Q62170 (SELPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: P-selectin glycoprotein ligand 1 Short name=PSGL-1 Alternative name(s): Selectin P ligand CD_antigen=CD162 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 397 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- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. PSGL1 is critical for the initial leukocyte capture. Ref.3 Ref.4 Ref.6 |
| Subunit structure | Homodimer; disulfide-linked. Interacts with P- and E-selectins, through their lectin/EGF domains. Interaction with P-selectin requires sialyl Lewis X glycan modification and tyrosine sulfation, probably on Tyr-54, for high affinity binding By similarity. Dimerization appears not to be required for P-selectin/SELP binding By similarity. Interacts with SNX20 By similarity. Interacts with MSN and SYK; mediates SYK activation downstream of SELPLG By similarity. Ref.1 Ref.3 Ref.5 |
| Subcellular location | Cell membrane; Single-pass membrane protein Potential. |
| Tissue specificity | Highly expressed in blood, bone marrow, brain, adipose tissue, spleen, and thymus. Also expressed in heart, kidney, liver, muscle, ovary, and stomach. Ref.1 |
| 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. No sulfated O-glycans. Some N-glycosylation By similarity. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Cell membrane Membrane |
| Domain | Repeat Signal Transmembrane Transmembrane helix |
| Ligand | Sialic acid |
| PTM | Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid Sulfation |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular response to interleukin-6 Inferred from electronic annotation. Source: Compara leukocyte adhesive activationInferred from mutant phenotype PubMed 17632516. Source: UniProtKB leukocyte tethering or rollingInferred from mutant phenotype PubMed 15956287. Source: MGI |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 | By similarity | PRO_0000022304 | |||||||
| Chain | 42 – 397 | 356 | P-selectin glycoprotein ligand 1 | PRO_0000022305 | |||||||
Regions | |||||||||||
| Topological domain | 18 – 307 | 290 | Extracellular Potential | ||||||||
| Transmembrane | 308 – 328 | 21 | Helical; Potential | ||||||||
| Topological domain | 329 – 397 | 69 | Cytoplasmic Potential | ||||||||
| Repeat | 126 – 135 | 10 | 1 | ||||||||
| Repeat | 136 – 145 | 10 | 2 | ||||||||
| Repeat | 146 – 155 | 10 | 3 | ||||||||
| Repeat | 156 – 165 | 10 | 4 | ||||||||
| Repeat | 166 – 175 | 10 | 5 | ||||||||
| Repeat | 176 – 185 | 10 | 6 | ||||||||
| Repeat | 186 – 195 | 10 | 7 | ||||||||
| Repeat | 196 – 205 | 10 | 8 | ||||||||
| Repeat | 206 – 215 | 10 | 9 | ||||||||
| Repeat | 216 – 225 | 10 | 10 | ||||||||
| Region | 126 – 225 | 100 | 10 X 10 AA tandem repeats | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 42 | 1 | Pyrrolidone carboxylic acid By similarity | ||||||||
| Modified residue | 54 | 1 | Sulfotyrosine Probable | ||||||||
| Modified residue | 56 | 1 | Sulfotyrosine Potential | ||||||||
| Glycosylation | 58 | 1 | O-linked (GalNAc...) Probable | ||||||||
| Glycosylation | 66 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 261 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 307 | Interchain By similarity | |||||||||
Experimental info | |||||||||||
| Mutagenesis | 54 | 1 | Y → F: Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction of P-selectin binding; when associated with Y-56. Binding of P-selectin completely abolished; when associated with A-55; Y-56 and A-58. Ref.5 | ||||||||
| Mutagenesis | 55 | 1 | T → A: No effect on P-selectin binding. Greatly reduced P-selectin binding and tethering and rolling of cells; when associated with A-58. Binding of P-selectin completely abolished; when associated with Y-54; Y-56 and A-58. Ref.5 | ||||||||
| Mutagenesis | 56 | 1 | Y → F: No effect on P-selectin binding. Greatly decreased P-selectin binding and tethering and rolling of cells; when associated with Y-54. Binding of P-selectin completely abolished; when associated with Y-54; A-55 and A-58. Ref.5 | ||||||||
| Mutagenesis | 58 | 1 | T → A: Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction in P-selectin binding when associated with A-55. Binding of P-selectin completely abolished; when associated with Y-54; A-55; and Y-56. Ref.5 | ||||||||
| Mutagenesis | 66 | 1 | N → T: No effect on P-selectin binding; when associated with A-261. | ||||||||
| Mutagenesis | 261 | 1 | N → A: No effect on P-selectin binding; when associated with T-66. | ||||||||
| Sequence conflict | 173 | 1 | E → D in CAA62583. Ref.1 | ||||||||
| Sequence conflict | 176 | 1 | Q → K in CAA62583. Ref.1 | ||||||||
| Sequence conflict | 180 | 1 | M → T in CAA62583. Ref.1 | ||||||||
| Sequence conflict | 183 | 1 | D → E in CAA62583. Ref.1 | ||||||||
| Sequence conflict | 186 | 1 | Q → K in CAA62583. Ref.1 | ||||||||
| Sequence conflict | 190 | 1 | M → T in CAA62583. Ref.1 | ||||||||
Secondary structure | |||||||||||
Helix Strand Turn | |||||||||||
| Beta strand | 337 – 342 | 6 | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Mouse P-selectin glycoprotein ligand-1: molecular cloning, chromosomal localization, and expression of a functional P-selectin receptor." Yang J., Galipeau J., Kozak C., Furie B.C., Furie B. Blood 87:4176-4186(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH SELE AND SELP, TISSUE SPECIFICITY. Strain: BALB/c. |
| [2] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [3] | "P-Selectin glycoprotein ligand 1 (PSGL-1) is a physiological ligand for E-selectin in mediating T helper 1 lymphocyte migration." Hirata T., Merrill-Skoloff G., Aab M., Yang J., Furie B.C., Furie B. J. Exp. Med. 192:1669-1676(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SELE AND SELP, FUNCTION. |
| [4] | "P-, E-, and L-selectin mediate migration of activated CD8+ T lymphocytes into inflamed skin." Hirata T., Furie B.C., Furie B. J. Immunol. 169:4307-4313(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [5] | "N-terminal residues in murine P-selectin glycoprotein ligand-1 required for binding to murine P-selectin." Xia L., Ramachandran V., McDaniel J.M., Nguyen K.N., Cummings R.D., McEver R.P. Blood 101:552-559(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SELP, SULFATION, MUTAGENESIS OF TYR-54; THR-55; TYR-56 AND THR-58. |
| [6] | "Complete identification of E-selectin ligands on neutrophils reveals distinct functions of PSGL-1, ESL-1, and CD44." Hidalgo A., Peired A.J., Wild M.K., Vestweber D., Frenette P.S. Immunity 26:477-489(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X91144 mRNA. Translation: CAA62583.1. AC159240 Genomic DNA. No translation available. | ||||||||||||
| IPI | IPI00311080. | ||||||||||||
| UniGene | Mm.332590. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-59330N. | ||||||||||||
| STRING | 10090.ENSMUSP00000098436. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q62170. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q62170. | ||||||||||||
| PRIDE | Q62170. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Organism-specific databases | |||||||||||||
| MGI | MGI:106689. Selplg. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG300903. | ||||||||||||
| HOGENOM | HOG000013048. | ||||||||||||
| HOVERGEN | HBG061628. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q62170. | ||||||||||||
| Bgee | Q62170. | ||||||||||||
| CleanEx | MM_SELPLG. | ||||||||||||
| Genevestigator | Q62170. | ||||||||||||
| GermOnline | ENSMUSG00000048163. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR026195. PSGL-1. [Graphical view] | ||||||||||||
| PANTHER | PTHR17384. PTHR17384. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q62170. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | SELPL_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q62170 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |

Clusters with
