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Protein

Platelet endothelial cell adhesion molecule

Gene

PECAM1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-692 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. Induces susceptibility to atherosclerosis (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet endothelial cell adhesion molecule
Short name:
PECAM-1
Alternative name(s):
CD_antigen: CD31
Gene namesi
Name:PECAM1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 12

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Membrane raft By similarity
  • Cell junction By similarity

  • Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 602ExtracellularSequence analysisAdd BLAST575
Transmembranei603 – 621HelicalSequence analysisAdd BLAST19
Topological domaini622 – 740CytoplasmicSequence analysisAdd BLAST119

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
ChainiPRO_000001489728 – 740Platelet endothelial cell adhesion moleculeAdd BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi57 ↔ 109PROSITE-ProRule annotation
Glycosylationi84N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi152 ↔ 206PROSITE-ProRule annotation
Disulfide bondi256 ↔ 304PROSITE-ProRule annotation
Glycosylationi284N-linked (GlcNAc...)Sequence analysis1
Glycosylationi301N-linked (GlcNAc...)Sequence analysis1
Glycosylationi320N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi347 ↔ 387PROSITE-ProRule annotation
Glycosylationi357N-linked (GlcNAc...)Sequence analysis1
Glycosylationi372N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi432 ↔ 477PROSITE-ProRule annotation
Glycosylationi436N-linked (GlcNAc...)Sequence analysis1
Glycosylationi456N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi524 ↔ 573PROSITE-ProRule annotation
Glycosylationi552N-linked (GlcNAc...)Sequence analysis1
Modified residuei692Phosphotyrosine; by FERBy similarity1
Modified residuei715Phosphotyrosine; by FERBy similarity1

Post-translational modificationi

Phosphorylated on Ser and Tyr residues after cellular activation. In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation. Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation (By similarity).By similarity
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ95242.
PeptideAtlasiQ95242.
PRIDEiQ95242.

Expressioni

Gene expression databases

BgeeiENSSSCG00000017277.
GenevisibleiQ95242. SS.

Interactioni

Subunit structurei

Interacts with PTPN11; Tyr-715 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000018307.

Structurei

3D structure databases

ProteinModelPortaliQ95242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 126Ig-like C2-type 1Add BLAST92
Domaini145 – 223Ig-like C2-type 2Add BLAST79
Domaini236 – 315Ig-like C2-type 3Add BLAST80
Domaini328 – 404Ig-like C2-type 4Add BLAST77
Domaini425 – 494Ig-like C2-type 5Add BLAST70
Domaini500 – 592Ig-like C2-type 6Add BLAST93

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni723 – 740May play a role in cytoprotective signalingBy similarityAdd BLAST18

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II37. Eukaryota.
ENOG4111F9A. LUCA.
GeneTreeiENSGT00440000034155.
HOGENOMiHOG000049132.
HOVERGENiHBG059434.
InParanoidiQ95242.
KOiK06471.
OMAiENSFTIN.
OrthoDBiEOG091G033M.
TreeFamiTF338229.

Family and domain databases

Gene3Di2.60.40.10. 6 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF13895. Ig_2. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q95242-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLRWTQGGN MWLGVLLTLQ LCSSLEGQEN SFTINSIHME MLPGQEVHNG
60 70 80 90 100
ENLTLQCIVD VSTTSSVKPQ HQVLFYKDDV LFHNVSSTKN TESYFISEAR
110 120 130 140 150
VYNSGRYKCT VILNNKEKTT AEYKVVVEGV SNPRVTLDKK EVIEGGVVKV
160 170 180 190 200
TCSVPEEKPP VHFIIEKFEL NVRDVKQRRE KTANNQNSVT LEFTVEEQDR
210 220 230 240 250
VILFSCQANV IFGTRVEISD SVRSDLVTVR ESFSNPKFHI SPKGVIIEGD
260 270 280 290 300
QLLIKCTIQV THQAQSFPEI IIQKDKEIVA HSRNGSEAVY SVMATVEHNS
310 320 330 340 350
NYTCKVEASR ISKVSSIMVN ITELFSRPKL KSSATRLDQG ESLRLWCSIP
360 370 380 390 400
GAPPEANFTI QKGGMMMLQD QNLTKVASER DSGTYTCVAG IGKVVKRSNE
410 420 430 440 450
VQIAVCEMLS KPSIFHDSGS EVIKGQTIEV SCQSINGTSP ISYQLLKGSD
460 470 480 490 500
LLASQNVSSN EPAVFKDNPT KDVEYQCIAD NCHSHAGMPS KVLRVKVIAP
510 520 530 540 550
VEEVKLSILL SEEVESGQAI VLQCSVKEGS GPITYKFYKE KENKPFHQVT
560 570 580 590 600
LNDTQAIWHK PKASKDQEGQ YYCLASNRAT PSKNFLQSNI LAVRVYLAPW
610 620 630 640 650
KKGLIAVVVI AVIIAVLLLG ARFYFLKKSK AKQMPVEMCR PAAPLLNSNN
660 670 680 690 700
EKTLSDPNTE ANRHYGYNED VGNHAMKPLN ENKEPLTLDV EYTEVEVTSP
710 720 730 740
EPHRGLGTKG TETVYSEIRK ADPDLVENRY SRTEGSLDGT
Length:740
Mass (Da):82,379
Last modified:February 1, 1997 - v1
Checksum:iF312DC62C4B4A217
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98505 mRNA. Translation: CAA67129.1.
RefSeqiNP_999072.1. NM_213907.1.
UniGeneiSsc.14558.

Genome annotation databases

EnsembliENSSSCT00000018809; ENSSSCP00000018307; ENSSSCG00000017277.
GeneIDi396941.
KEGGissc:396941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98505 mRNA. Translation: CAA67129.1.
RefSeqiNP_999072.1. NM_213907.1.
UniGeneiSsc.14558.

3D structure databases

ProteinModelPortaliQ95242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000018307.

Proteomic databases

PaxDbiQ95242.
PeptideAtlasiQ95242.
PRIDEiQ95242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000018809; ENSSSCP00000018307; ENSSSCG00000017277.
GeneIDi396941.
KEGGissc:396941.

Organism-specific databases

CTDi5175.

Phylogenomic databases

eggNOGiENOG410II37. Eukaryota.
ENOG4111F9A. LUCA.
GeneTreeiENSGT00440000034155.
HOGENOMiHOG000049132.
HOVERGENiHBG059434.
InParanoidiQ95242.
KOiK06471.
OMAiENSFTIN.
OrthoDBiEOG091G033M.
TreeFamiTF338229.

Gene expression databases

BgeeiENSSSCG00000017277.
GenevisibleiQ95242. SS.

Family and domain databases

Gene3Di2.60.40.10. 6 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF13895. Ig_2. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPECA1_PIG
AccessioniPrimary (citable) accession number: Q95242
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 30, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.