 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 57 57 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:11081633}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 320 320 Interchain.
{ECO:0000269|PubMed:10713099}.
VAR_SEQ 1 1 M -> MAVGASGLEGDKMAGAM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044827.
VARIANT 62 62 M -> I (in dbSNP:rs2228315).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.4}.
/FTId=VAR_019156.
VARIANT 132 141 Missing (in short form; not an
alternative splicing; dbSNP:rs63748999).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7505206}.
/FTId=VAR_005611.
VARIANT 246 246 P -> S (in dbSNP:rs8179142).
{ECO:0000269|Ref.4}.
/FTId=VAR_019157.
VARIANT 249 249 T -> M (in dbSNP:rs756234416).
{ECO:0000269|PubMed:25102098}.
/FTId=VAR_076761.
MUTAGEN 44 44 T->A: No effect on L-selectin binding nor
neutrophil rolling.
{ECO:0000269|PubMed:12403782}.
MUTAGEN 46 52 YEYLDYD->FEFLDFE: No sulfation. Almost
complete loss of P-selectin binding. No
effect on E-selectin binding.
{ECO:0000269|PubMed:7585949}.
MUTAGEN 46 51 YEYLDY->FEFLDF: No sulfation. Almost
complete loss of P-selectin binding. No
effect on E-selectin binding.
MUTAGEN 46 46 Y->F: Binding L-selectin reduced by 20%,
neutrophil recruitment reduced by 30%,
and lymphocyte rolling reduced by 32%;
when associated with F-48. Binding L-
selectin reduced by 86%, neutrophil
recruitment reduced by 75%, and
lymphocyte rolling reduced by 69%; when
associated with F-51. Binding L-selectin
reduced by 89%, and neutrophil
recruitment reduced by 90%; when
associated with F-48 and F-51. Binding of
L-selectin reduced by 91%; when
associated with F-48; F-51 and A-57.
{ECO:0000269|PubMed:7585950}.
MUTAGEN 48 48 Y->F: Binding L-selectin reduced by 20%,
neutrophil recruitment reduced by 30%,
and lymphocyte rolling reduced by 32%;
when associated with F-46. Binding L-
lectin reduced by 31%, neutrophil
recruitment reduced by 52%, and
lymphocyte rolling reduced by 52%; when
associated with F-51. Binding L-selectin
reduced by 89%, and neutrophil
recruitment reduced by 90%; when
associated with F-46 and F-51. Binding of
L-selectin reduced by 91%; when
associated with F-46; F-51 and A-57.
{ECO:0000269|PubMed:12403782,
ECO:0000269|PubMed:7585950}.
MUTAGEN 51 51 Y->F: Binding L-selectin reduced by 86%,
neutrophil recruitment reduced by 75%
and, lymphocyte rolling reduced by 69%;
when associated with F-46. Binding L-
selectin reduced by 31%, neutrophil
recruitment reduced by 52%, and
lymphocyte rolling reduced by 52%; when
associated with F-48; Binding L-selectin
reduced by 89%, and neutrophil
recruitment reduced by 90%; when
associated with F-46 and F-48. Binding of
L-selectin reduced by 91%; when
associated with F-46; F-48 and A-57.
{ECO:0000269|PubMed:12403782,
ECO:0000269|PubMed:7585950}.
MUTAGEN 57 57 T->A: No E- nor P-selectin binding, and
very little neutrophil rolling. Binding
of L-selectin reduced by 91%; when
associated with F-46; F-48 and F-51.
{ECO:0000269|PubMed:12403782,
ECO:0000269|PubMed:7585950}.
MUTAGEN 320 320 C->A,S: No dimer formation. No effect on
P-selectin binding.
{ECO:0000269|PubMed:10713099}.
CONFLICT 23 39 Missing (in Ref. 3; BAC05283).
{ECO:0000305}.
CONFLICT 50 50 D -> E (in Ref. 3; BAC05283).
{ECO:0000305}.
CONFLICT 219 219 M -> T (in Ref. 3; BAC05283).
{ECO:0000305}.
CONFLICT 222 222 Q -> R (in Ref. 3; BAH12863).
{ECO:0000305}.
CONFLICT 396 396 P -> A (in Ref. 3; BAC05283).
{ECO:0000305}.
TURN 51 53 {ECO:0000244|PDB:1G1S}.
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


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