[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Placenta; DOI=10.1074/jbc.270.27.16470; PubMed=7541799 [NCBI, ExPASy, EBI, Israel, Japan] 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], AND VARIANT 132-GLN--ALA-141 DEL. DOI=10.1016/0092-8674(93)90327-M; PubMed=7505206 [NCBI, ExPASy, EBI, Israel, Japan] 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 [GENOMIC DNA], AND VARIANTS ILE-62 AND SER-246. SeattleSNPs program for genomic applications; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT 132-GLN--ALA-141 DEL. TISSUE=Uterus; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT 132-GLN--ALA-141 DEL. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	PROTEIN SEQUENCE OF 350-355 AND 390-396, INTERACTION WITH SELP AND SELE, CARBOHYDRATE STRUCTURE, SUBUNIT, AND SIALIC ACID CONTENT. TISSUE=Neutrophil; PubMed=7521878 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	SULFATION, INTERACTION WITH SELP, AND MUTAGENESIS OF 46-TYR--ASP-52. DOI=10.1016/0092-8674(95)90173-6; PubMed=7585949 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	SULFATION, INTERACTION WITH SELP, AND MUTAGENESIS OF TYR-46; TYR-48; TYR-51 AND THR-57. DOI=10.1016/0092-8674(95)90174-4; PubMed=7585950 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	SULFATION, AND INTERACTION WITH SELP. DOI=10.1074/jbc.270.39.22677; PubMed=7559387 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	STRUCTURE OF O-LINKED CARBOHYDRATES. DOI=10.1074/jbc.271.31.18732; PubMed=8702529 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	INTERACTION WITH SELP, DISULFIDE BOND AT CYS-320, AND MUTAGENESIS OF CYS-320. DOI=10.1074/jbc.275.11.7839; PubMed=10713099 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	INTERACTION WITH SELE AND SELP, SULFATION, AND FUNCTION. PubMed=11566773 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	INTERACTION WITH SELL, FUNCTION, AND MUTAGENESIS OF THR-44; TYR-48; TYR-51 AND THR-57. DOI=10.1074/jbc.M204360200; PubMed=12403782 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	INTERACTION WITH SELL, SULFATION, AND GYCOSYLATION. DOI=10.1074/jbc.M303551200; PubMed=12736247 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	INTERACTION WITH SNX20. DOI=10.1002/eji.200737777; PubMed=18196517 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	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, GLYCOLYSATION AT THR-57, AND PYROGLUTAMATE FORMATION AT GLN-42. DOI=10.1016/S0092-8674(00)00138-0; PubMed=11081633 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	ERRATUM. Somers W.S., Tang J., Shaw G.D., Camphausen R.T.; Cell 105:971-971(2001).

Comments

FUNCTION: A SLe(x)-type glycan, 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. PSGL1 is critical for the initial leukocyte capture.
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.
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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.
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.
WEB RESOURCE: Name=Wikipedia; Note=P-selectin glycoprotein ligand 1 entry; URL="http://en.wikipedia.org/wiki/P-selectin_glycoprotein_ligand-1";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/selplg/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U25956; AAA74577.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U02297; AAC50061.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY331789; AAP81163.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK098315; BAC05283.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029782; AAH29782.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A57468; A57468.

NP_002997.1; -.

3D structure databases

PDB

1G1S; X-ray; 1.90 A; C/D=42-68.

[ExPASy / RCSB / EBI]

PDBsum

1G1S; -.

ModBase

Q14242.

Protein-protein interaction databases

IntAct

Q14242; -.

PTM databases

GlycoSuiteDB

Q14242; -.

Organism-specific databases

HGNC:10722; SELPLG.

CAB002431; -.

600738; gene. [NCBI / EBI]

PharmGKB

PA35644; -.

GeneCards

Q14242.

Gene expression databases

ArrayExpress

Q14242; -.

CleanEx

HS_SELPLG; -.

GermOnline

ENSG00000110876; Homo sapiens.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005624;	Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0008367;	Molecular function: bacterial binding (traceable author statement from ProtInc).
GO:0005102;	Molecular function: receptor binding (non-traceable author statement from ProtInc).
GO:0007155;	Biological process: cell adhesion (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

BLOCKS

Q14242.

Genome annotation databases

Ensembl

ENSG00000110876; Homo sapiens. [Contig view]

GeneID

6404; -.

KEGG

hsa:6404; -.

Phylogenomic databases

HOGENOM

Q14242; -.

HOVERGEN

Q14242; -.

Other

LinkHub

Q14242; -.

SOURCE

SELPLG; Homo sapiens.

ProtoNet

Q14242.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell adhesion; Cleavage on pair of basic residues; Direct protein sequencing; Glycoprotein; Membrane; Polymorphism; Pyrrolidone carboxylic acid; Repeat; Sialic acid; Signal; Sulfation; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Potential.`
`PROPEP`	`18 41`	`24`		`PRO_0000022302`
`CHAIN`	`42 412`	`371`	`P-selectin glycoprotein ligand 1.`	`PRO_0000022303`
`TOPO_DOM`	`18 320`	`303`	`Extracellular (Potential).`
`TRANSMEM`	`321 341`	`21`	`Potential.`
`TOPO_DOM`	`342 412`	`71`	`Cytoplasmic (Potential).`
`REPEAT`	`122 131`	`10`	`1.`
`REPEAT`	`132 141`	`10`	`2.`
`REPEAT`	`142 151`	`10`	`3.`
`REPEAT`	`162 171`	`10`	`4.`
`REPEAT`	`182 191`	`10`	`5.`
`REPEAT`	`192 201`	`10`	`6.`
`REPEAT`	`202 211`	`10`	`7.`
`REPEAT`	`212 221`	`10`	`8.`
`REPEAT`	`222 231`	`10`	`9.`
`REPEAT`	`232 241`	`10`	`10.`
`REPEAT`	`242 251`	`10`	`11.`
`REPEAT`	`252 261`	`10`	`12.`
`REGION`	`122 261`	`140`	`12 X 10 AA tandem repeats.`
`MOD_RES`	`42 42`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`46 46`		`Sulfotyrosine.`
`MOD_RES`	`48 48`		`Sulfotyrosine.`
`MOD_RES`	`51 51`		`Sulfotyrosine.`
`CARBOHYD`	`57 57`		`O-linked (GalNAc...).`
`CARBOHYD`	`65 65`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`111 111`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`302 302`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`320 320`		`Interchain.`
`VARIANT`	`62 62`	`1`	`M -> I (in dbSNP:rs2228315 [NCBI]).`	`VAR_019156`
`VARIANT`	`132 141`	`10`	`Missing (in short form; not an alternative splicing).`	`VAR_005611`
`VARIANT`	`246 246`	`1`	`P -> S (in dbSNP:rs8179142 [NCBI]).`	`VAR_019157`
`MUTAGEN`	`44 44`		`T->A: No effect on L-selectin binding nor neutrophil rolling.`
`MUTAGEN`	`46 52`		`YEYLDYD->FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding.`
`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.`
`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.`
`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.`
`MUTAGEN`	`57 57`		`T->A: No E- nor P-selctin binding, and very little neutrophil rolling. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and F-51.`
`MUTAGEN`	`320 320`		`C->A,S: No dimer formation. No effect on P-selectin binding.`
`CONFLICT`	`23 39`		`Missing (in Ref. 4; BAC05283).`
`CONFLICT`	`50 50`		`D -> E (in Ref. 4; BAC05283).`
`CONFLICT`	`219 219`		`M -> T (in Ref. 4; BAC05283).`
`CONFLICT`	`396 396`		`P -> A (in Ref. 4; BAC05283).`
`TURN`	`51 53`	`3`

Sequence information

Length: 412 AA [This is the length of the unprocessed precursor]

Molecular weight: 43201 Da [This is the MW of the unprocessed precursor]

CRC64: A92A2A902DC9963A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPLQLLLLLI LLGPGNSLQL WDTWADEAEK ALGPLLARDR RQATEYEYLD YDFLPETEPP 

        70         80         90        100        110        120 
EMLRNSTDTT PLTGPGTPES TTVEPAARRS TGLDAGGAVT ELTTELANMG NLSTDSAAME 

       130        140        150        160        170        180 
IQTTQPAATE AQTTQPVPTE AQTTPLAATE AQTTRLTATE AQTTPLAATE AQTTPPAATE 

       190        200        210        220        230        240 
AQTTQPTGLE AQTTAPAAME AQTTAPAAME AQTTPPAAME AQTTQTTAME AQTTAPEATE 

       250        260        270        280        290        300 
AQTTQPTATE AQTTPLAAME ALSTEPSATE ALSMEPTTKR GLFIPFSVSS VTHKGIPMAA 

       310        320        330        340        350        360 
SNLSVNYPVG APDHISVKQC LLAILILALV ATIFFVCTVV LAVRLSRKGH MYPVRNYSPT 

       370        380        390        400        410 
EMVCISSLLP DGGEGPSATA NGGLSKAKSP GLTPEPREDR EGDDLTLHSF LP

Q14242 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools