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Protein

P-selectin glycoprotein ligand 1

Gene

SELPLG

Organism
Homo sapiens (Human)
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-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.2 Publications
(Microbial infection) Acts as a receptor for enterovirus 71.1 Publication

GO - Molecular functioni

  • receptor binding Source: ProtInc
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • cell adhesion Source: ProtInc
  • cellular response to interleukin-6 Source: MGI
  • leukocyte adhesive activation Source: UniProtKB
  • leukocyte migration Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110876-MONOMER.
ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
SIGNORiQ14242.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10722. SELPLG.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini18 – 320ExtracellularSequence analysisAdd BLAST303
Transmembranei321 – 341HelicalSequence analysisAdd BLAST21
Topological domaini342 – 412CytoplasmicSequence analysisAdd BLAST71

GO - Cellular componenti

  • integral component of membrane Source: ProtInc
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: ProtInc
  • plasma membrane Source: UniProtKB
  • uropod Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44T → A: No effect on L-selectin binding nor neutrophil rolling. 1 Publication1
Mutagenesisi46 – 52YEYLDYD → FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. 1 Publication7
Mutagenesisi46 – 51YEYLDY → FEFLDF: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. 6
Mutagenesisi46Y → 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. 1 Publication1
Mutagenesisi48Y → 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. 2 Publications1
Mutagenesisi51Y → 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. 2 Publications1
Mutagenesisi57T → A: No E- nor P-selectin binding, and very little neutrophil rolling. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and F-51. 2 Publications1
Mutagenesisi320C → A or S: No dimer formation. No effect on P-selectin binding. 1 Publication1

Organism-specific databases

DisGeNETi6404.
OpenTargetsiENSG00000110876.
PharmGKBiPA35644.

Chemistry databases

ChEMBLiCHEMBL4183.

Polymorphism and mutation databases

BioMutaiSELPLG.
DMDMi2498904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002230218 – 41Add BLAST24
ChainiPRO_000002230342 – 412P-selectin glycoprotein ligand 1Add BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42Pyrrolidone carboxylic acid1 Publication1
Modified residuei46Sulfotyrosine1 Publication1
Modified residuei48Sulfotyrosine1 Publication1
Modified residuei51Sulfotyrosine1 Publication1
Glycosylationi57O-linked (GalNAc...)1 Publication1
Glycosylationi65N-linked (GlcNAc...)Sequence analysis1
Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
Glycosylationi302N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi320Interchain1 Publication
Modified residuei406PhosphothreonineCombined sources1
Modified residuei409PhosphoserineCombined sources1

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 in leukocyte rolling. The modification containing the sialyl Lewis X glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation.2 Publications
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.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiQ14242.
MaxQBiQ14242.
PaxDbiQ14242.
PeptideAtlasiQ14242.
PRIDEiQ14242.

PTM databases

iPTMnetiQ14242.
PhosphoSitePlusiQ14242.
UniCarbKBiQ14242.

Miscellaneous databases

PMAP-CutDBA8K2Y0.

Expressioni

Tissue specificityi

Expressed on neutrophils, monocytes and most lymphocytes.

Gene expression databases

BgeeiENSG00000110876.
CleanExiHS_SELPLG.
ExpressionAtlasiQ14242. baseline and differential.
GenevisibleiQ14242. HS.

Organism-specific databases

HPAiCAB002431.

Interactioni

Subunit structurei

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. Interacts with MSN and SYK; mediates the activation of SYK by SELPLG.11 Publications
(Microbial infection) Interacts with enterovirus 71 capsid proteins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SELPP161093EBI-1030190,EBI-1030170
SNX20Q7Z6145EBI-1030190,EBI-744896

GO - Molecular functioni

  • receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi112304. 6 interactors.
DIPiDIP-37668N.
IntActiQ14242. 7 interactors.
STRINGi9606.ENSP00000228463.

Chemistry databases

BindingDBiQ14242.

Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni51 – 53Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1SX-ray1.90C/D42-60[»]
ProteinModelPortaliQ14242.
SMRiQ14242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14242.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati122 – 131110
Repeati132 – 141210
Repeati142 – 151310
Repeati162 – 171410
Repeati182 – 191510
Repeati192 – 201610
Repeati202 – 211710
Repeati212 – 221810
Repeati222 – 231910
Repeati232 – 2411010
Repeati242 – 2511110
Repeati252 – 2611210

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni122 – 26112 X 10 AA tandem repeatsAdd BLAST140

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410JASD. Eukaryota.
ENOG410Y5S5. LUCA.
GeneTreeiENSGT00440000039754.
HOGENOMiHOG000013048.
HOVERGENiHBG061628.
InParanoidiQ14242.
KOiK06544.
OMAiNYSPTEM.
OrthoDBiEOG091G0BCI.
PhylomeDBiQ14242.
TreeFamiTF337792.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14242-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPLQLLLLLI LLGPGNSLQL WDTWADEAEK ALGPLLARDR RQATEYEYLD
60 70 80 90 100
YDFLPETEPP EMLRNSTDTT PLTGPGTPES TTVEPAARRS TGLDAGGAVT
110 120 130 140 150
ELTTELANMG NLSTDSAAME IQTTQPAATE AQTTQPVPTE AQTTPLAATE
160 170 180 190 200
AQTTRLTATE AQTTPLAATE AQTTPPAATE AQTTQPTGLE AQTTAPAAME
210 220 230 240 250
AQTTAPAAME AQTTPPAAME AQTTQTTAME AQTTAPEATE AQTTQPTATE
260 270 280 290 300
AQTTPLAAME ALSTEPSATE ALSMEPTTKR GLFIPFSVSS VTHKGIPMAA
310 320 330 340 350
SNLSVNYPVG APDHISVKQC LLAILILALV ATIFFVCTVV LAVRLSRKGH
360 370 380 390 400
MYPVRNYSPT EMVCISSLLP DGGEGPSATA NGGLSKAKSP GLTPEPREDR
410
EGDDLTLHSF LP
Length:412
Mass (Da):43,201
Last modified:November 1, 1996 - v1
Checksum:iA92A2A902DC9963A
GO
Isoform 2 (identifier: Q14242-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAVGASGLEGDKMAGAM

Note: No experimental confirmation available.
Show »
Length:428
Mass (Da):44,648
Checksum:iFDB7B0A35F5C4CCC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23 – 39Missing in BAC05283 (PubMed:14702039).CuratedAdd BLAST17
Sequence conflicti50D → E in BAC05283 (PubMed:14702039).Curated1
Sequence conflicti219M → T in BAC05283 (PubMed:14702039).Curated1
Sequence conflicti222Q → R in BAH12863 (PubMed:14702039).Curated1
Sequence conflicti396P → A in BAC05283 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01915662M → I.2 PublicationsCorresponds to variant rs2228315dbSNPEnsembl.1
Natural variantiVAR_005611132 – 141Missing in short form; not an alternative splicing. 3 PublicationsCorresponds to variant rs63748999dbSNPEnsembl.10
Natural variantiVAR_019157246P → S.1 PublicationCorresponds to variant rs8179142dbSNPEnsembl.1
Natural variantiVAR_076761249T → M.1 PublicationCorresponds to variant rs756234416dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0448271M → MAVGASGLEGDKMAGAM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25956 Genomic DNA. Translation: AAA74577.1.
U02297 mRNA. Translation: AAC50061.1.
AK098315 mRNA. Translation: BAC05283.1.
AK290395 mRNA. Translation: BAF83084.1.
AK298738 mRNA. Translation: BAG60885.1.
AK298742 mRNA. Translation: BAH12863.1.
AY331789 Genomic DNA. Translation: AAP81163.1.
AC007569 Genomic DNA. No translation available.
AC008119 Genomic DNA. No translation available.
BC029782 mRNA. Translation: AAH29782.1.
CCDSiCCDS31895.2. [Q14242-1]
CCDS55881.1. [Q14242-2]
PIRiA57468.
RefSeqiNP_001193538.1. NM_001206609.1. [Q14242-2]
NP_002997.2. NM_003006.4. [Q14242-1]
UniGeneiHs.591014.

Genome annotation databases

EnsembliENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2]
ENST00000550948; ENSP00000447752; ENSG00000110876. [Q14242-1]
GeneIDi6404.
KEGGihsa:6404.
UCSCiuc001tni.4. human. [Q14242-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

P-selectin glycoprotein ligand 1 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25956 Genomic DNA. Translation: AAA74577.1.
U02297 mRNA. Translation: AAC50061.1.
AK098315 mRNA. Translation: BAC05283.1.
AK290395 mRNA. Translation: BAF83084.1.
AK298738 mRNA. Translation: BAG60885.1.
AK298742 mRNA. Translation: BAH12863.1.
AY331789 Genomic DNA. Translation: AAP81163.1.
AC007569 Genomic DNA. No translation available.
AC008119 Genomic DNA. No translation available.
BC029782 mRNA. Translation: AAH29782.1.
CCDSiCCDS31895.2. [Q14242-1]
CCDS55881.1. [Q14242-2]
PIRiA57468.
RefSeqiNP_001193538.1. NM_001206609.1. [Q14242-2]
NP_002997.2. NM_003006.4. [Q14242-1]
UniGeneiHs.591014.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1SX-ray1.90C/D42-60[»]
ProteinModelPortaliQ14242.
SMRiQ14242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112304. 6 interactors.
DIPiDIP-37668N.
IntActiQ14242. 7 interactors.
STRINGi9606.ENSP00000228463.

Chemistry databases

BindingDBiQ14242.
ChEMBLiCHEMBL4183.

PTM databases

iPTMnetiQ14242.
PhosphoSitePlusiQ14242.
UniCarbKBiQ14242.

Polymorphism and mutation databases

BioMutaiSELPLG.
DMDMi2498904.

Proteomic databases

EPDiQ14242.
MaxQBiQ14242.
PaxDbiQ14242.
PeptideAtlasiQ14242.
PRIDEiQ14242.

Protocols and materials databases

DNASUi6404.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2]
ENST00000550948; ENSP00000447752; ENSG00000110876. [Q14242-1]
GeneIDi6404.
KEGGihsa:6404.
UCSCiuc001tni.4. human. [Q14242-1]

Organism-specific databases

CTDi6404.
DisGeNETi6404.
GeneCardsiSELPLG.
H-InvDBHIX0010969.
HGNCiHGNC:10722. SELPLG.
HPAiCAB002431.
MIMi600738. gene.
neXtProtiNX_Q14242.
OpenTargetsiENSG00000110876.
PharmGKBiPA35644.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JASD. Eukaryota.
ENOG410Y5S5. LUCA.
GeneTreeiENSGT00440000039754.
HOGENOMiHOG000013048.
HOVERGENiHBG061628.
InParanoidiQ14242.
KOiK06544.
OMAiNYSPTEM.
OrthoDBiEOG091G0BCI.
PhylomeDBiQ14242.
TreeFamiTF337792.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110876-MONOMER.
ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
SIGNORiQ14242.

Miscellaneous databases

ChiTaRSiSELPLG. human.
EvolutionaryTraceiQ14242.
GeneWikiiP-selectin_glycoprotein_ligand-1.
GenomeRNAii6404.
PMAP-CutDBA8K2Y0.
PROiQ14242.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110876.
CleanExiHS_SELPLG.
ExpressionAtlasiQ14242. baseline and differential.
GenevisibleiQ14242. HS.

Family and domain databases

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

Entry informationi

Entry nameiSELPL_HUMAN
AccessioniPrimary (citable) accession number: Q14242
Secondary accession number(s): A8K2Y0
, B4DQC3, B7Z5C7, J3KMX6, Q12775, Q6GTW7, Q8N7J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. 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.