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Q08481 (PECA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet endothelial cell adhesion molecule

Short name=PECAM-1
Alternative name(s):
CD_antigen=CD31
Gene names
Name:Pecam1
Synonyms:Pecam, Pecam-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-679 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Modulates BDKRB2 activation By similarity. Induces susceptibility to atherosclerosis. Ref.9

Subunit structure

Interacts with PTPN11; Tyr-702 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Cell membrane; Lipid-anchor By similarity. Cell junction. Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells By similarity.

Tissue specificity

Isoform 1 and isoform 3 are expressed in lung and platelets. Ref.10

Domain

The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity By similarity.

Post-translational modification

Phosphorylated on Ser and Tyr residues after cellular activation. In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation By similarity. Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation. Ref.7

Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells By similarity.

Disruption phenotype

Mice show reduced atherosclerotic lesions. There is down-regulation of ICAM-1 in endothelial cells at the lesion periphery, and reduced disruption of Cx43 junctional staining at arterial branch points and in the descending aorta. Ref.9

Sequence similarities

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRho protein signal transduction

Inferred from mutant phenotype PubMed 12890700. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular component movement

Inferred from electronic annotation. Source: Ensembl

negative regulation of Rho GTPase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of leukocyte migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from direct assay PubMed 11254359. Source: MGI

regulation of cell migration

Inferred from mutant phenotype PubMed 12890700. Source: MGI

response to cytokine

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from mutant phenotype PubMed 12890700. Source: MGI

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell periphery

Inferred from direct assay PubMed 21464233. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 20620994. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 16691571. Source: MGI

membrane raft

Inferred from direct assay PubMed 12890700. Source: MGI

plasma membrane

Inferred from direct assay PubMed 12736726PubMed 16251442. Source: MGI

smooth muscle contractile fiber

Inferred from direct assay PubMed 18332105. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 10562326PubMed 11254359. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08481-1)

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.
Isoform 2 (identifier: Q08481-2)

The sequence of this isoform differs from the canonical sequence as follows:
     692-727: ALGTRATETVYSEIRKVDPNLMENRYSRTEGSLNGT → ENGRLP
Isoform 3 (identifier: Q08481-3)

The sequence of this isoform differs from the canonical sequence as follows:
     711-727: NLMENRYSRTEGSLNGT → KNGRLP
Isoform 4 (identifier: Q08481-4)

The sequence of this isoform differs from the canonical sequence as follows:
     119-219: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.6
Chain18 – 727710Platelet endothelial cell adhesion molecule
PRO_0000014896

Regions

Topological domain18 – 590573Extracellular Potential
Transmembrane591 – 60919Helical; Potential
Topological domain610 – 727118Cytoplasmic Potential
Domain40 – 12687Ig-like C2-type 1
Domain135 – 21379Ig-like C2-type 2
Domain225 – 30985Ig-like C2-type 3
Domain315 – 39177Ig-like C2-type 4
Domain413 – 47260Ig-like C2-type 5
Domain488 – 57891Ig-like C2-type 6
Region710 – 72718May play a role in cytoprotective signaling By similarity

Amino acid modifications

Modified residue6791Phosphotyrosine; by FER Probable
Modified residue7021Phosphotyrosine; by FER Ref.7 Ref.8
Lipidation6111S-palmitoyl cysteine By similarity
Glycosylation741N-linked (GlcNAc...) Ref.11
Glycosylation1411N-linked (GlcNAc...) Ref.11
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Ref.11
Glycosylation4241N-linked (GlcNAc...) Ref.11
Glycosylation5401N-linked (GlcNAc...) Ref.11
Disulfide bond47 ↔ 99 Potential
Disulfide bond142 ↔ 195 Potential
Disulfide bond245 ↔ 293 Potential
Disulfide bond336 ↔ 375 Potential
Disulfide bond420 ↔ 465 Potential
Disulfide bond512 ↔ 561 Potential

Natural variations

Alternative sequence119 – 219101Missing in isoform 4.
VSP_038723
Alternative sequence692 – 72736ALGTR…SLNGT → ENGRLP in isoform 2.
VSP_038724
Alternative sequence711 – 72717NLMEN…SLNGT → KNGRLP in isoform 3.
VSP_038725

Experimental info

Mutagenesis6791Y → F: Reduces tyrosine phosphorylation by FER by about 60%. Ref.7
Mutagenesis7021Y → F: Reduces tyrosine phosphorylation by FER by about 60%. Ref.7
Mutagenesis7171Y → F: No significant effect on phosphorylation by FER. Ref.7
Sequence conflict181E → T AA sequence Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 34C04752D199BAA5

FASTA72781,263
        10         20         30         40         50         60 
MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD ISTTSKSRSQ 

        70         80         90        100        110        120 
HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT VMLNNKEKTT IEYEVKVHGV 

       130        140        150        160        170        180 
SKPKVTLDKK EVTEGGVVTV NCSLQEEKPP IFFKIEKLEV GTKFVKRRID KTSNENFVLM 

       190        200        210        220        230        240 
EFPIEAQDHV LVFRCQAGIL SGFKLQESEP IRSEYVTVQE SFSTPKFEIK PPGMIIEGDQ 

       250        260        270        280        290        300 
LHIRCIVQVT HLVQEFTEII IQKDKAIVAT SKQSSEAVYS VMAMVEYSGH YTCKVESNRI 

       310        320        330        340        350        360 
SKASSIMVNI TELFPKPKLE FSSSRLDQGE LLDLSCSVSG TPVANFTIQK EETVLSQYQN 

       370        380        390        400        410        420 
FSKIAEESDS GEYSCTAGIG KVVKRSGLVP IQVCEMLSKP SIFHDAKSEI IKGHAIGISC 

       430        440        450        460        470        480 
QSENGTAPIT YHLMKAKSDF QTLEVTSNDP ATFTDKPTRD MEYQCRADNC HSHPAVFSEI 

       490        500        510        520        530        540 
LRVRVIAPVD EVVISILSSN EVQSGSEMVL RCSVKEGTSP ITFQFYKEKE DRPFHQAVVN 

       550        560        570        580        590        600 
DTQAFWHNKQ ASKKQEGQYY CTASNRASSM RTSPRSSTLA VRVFLAPWKK GLIAVVVIGV 

       610        620        630        640        650        660 
VIATLIVAAK CYFLRKAKAK QKPVEMSRPA APLLNSNSEK ISEPSVEANS HYGYDDVSGN 

       670        680        690        700        710        720 
DAVKPINQNK DPQNMDVEYT EVEVSSLEPH QALGTRATET VYSEIRKVDP NLMENRYSRT 


EGSLNGT 

« Hide

Isoform 2 [UniParc].

Checksum: EF8538025C1AB55F
Show »

FASTA69777,917
Isoform 3 [UniParc].

Checksum: E4D281B5523017B6
Show »

FASTA71680,004
Isoform 4 [UniParc].

Checksum: 0CF4D64C49CE468B
Show »

FASTA62669,823

References

« Hide 'large scale' references
[1]"Molecular cloning and adhesive properties of murine platelet/endothelial cell adhesion molecule 1."
Xie Y., Muller W.A.
Proc. Natl. Acad. Sci. U.S.A. 90:5569-5573(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
Tissue: Lung.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Strain: C57BL/6J.
Tissue: Stomach.
[3]"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.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 2).
Strain: C57BL/6 and FVB/N.
Tissue: Mammary tumor.
[6]"Association of murine CD31 with transmigrating lymphocytes following antigenic stimulation."
Bogen S.A., Baldwin H.S., Watkins S.C., Albelda S.M., Abbas A.K.
Am. J. Pathol. 141:843-854(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-26.
Tissue: Heart.
[7]"Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-679 AND TYR-702 BY FES AND FER, MUTAGENESIS OF TYR-679; TYR-702 AND TYR-717.
[8]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[9]"PECAM-1 is a critical mediator of atherosclerosis."
Stevens H.Y., Melchior B., Bell K.S., Yun S., Yeh J.C., Frangos J.A.
Dis. Model. Mech. 1:175-181(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"An alternatively spliced isoform of PECAM-1 is expressed at high levels in human and murine tissues, and suggests a novel role for the C-terminus of PECAM-1 in cytoprotective signaling."
Bergom C., Paddock C., Gao C., Holyst T., Newman D.K., Newman P.J.
J. Cell Sci. 121:1235-1242(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), TISSUE SPECIFICITY.
[11]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-141; ASN-360; ASN-424 AND ASN-540.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06039 mRNA. Translation: AAA16230.1.
AK169431 mRNA. Translation: BAE41172.1.
AL603664 Genomic DNA. Translation: CAM18558.1.
AL603664 Genomic DNA. Translation: CAM18559.1.
AL603664 Genomic DNA. Translation: CAM18560.1.
CH466558 Genomic DNA. Translation: EDL34303.1.
CH466558 Genomic DNA. Translation: EDL34304.1.
CH466558 Genomic DNA. Translation: EDL34305.1.
BC008519 mRNA. Translation: AAH08519.1.
BC085502 mRNA. Translation: AAH85502.1.
CCDSCCDS25558.1. [Q08481-2]
CCDS25559.1. [Q08481-3]
RefSeqNP_001027550.1. NM_001032378.1. [Q08481-2]
NP_032842.2. NM_008816.2. [Q08481-3]
XP_006532533.1. XM_006532470.1. [Q08481-1]
XP_006532539.1. XM_006532476.1. [Q08481-4]
UniGeneMm.343951.

3D structure databases

ProteinModelPortalQ08481.
SMRQ08481. Positions 193-393, 693-727.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ08481. 5 interactions.
MINTMINT-4106994.
STRING10090.ENSMUSP00000067111.

PTM databases

PhosphoSiteQ08481.

Proteomic databases

MaxQBQ08481.
PaxDbQ08481.
PRIDEQ08481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080853; ENSMUSP00000079664; ENSMUSG00000020717. [Q08481-3]
ENSMUST00000103069; ENSMUSP00000099358; ENSMUSG00000020717. [Q08481-2]
ENSMUST00000106796; ENSMUSP00000102408; ENSMUSG00000020717. [Q08481-1]
ENSMUST00000183610; ENSMUSP00000138959; ENSMUSG00000020717. [Q08481-4]
GeneID18613.
KEGGmmu:18613.
UCSCuc007lze.1. mouse. [Q08481-1]
uc007lzf.1. mouse. [Q08481-3]
uc007lzg.1. mouse. [Q08481-2]
uc007lzh.1. mouse. [Q08481-4]

Organism-specific databases

CTD5175.
MGIMGI:97537. Pecam1.

Phylogenomic databases

eggNOGNOG78738.
GeneTreeENSGT00440000034155.
HOGENOMHOG000049132.
HOVERGENHBG059434.
KOK06471.
OrthoDBEOG7Z95KP.
TreeFamTF338229.

Gene expression databases

ArrayExpressQ08481.
BgeeQ08481.
CleanExMM_PECAM1.
GenevestigatorQ08481.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio294550.
PROQ08481.
SOURCESearch...

Entry information

Entry namePECA1_MOUSE
AccessionPrimary (citable) accession number: Q08481
Secondary accession number(s): B1ARB1 expand/collapse secondary AC list , B1ARB2, Q3TES6, Q922E0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 132 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

MGD cross-references

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