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Q62170 (SELPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-selectin glycoprotein ligand 1

Short name=PSGL-1
Alternative name(s):
Selectin P ligand
CD_antigen=CD162
Gene names
Name:Selplg
Synonyms:Selp1, Selpl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A SLe(x)-type proteoglycan, 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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 4124 By similarity
PRO_0000022304
Chain42 – 397356P-selectin glycoprotein ligand 1
PRO_0000022305

Regions

Topological domain18 – 307290Extracellular Potential
Transmembrane308 – 32821Helical; Potential
Topological domain329 – 39769Cytoplasmic Potential
Repeat126 – 135101
Repeat136 – 145102
Repeat146 – 155103
Repeat156 – 165104
Repeat166 – 175105
Repeat176 – 185106
Repeat186 – 195107
Repeat196 – 205108
Repeat206 – 215109
Repeat216 – 2251010
Region126 – 22510010 X 10 AA tandem repeats

Amino acid modifications

Modified residue421Pyrrolidone carboxylic acid By similarity
Modified residue541Sulfotyrosine Probable
Modified residue561Sulfotyrosine Potential
Glycosylation581O-linked (GalNAc...) Probable
Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Disulfide bond307Interchain By similarity

Experimental info

Mutagenesis541Y → 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
Mutagenesis551T → 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
Mutagenesis561Y → 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
Mutagenesis581T → 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
Mutagenesis661N → T: No effect on P-selectin binding; when associated with A-261.
Mutagenesis2611N → A: No effect on P-selectin binding; when associated with T-66.
Sequence conflict1731E → D in CAA62583. Ref.1
Sequence conflict1761Q → K in CAA62583. Ref.1
Sequence conflict1801M → T in CAA62583. Ref.1
Sequence conflict1831D → E in CAA62583. Ref.1
Sequence conflict1861Q → K in CAA62583. Ref.1
Sequence conflict1901M → T in CAA62583. Ref.1

Secondary structure

... 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62170 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: D5EB53D493AE26EE

FASTA39741,842
        10         20         30         40         50         60 
MSPSFLVLLT ILGPGNSLQL QDPWGHETKE APGPVHLRER RQVVGDDDFE DPDYTYNTDP 

        70         80         90        100        110        120 
PELLKNVTNT VAAHPELPTT VVMLERDSTS AGTSERATEK IATTDPTAPG TGGTAVGMLS 

       130        140        150        160        170        180 
TDSATQWSLT SVETVQPAST EVETSQPAPM EAETSQPAPM EAETSQPAPM EAETSQPAPM 

       190        200        210        220        230        240 
EADTSQPAPM EAETSQPAPN EAETSKPAPT EAETSKPAPT EAETTQLPRI QAVKTLFTTS 

       250        260        270        280        290        300 
AATEVPSTEP TTMETASTES NESTIFLGPS VTHLPDSGLK KGLIVTPGNS PAPTLPGSSD 

       310        320        330        340        350        360 
LIPVKQCLLI ILILASLATI FLVCTVVLAV RLSRKTHMYP VRNYSPTEMI CISSLLPEGG 

       370        380        390 
DGAPVTANGG LPKVQDLKTE PSGDRDGDDL TLHSFLP 

« Hide

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. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., 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.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91144 mRNA. Translation: CAA62583.1.
AC159240 Genomic DNA. No translation available.
UniGeneMm.332590.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EMTX-ray2.80C/D/E331-348[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59330N.
STRING10090.ENSMUSP00000098436.

PTM databases

PhosphoSiteQ62170.

Proteomic databases

PaxDbQ62170.
PRIDEQ62170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:106689. Selplg.

Phylogenomic databases

eggNOGNOG300903.
HOGENOMHOG000013048.
HOVERGENHBG061628.

Gene expression databases

ArrayExpressQ62170.
BgeeQ62170.
CleanExMM_SELPLG.
GenevestigatorQ62170.

Family and domain databases

InterProIPR026195. PSGL-1.
[Graphical view]
PANTHERPTHR17384. PTHR17384. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ62170.
PROQ62170.
SOURCESearch...

Entry information

Entry nameSELPL_MOUSE
AccessionPrimary (citable) accession number: Q62170
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: February 19, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot