Reviewed,
UniProtKB/Swiss-Prot Q14242 (SELPL_HUMAN)
Last modified
November 25, 2008.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: P-selectin glycoprotein ligand 1 Short name=PSGL-1 Short name=Selectin P ligand Alternative name(s): CD_antigen=CD162 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 412 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (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 structure | 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 | |
| Tissue specificity | Expressed on neutrophils, monocytes and most lymphocytes. |
| Post-translational modification | 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. 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. |
Ontologies
Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Membrane |
| Coding sequence diversity | Polymorphism |
| Domain | Repeat Signal Transmembrane |
| Ligand | Sialic acid |
| PTM | Cleavage on pair of basic residues Glycoprotein Phosphoprotein Pyrrolidone carboxylic acid Sulfation |
| Technical term | 3D-structure Direct protein sequencing |
Gene Ontology (GO) | |
| Cellular component | integral to plasma membrane Ref.2 Traceable author statement. Source: ProtInc membrane fraction Ref.2Traceable author statement. Source: ProtInc |
| Molecular function | bacterial binding Traceable author statement. Source: ProtInc receptor binding Ref.2Non-traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Potential | ||||||||
| Propeptide | 18 – 41 | 24 | PRO_0000022302 | ||||||||
| Chain | 42 – 412 | 371 | P-selectin glycoprotein ligand 1 | PRO_0000022303 | |||||||
Regions | |||||||||||
| Topological domain | 18 – 320 | 303 | Extracellular Potential | ||||||||
| Transmembrane | 321 – 341 | 21 | Potential | ||||||||
| Topological domain | 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 | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 42 | 1 | Pyrrolidone carboxylic acid | ||||||||
| Modified residue | 46 | 1 | Sulfotyrosine | ||||||||
| Modified residue | 48 | 1 | Sulfotyrosine | ||||||||
| Modified residue | 51 | 1 | Sulfotyrosine | ||||||||
| Modified residue | 389 | 1 | Phosphoserine | ||||||||
| Modified residue | 393 | 1 | Phosphothreonine | ||||||||
| Glycosylation | 57 | 1 | O-linked (GalNAc...) | ||||||||
| Glycosylation | 65 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 111 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 302 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 320 | Interchain | |||||||||
Natural variations | |||||||||||
| Natural variant | 62 | 1 | M → I: dbSNP rs2228315. | VAR_019156 | |||||||
| Natural variant | 132 – 141 | 10 | Missing in short form; not an alternative splicing. | VAR_005611 | |||||||
| Natural variant | 246 | 1 | P → S: dbSNP rs8179142. | VAR_019157 | |||||||
Experimental info | |||||||||||
| Mutagenesis | 44 | 1 | T → A: No effect on L-selectin binding nor neutrophil rolling | ||||||||
| Mutagenesis | 46 – 52 | 7 | YEYLDYD → FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding | ||||||||
| Mutagenesis | 46 – 51 | 6 | YEYLDY → FEFLDF: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding | ||||||||
| Mutagenesis | 46 | 1 | 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 | ||||||||
| Mutagenesis | 48 | 1 | 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 | ||||||||
| Mutagenesis | 51 | 1 | 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 | ||||||||
| Mutagenesis | 57 | 1 | 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 | ||||||||
| Mutagenesis | 320 | 1 | C → A or S: No dimer formation. No effect on P-selectin binding | ||||||||
| Sequence conflict | 23 – 39 | 17 | Missing in BAC05283. Ref.4 | ||||||||
| Sequence conflict | 50 | 1 | D → E in BAC05283. Ref.4 | ||||||||
| Sequence conflict | 219 | 1 | M → T in BAC05283. Ref.4 | ||||||||
| Sequence conflict | 396 | 1 | P → A in BAC05283. Ref.4 | ||||||||
Secondary structure | |||||||||||
Helix Strand Turn | |||||||||||
| Turn | 51 – 53 | 3 | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genomic organization and chromosomal localization of the gene encoding human P-selectin glycoprotein ligand." Veldman G.M., Bean K.M., Cumming D.A., Eddy R.L., Sait S.N.J., Shows T.B. J. Biol. Chem. 270:16470-16475(1995) [PubMed: 7541799] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta. |
| [2] | "Expression cloning of a functional glycoprotein ligand for P-selectin." 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. Cell 75:1179-1186(1993) [PubMed: 7505206] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 132-GLN--ALA-141 DEL. |
| [3] | SeattleSNPs program for genomic applications Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-62 AND SER-246. |
| [4] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT 132-GLN--ALA-141 DEL. Tissue: Uterus. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT 132-GLN--ALA-141 DEL. Tissue: Brain. |
| [6] | "The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine." Moore K.L., Eaton S.F., Lyons D.E., Lichenstein H.S., Cummings R.D., McEver R.P. J. Biol. Chem. 269:23318-23327(1994) [PubMed: 7521878] [Abstract] Cited for: PROTEIN SEQUENCE OF 350-355 AND 390-396, INTERACTION WITH SELP AND SELE, CARBOHYDRATE STRUCTURE, SUBUNIT, SIALIC ACID CONTENT. Tissue: Neutrophil. |
| [7] | "A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding." Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A., Shaw G.D. Cell 83:323-331(1995) [PubMed: 7585949] [Abstract] Cited for: SULFATION, INTERACTION WITH SELP, MUTAGENESIS OF 46-TYR--ASP-52. |
| [8] | "PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus." Pouyani T., Seed B. Cell 83:333-343(1995) [PubMed: 7585950] [Abstract] Cited for: SULFATION, INTERACTION WITH SELP, MUTAGENESIS OF TYR-46; TYR-48; TYR-51 AND THR-57. |
| [9] | "Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin." Wilkins P.P., Moore K.L., McEver R.P., Cummings R.D. J. Biol. Chem. 270:22677-22680(1995) [PubMed: 7559387] [Abstract] Cited for: SULFATION, INTERACTION WITH SELP. |
| [10] | "Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells." Wilkins P.P., McEver R.P., Cummings R.D. J. Biol. Chem. 271:18732-18742(1996) [PubMed: 8702529] [Abstract] Cited for: STRUCTURE OF O-LINKED CARBOHYDRATES. |
| [11] | "Noncovalent association of P-selectin glycoprotein ligand-1 and minimal determinants for binding to P-selectin." Epperson T.K., Patel K.D., McEver R.P., Cummings R.D. J. Biol. Chem. 275:7839-7853(2000) [PubMed: 10713099] [Abstract] Cited for: INTERACTION WITH SELP, DISULFIDE BOND AT CYS-320, MUTAGENESIS OF CYS-320. |
| [12] | "Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin." Rodgers S.D., Camphausen R.T., Hammer D.A. Biophys. J. 81:2001-2009(2001) [PubMed: 11566773] [Abstract] Cited for: INTERACTION WITH SELE AND SELP, SULFATION, FUNCTION. |
| [13] | "Molecular basis of leukocyte rolling on PSGL-1. Predominant role of core-2 O-glycans and of tyrosine sulfate residue 51." Bernimoulin M.P., Zeng X.-L., Abbal C., Giraud S., Martinez M., Michielin O., Schapira M., Spertini O. J. Biol. Chem. 278:37-47(2003) [PubMed: 12403782] [Abstract] Cited for: INTERACTION WITH SELL, FUNCTION, MUTAGENESIS OF THR-44; TYR-48; TYR-51 AND THR-57. |
| [14] | "Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin." Leppaenen A., Yago T., Otto V.I., McEver R.P., Cummings R.D. J. Biol. Chem. 278:26391-26400(2003) [PubMed: 12736247] [Abstract] Cited for: INTERACTION WITH SELL, SULFATION, GYCOSYLATION. |
| [15] | "SLIC-1/sorting nexin 20: a novel sorting nexin that directs subcellular distribution of PSGL-1." Schaff U.Y., Shih H.H., Lorenz M., Sako D., Kriz R., Milarski K., Bates B., Tchernychev B., Shaw G.D., Simon S.I. Eur. J. Immunol. 38:550-564(2008) [PubMed: 18196517] [Abstract] Cited for: INTERACTION WITH SNX20. |
| [16] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND THR-393, MASS SPECTROMETRY. |
| [17] | "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." Somers W.S., Tang J., Shaw G.D., Camphausen R.T. Cell 103:467-479(2000) [PubMed: 11081633] [Abstract] Cited for: 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, PYROGLUTAMATE FORMATION AT GLN-42. |
| [18] | Erratum Somers W.S., Tang J., Shaw G.D., Camphausen R.T. Cell 105:971-971(2001) |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U25956 Genomic DNA. Translation: AAA74577.1. U02297 mRNA. Translation: AAC50061.1. AY331789 Genomic DNA. Translation: AAP81163.1. AK098315 mRNA. Translation: BAC05283.1. BC029782 mRNA. Translation: AAH29782.1. | |||||||||||||
| PIR | A57468. | ||||||||||||
| RefSeq | NP_002997.1. | ||||||||||||
| UniGene | Hs.591014 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| GlycoSuiteDB | Q14242. | ||||||||||||
| PhosphoSite | Q14242. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000110876. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 6404. | ||||||||||||
| KEGG | hsa:6404. | ||||||||||||
Organism-specific databases | |||||||||||||
| HGNC | HGNC:10722. SELPLG. | ||||||||||||
| HPA | CAB002431. | ||||||||||||
| MIM | 600738. gene. | ||||||||||||
| PharmGKB | PA35644. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
| GeneCards | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | < | ||||||||||||

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