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Q62170

- SELPL_MOUSE

UniProt

Q62170 - SELPL_MOUSE

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Protein

P-selectin glycoprotein ligand 1

Gene

Selplg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Biological processi

  1. cellular response to interleukin-6 Source: Ensembl
  2. leukocyte adhesive activation Source: UniProtKB
  3. leukocyte tethering or rolling Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiREACT_225233. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
P-selectin glycoprotein ligand 1
Short name:
PSGL-1
Alternative name(s):
Selectin P ligand
CD_antigen: CD162
Gene namesi
Name:Selplg
Synonyms:Selp1, Selpl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:106689. Selplg.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541Y → 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. 1 Publication
Mutagenesisi55 – 551T → 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. 1 Publication
Mutagenesisi56 – 561Y → 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. 1 Publication
Mutagenesisi58 – 581T → 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. 1 Publication
Mutagenesisi66 – 661N → T: No effect on P-selectin binding; when associated with A-261.
Mutagenesisi261 – 2611N → A: No effect on P-selectin binding; when associated with T-66.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 4124By similarityPRO_0000022304Add
BLAST
Chaini42 – 397356P-selectin glycoprotein ligand 1PRO_0000022305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Pyrrolidone carboxylic acidBy similarity
Modified residuei54 – 541Sulfotyrosine1 Publication
Modified residuei56 – 561SulfotyrosineSequence Analysis
Glycosylationi58 – 581O-linked (GalNAc...)Curated
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi307 – 307InterchainBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiQ62170.
PRIDEiQ62170.

PTM databases

PhosphoSiteiQ62170.

Expressioni

Tissue specificityi

Highly expressed in blood, bone marrow, brain, adipose tissue, spleen, and thymus. Also expressed in heart, kidney, liver, muscle, ovary, and stomach.1 Publication

Gene expression databases

BgeeiQ62170.
CleanExiMM_SELPLG.
ExpressionAtlasiQ62170. baseline and differential.
GenevestigatoriQ62170.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

DIPiDIP-59330N.
STRINGi10090.ENSMUSP00000098436.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi337 – 3426

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EMTX-ray2.80C/D/E331-348[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62170.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 307290ExtracellularSequence AnalysisAdd
BLAST
Topological domaini329 – 39769CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei308 – 32821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati126 – 135101
Repeati136 – 145102
Repeati146 – 155103
Repeati156 – 165104
Repeati166 – 175105
Repeati176 – 185106
Repeati186 – 195107
Repeati196 – 205108
Repeati206 – 215109
Repeati216 – 2251010

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 22510010 X 10 AA tandem repeatsAdd
BLAST

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300903.
HOGENOMiHOG000013048.
HOVERGENiHBG061628.
InParanoidiQ62170.

Family and domain databases

InterProiIPR026195. PSGL-1.
[Graphical view]
PANTHERiPTHR17384. PTHR17384. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62170-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPSFLVLLT ILGPGNSLQL QDPWGHETKE APGPVHLRER RQVVGDDDFE
60 70 80 90 100
DPDYTYNTDP PELLKNVTNT VAAHPELPTT VVMLERDSTS AGTSERATEK
110 120 130 140 150
IATTDPTAPG TGGTAVGMLS TDSATQWSLT SVETVQPAST EVETSQPAPM
160 170 180 190 200
EAETSQPAPM EAETSQPAPM EAETSQPAPM EADTSQPAPM EAETSQPAPN
210 220 230 240 250
EAETSKPAPT EAETSKPAPT EAETTQLPRI QAVKTLFTTS AATEVPSTEP
260 270 280 290 300
TTMETASTES NESTIFLGPS VTHLPDSGLK KGLIVTPGNS PAPTLPGSSD
310 320 330 340 350
LIPVKQCLLI ILILASLATI FLVCTVVLAV RLSRKTHMYP VRNYSPTEMI
360 370 380 390
CISSLLPEGG DGAPVTANGG LPKVQDLKTE PSGDRDGDDL TLHSFLP
Length:397
Mass (Da):41,842
Last modified:July 27, 2011 - v2
Checksum:iD5EB53D493AE26EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731E → D in CAA62583. (PubMed:8639776)Curated
Sequence conflicti176 – 1761Q → K in CAA62583. (PubMed:8639776)Curated
Sequence conflicti180 – 1801M → T in CAA62583. (PubMed:8639776)Curated
Sequence conflicti183 – 1831D → E in CAA62583. (PubMed:8639776)Curated
Sequence conflicti186 – 1861Q → K in CAA62583. (PubMed:8639776)Curated
Sequence conflicti190 – 1901M → T in CAA62583. (PubMed:8639776)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91144 mRNA. Translation: CAA62583.1.
AC159240 Genomic DNA. No translation available.
UniGeneiMm.332590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91144 mRNA. Translation: CAA62583.1 .
AC159240 Genomic DNA. No translation available.
UniGenei Mm.332590.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EMT X-ray 2.80 C/D/E 331-348 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59330N.
STRINGi 10090.ENSMUSP00000098436.

PTM databases

PhosphoSitei Q62170.

Proteomic databases

PaxDbi Q62170.
PRIDEi Q62170.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:106689. Selplg.

Phylogenomic databases

eggNOGi NOG300903.
HOGENOMi HOG000013048.
HOVERGENi HBG061628.
InParanoidi Q62170.

Enzyme and pathway databases

Reactomei REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

EvolutionaryTracei Q62170.
PROi Q62170.
SOURCEi Search...

Gene expression databases

Bgeei Q62170.
CleanExi MM_SELPLG.
ExpressionAtlasi Q62170. baseline and differential.
Genevestigatori Q62170.

Family and domain databases

InterProi IPR026195. PSGL-1.
[Graphical view ]
PANTHERi PTHR17384. PTHR17384. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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].

Entry informationi

Entry nameiSELPL_MOUSE
AccessioniPrimary (citable) accession number: Q62170
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3