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Protein

P-selectin glycoprotein ligand 1

Gene

Selplg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

  • leukocyte adhesive activation Source: UniProtKB
  • leukocyte tethering or rolling Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Sialic acid

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
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:106689. Selplg.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini18 – 307ExtracellularSequence analysisAdd BLAST290
Transmembranei308 – 328HelicalSequence analysisAdd BLAST21
Topological domaini329 – 397CytoplasmicSequence analysisAdd BLAST69

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54Y → 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 Publication1
Mutagenesisi55T → 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 Publication1
Mutagenesisi56Y → 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 Publication1
Mutagenesisi58T → 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 Publication1
Mutagenesisi66N → T: No effect on P-selectin binding; when associated with A-261. 1
Mutagenesisi261N → A: No effect on P-selectin binding; when associated with T-66. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002230418 – 41By similarityAdd BLAST24
ChainiPRO_000002230542 – 397P-selectin glycoprotein ligand 1Add BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42Pyrrolidone carboxylic acidBy similarity1
Modified residuei54Sulfotyrosine1 Publication1
Modified residuei56SulfotyrosineSequence analysis1
Glycosylationi58O-linked (GalNAc...)Curated1
Glycosylationi66N-linked (GlcNAc...)Sequence analysis1
Glycosylationi261N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi307InterchainBy similarity
Modified residuei391PhosphothreonineBy similarity1
Modified residuei394PhosphoserineBy similarity1

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, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

EPDiQ62170.
PaxDbiQ62170.
PRIDEiQ62170.

PTM databases

iPTMnetiQ62170.
PhosphoSitePlusiQ62170.
SwissPalmiQ62170.

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

BgeeiENSMUSG00000048163.
CleanExiMM_SELPLG.

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

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi337 – 342Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EMTX-ray2.80C/D/E331-348[»]
ProteinModelPortaliQ62170.
SMRiQ62170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62170.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati126 – 135110
Repeati136 – 145210
Repeati146 – 155310
Repeati156 – 165410
Repeati166 – 175510
Repeati176 – 185610
Repeati186 – 195710
Repeati196 – 205810
Repeati206 – 215910
Repeati216 – 2251010

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 22510 X 10 AA tandem repeatsAdd BLAST100

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410JASD. Eukaryota.
ENOG410Y5S5. LUCA.
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)DescriptionActionsGraphical viewLength
Sequence conflicti173E → D in CAA62583 (PubMed:8639776).Curated1
Sequence conflicti176Q → K in CAA62583 (PubMed:8639776).Curated1
Sequence conflicti180M → T in CAA62583 (PubMed:8639776).Curated1
Sequence conflicti183D → E in CAA62583 (PubMed:8639776).Curated1
Sequence conflicti186Q → K in CAA62583 (PubMed:8639776).Curated1
Sequence conflicti190M → T in CAA62583 (PubMed:8639776).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91144 mRNA. Translation: CAA62583.1.
AC159240 Genomic DNA. No translation available.
UniGeneiMm.332590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91144 mRNA. Translation: CAA62583.1.
AC159240 Genomic DNA. No translation available.
UniGeneiMm.332590.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EMTX-ray2.80C/D/E331-348[»]
ProteinModelPortaliQ62170.
SMRiQ62170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59330N.
STRINGi10090.ENSMUSP00000098436.

PTM databases

iPTMnetiQ62170.
PhosphoSitePlusiQ62170.
SwissPalmiQ62170.

Proteomic databases

EPDiQ62170.
PaxDbiQ62170.
PRIDEiQ62170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:106689. Selplg.

Phylogenomic databases

eggNOGiENOG410JASD. Eukaryota.
ENOG410Y5S5. LUCA.
HOGENOMiHOG000013048.
HOVERGENiHBG061628.
InParanoidiQ62170.

Miscellaneous databases

EvolutionaryTraceiQ62170.
PROiQ62170.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000048163.
CleanExiMM_SELPLG.

Family and domain databases

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

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: November 2, 2016
This is version 121 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.