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Q01102 (LYAM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-selectin
Alternative name(s):
CD62 antigen-like family member P
Granule membrane protein 140
Short name=GMP-140
Leukocyte-endothelial cell adhesion molecule 3
Short name=LECAM3
Platelet activation dependent granule-external membrane protein
Short name=PADGEM
CD_antigen=CD62P
Gene names
Name:Selp
Synonyms:Grmp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length768 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ca2+-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. Ref.4

Subunit structure

Interacts with SNX17. Interacts with PSGL1/SEPL and PODXL2 and mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of PSGL1 and PODXL2, and specific tyrosine sulfation on PSGL1 By similarity. Ref.5

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface.

Induction

By TNF-alpha. Induced expression in lung, liver, kidney and heart after endotoxin treatment. Ref.1 Ref.2

Sequence similarities

Belongs to the selectin/LECAM family.

Contains 1 C-type lectin domain.

Contains 1 EGF-like domain.

Contains 8 Sushi (CCP/SCR) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   DomainEGF-like domain
Repeat
Signal
Sushi
Transmembrane
Transmembrane helix
   LigandLectin
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to interleukin-6

Inferred from sequence orthology PubMed 9486531. Source: MGI

heterophilic cell-cell adhesion

Inferred from mutant phenotype PubMed 8557754PubMed 8562500. Source: MGI

inflammatory response

Inferred from mutant phenotype PubMed 7688665. Source: MGI

leukocyte cell-cell adhesion

Inferred from mutant phenotype PubMed 8557754PubMed 8562500. Source: MGI

leukocyte migration

Inferred from mutant phenotype PubMed 15484189. Source: MGI

leukocyte tethering or rolling

Inferred from mutant phenotype PubMed 15956287. Source: MGI

positive regulation of leukocyte migration

Inferred from mutant phenotype PubMed 17114491. Source: MGI

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of platelet activation

Inferred from mutant phenotype PubMed 16514062. Source: BHF-UCL

regulation of integrin activation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentexternal side of plasma membrane

Inferred from direct assay PubMed 17114491PubMed 19349303PubMed 23583643PubMed 8562500. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 15956287PubMed 7688665. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

platelet alpha granule membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium-dependent protein binding

Inferred from direct assay PubMed 7524641. Source: MGI

fucose binding

Inferred from electronic annotation. Source: Ensembl

glycoprotein binding

Inferred from direct assay PubMed 8562500. Source: MGI

heparin binding

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide binding

Inferred from electronic annotation. Source: Ensembl

oligosaccharide binding

Inferred from electronic annotation. Source: Ensembl

sialic acid binding

Inferred from direct assay PubMed 8562500. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 768727P-selectin
PRO_0000017499

Regions

Topological domain42 – 709668Extracellular Potential
Transmembrane710 – 73324Helical; Potential
Topological domain734 – 76835Cytoplasmic Potential
Domain58 – 158101C-type lectin
Domain159 – 19537EGF-like
Domain198 – 25962Sushi 1
Domain260 – 32162Sushi 2
Domain322 – 38362Sushi 3
Domain384 – 44562Sushi 4
Domain446 – 50762Sushi 5
Domain508 – 56962Sushi 6
Domain578 – 63962Sushi 7
Domain640 – 70162Sushi 8
Region759 – 76810Interaction with SNX17 By similarity
Motif756 – 7594Endocytosis signal Probable

Amino acid modifications

Lipidation7451S-palmitoyl cysteine By similarity
Glycosylation3981N-linked (GlcNAc...) Potential
Glycosylation6031N-linked (GlcNAc...) Potential
Glycosylation6541N-linked (GlcNAc...) Potential
Glycosylation6611N-linked (GlcNAc...) Potential
Glycosylation6791N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 158 By similarity
Disulfide bond131 ↔ 150 By similarity
Disulfide bond163 ↔ 174 By similarity
Disulfide bond168 ↔ 183 By similarity
Disulfide bond185 ↔ 194 By similarity
Disulfide bond200 ↔ 244 By similarity
Disulfide bond230 ↔ 257 By similarity
Disulfide bond262 ↔ 306 By similarity
Disulfide bond292 ↔ 319 By similarity
Disulfide bond324 ↔ 368 By similarity
Disulfide bond354 ↔ 381 By similarity
Disulfide bond386 ↔ 430 By similarity
Disulfide bond416 ↔ 443 By similarity
Disulfide bond448 ↔ 492 By similarity
Disulfide bond478 ↔ 505 By similarity
Disulfide bond510 ↔ 554 By similarity
Disulfide bond540 ↔ 567 By similarity
Disulfide bond580 ↔ 624 By similarity
Disulfide bond610 ↔ 637 By similarity
Disulfide bond642 ↔ 686 By similarity
Disulfide bond672 ↔ 699 By similarity

Experimental info

Sequence conflict7241A → E in AAA37712. Ref.2

Secondary structure

... 768
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01102 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: E5173074D2F66E68

FASTA76883,099
        10         20         30         40         50         60 
MAGCPKGSWT PRLRSVILGG AQLIWFSALI SELVNQKEVA AWTYNYSTKA YSWNNSRVFC 

        70         80         90        100        110        120 
RRHFTDLVAI QNKNEIAHLN DVIPFFNSYY WIGIRKINNK WTWVGTNKTL TEEAENWADN 

       130        140        150        160        170        180 
EPNNKKNNQD CVEIYIKSNS APGKWNDEPC FKRKRALCYT ASCQDMSCSN QGECIETIGS 

       190        200        210        220        230        240 
YTCSCYPGFY GPECEYVKEC GKVNIPQHVL MNCSHPLGEF SFNSQCTFSC AEGYELDGPG 

       250        260        270        280        290        300 
ELQCLASGIW TNNPPKCDAV QCQSLEAPPH GTMACMHPIA AFAYDSSCKF ECQPGYRARG 

       310        320        330        340        350        360 
SNTLHCTGSG QWSEPLPTCE AIACEPPEIP IHGSMDCVPS TGTFGYNSSC TFLCAEGFVL 

       370        380        390        400        410        420 
KGNDAIQCAD SGQWTAPAPF CEALQCPEFP VPSKAQVNCS DPFGTLTYQS VCSFSCDEGS 

       430        440        450        460        470        480 
LLVGASVIRC LATGHWNGAP PECQAVSCAP MLSPENGSMT CVQPLGNSTY KSTCQFMCDE 

       490        500        510        520        530        540 
GFYLSGPERL DCSPSGHWTG TPPTCEAIKC PGIFAPEQGN LDCSHVHGEF GVGSICHFSC 

       550        560        570        580        590        600 
NEDFELLGSE NVECTVSGRW SAPPPTCKGI TSLPAPAVRC PALTTPGQGT MSCQHHLGSF 

       610        620        630        640        650        660 
GPNTTCYFGC KTGFTLRGAN SLRCRASGQW TAVTPMCRAV KCSELHMDTA VAMNCSNPWG 

       670        680        690        700        710        720 
NFSYGSTCTF QCPEGQSLNG SVRATCREDG HWSDAMPTCQ AGTLTIQEAL TYLGGAVAST 

       730        740        750        760 
TGLAVGGTLL ALLRKRLRKK DDGKCPLNPH SHLGTYGVFT NAAYDPTP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the mouse endothelial selectins. Expression of both E- and P-selectin is inducible by tumor necrosis factor alpha."
Weller A., Isenmann S., Vestweber D.
J. Biol. Chem. 267:15176-15183(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]"Molecular cloning and analysis of in vivo expression of murine P-selectin."
Sanders W.E. Jr., Wilson R.W., Ballantyne C.M., Beaudet A.L.
Blood 80:795-800(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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 SELPLG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87861 mRNA. Translation: AAA40008.1.
M72332 mRNA. Translation: AAA37712.1.
BC109158 mRNA. Translation: AAI09159.1.
BC109159 mRNA. Translation: AAI09160.1.
PIRA42755.
RefSeqNP_035477.1. NM_011347.2.
UniGeneMm.3337.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GXBX-ray1.80B735-768[»]
ProteinModelPortalQ01102.
SMRQ01102. Positions 42-704.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ01102.
ChEMBLCHEMBL2455.

PTM databases

PhosphoSiteQ01102.

Proteomic databases

PRIDEQ01102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000162746; ENSMUSP00000123924; ENSMUSG00000026580.
GeneID20344.
KEGGmmu:20344.
UCSCuc007dhz.2. mouse.

Organism-specific databases

CTD6403.
MGIMGI:98280. Selp.

Phylogenomic databases

eggNOGNOG242963.
GeneTreeENSGT00750000117319.
HOGENOMHOG000236254.
HOVERGENHBG052375.
InParanoidQ32MF1.
KOK06496.
OMATYGVFTN.
OrthoDBEOG7DZ8J9.
PhylomeDBQ01102.
TreeFamTF326910.

Gene expression databases

BgeeQ01102.
CleanExMM_SELP.
GenevestigatorQ01102.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 8 hits.
[Graphical view]
PRINTSPR00343. SELECTIN.
SMARTSM00032. CCP. 8 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 8 hits.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50923. SUSHI. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio298177.
PROQ01102.
SOURCESearch...

Entry information

Entry nameLYAM3_MOUSE
AccessionPrimary (citable) accession number: Q01102
Secondary accession number(s): Q32MF1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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