UniProtKB - P51866 (PECA1_BOVIN)
Platelet endothelial cell adhesion molecule
PECAM1
Functioni
GO - Molecular functioni
- transmembrane signaling receptor activity Source: GO_Central
GO - Biological processi
- cell-cell adhesion via plasma-membrane adhesion molecules Source: GO_Central
- cell surface receptor signaling pathway Source: GO_Central
- positive regulation of protein phosphorylation Source: ARUK-UCL
Keywordsi
Biological process | Cell adhesion |
Names & Taxonomyi
Protein namesi | Recommended name: Platelet endothelial cell adhesion moleculeShort name: PECAM-1 Alternative name(s): CD_antigen: CD31 |
Gene namesi | Name:PECAM1 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Single-pass type I membrane protein By similarity
Other locations
- 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. Cell surface expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated stimulation.By similarity
Plasma Membrane
- integral component of plasma membrane Source: GO_Central
Other locations
- cell junction Source: UniProtKB-SubCell
- membrane raft Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 28 – 599 | ExtracellularSequence analysisAdd BLAST | 572 | |
Transmembranei | 600 – 618 | HelicalSequence analysisAdd BLAST | 19 | |
Topological domaini | 619 – 739 | CytoplasmicSequence analysisAdd BLAST | 121 |
Keywords - Cellular componenti
Cell junction, Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 689 | Y → F: Strongly reduced phosphorylation by FER. Abolishes phosphorylation by FER; when associated with F-714. 1 Publication | 1 | |
Mutagenesisi | 714 | Y → F: Reduced phosphorylation by FER. Abolishes phosphorylation by FER; when associated with F-689. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 27 | By similarityAdd BLAST | 27 | |
ChainiPRO_0000014894 | 28 – 739 | Platelet endothelial cell adhesion moleculeAdd BLAST | 712 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 52 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 57 ↔ 109 | PROSITE-ProRule annotation | ||
Glycosylationi | 84 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 151 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 152 ↔ 206 | PROSITE-ProRule annotation | ||
Disulfide bondi | 256 ↔ 304 | PROSITE-ProRule annotation | ||
Glycosylationi | 301 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 320 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 347 ↔ 386 | PROSITE-ProRule annotation | ||
Glycosylationi | 356 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 371 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 431 ↔ 476 | PROSITE-ProRule annotation | ||
Glycosylationi | 435 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 446 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 453 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 522 ↔ 571 | PROSITE-ProRule annotation | ||
Glycosylationi | 550 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 578 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Lipidationi | 620 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 689 | Phosphotyrosine; by FER1 Publication | 1 | |
Modified residuei | 714 | Phosphotyrosine; by FER1 Publication | 1 | |
Modified residuei | 730 | PhosphoserineBy similarity | 1 | |
Modified residuei | 735 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinProteomic databases
PaxDbi | P51866 |
PRIDEi | P51866 |
PTM databases
iPTMneti | P51866 |
Interactioni
Subunit structurei
Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-type 2 domains); trans-homodimerization is required for cell-cell interaction (By similarity).
Forms a complex with BDKRB2 and GNAQ (By similarity).
Interacts with BDKRB2 and GNAQ (By similarity).
Interacts with PTPN11; Tyr-714 is critical for PTPN11 recruitment (PubMed:12972546).
Interacts with FER (PubMed:12972546).
Interacts with CD177; the interaction is Ca2+-dependent; the interaction is direct (By similarity).
By similarity1 PublicationProtein-protein interaction databases
STRINGi | 9913.ENSBTAP00000040327 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 35 – 120 | Ig-like C2-type 1Add BLAST | 86 | |
Domaini | 145 – 213 | Ig-like C2-type 2Add BLAST | 69 | |
Domaini | 236 – 315 | Ig-like C2-type 3Add BLAST | 80 | |
Domaini | 328 – 403 | Ig-like C2-type 4Add BLAST | 76 | |
Domaini | 424 – 493 | Ig-like C2-type 5Add BLAST | 70 | |
Domaini | 499 – 590 | Ig-like C2-type 6Add BLAST | 92 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 708 – 730 | Membrane-bound segment which detaches upon phosphorylationBy similarityAdd BLAST | 23 | |
Regioni | 722 – 739 | May play a role in cytoprotective signalingBy similarityAdd BLAST | 18 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 687 – 692 | ITIM motif 1By similarity | 6 | |
Motifi | 712 – 717 | ITIM motif 2By similarity | 6 |
Domaini
Keywords - Domaini
Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502QW63, Eukaryota |
InParanoidi | P51866 |
OrthoDBi | 419506at2759 |
Family and domain databases
Gene3Di | 2.60.40.10, 6 hits |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR040878, Ig_C17orf99 IPR003599, Ig_sub |
Pfami | View protein in Pfam PF13895, Ig_2, 3 hits PF17736, Ig_C17orf99, 1 hit |
SMARTi | View protein in SMART SM00409, IG, 5 hits |
SUPFAMi | SSF48726, SSF48726, 5 hits |
PROSITEi | View protein in PROSITE PS50835, IG_LIKE, 4 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MQLRWTQRGM MWLGALLTLL LCSSLKGQEN SFTINSIHMQ ILPHSTVQNG
60 70 80 90 100
ENLTLQCLVD VSTTSRVKPL HQVLFYKDDV LLHNVSSRRN TESYLIPHVR
110 120 130 140 150
VCDSGRYKCN VILNNKEKTT PEYEVWVKGV SDPRVTLDKK EVIEGGVVVV
160 170 180 190 200
NCSVPEEKAP VHFTIEKFEL NIRGAKKKRE KTSQNQNFVT LEFTVEEQDR
210 220 230 240 250
TIRFQCQAKI FSGSNVESSR PIQSDLVTVR ESFSNPKFHI IPEGKVMEGD
260 270 280 290 300
DLQVKCTVQV THQAQSFPEI IIQKDREIVA HNSLSSEAVY SVMATTEHNG
310 320 330 340 350
NYTCKVEASR ISKVSSVVVN VTELFSKPKL ESSATHLDQG EDLNLLCSIP
360 370 380 390 400
GAPPANFTIQ KGGMTVSQTQ NFTKRVSEWD SGLYTCVAGV GRVFKRSNTV
410 420 430 440 450
QITVCEMLSK PSIFHDSRSE VIKGQTIEVS CQSVNGTAPI FYQLSNTSKP
460 470 480 490 500
VANQSVGSNK PAIFRVKPTK DVEYCCSADN CHSHSKMFSE VLRVKVIAPV
510 520 530 540 550
DEAQLVVLKG EVEPGEPIVF YCSVNEGSFP ITYKFYKEKE SKPFYQDTIN
560 570 580 590 600
ATQIMWHKTT ASKEYEGQYY CTASNRANLS KHVIQSNTLT VRVYLPLEKG
610 620 630 640 650
LIAVVVIGVI IVTLVLGAKC YFLKKAKAKQ MPVEMSRPAV PLLNSNNEKT
660 670 680 690 700
LSDAGTEADR HYGYNEDVGN HAMKPLNENK EPLTLDVEYT EVEVTSPEPH
710 720 730
QGLGTKGTET ETVYSEIRKA DPDFVENRYS RTEGSLDGS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U35433 mRNA Translation: AAC48566.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U35433 mRNA Translation: AAC48566.1 |
3D structure databases
SMRi | P51866 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9913.ENSBTAP00000040327 |
PTM databases
iPTMneti | P51866 |
Proteomic databases
PaxDbi | P51866 |
PRIDEi | P51866 |
Phylogenomic databases
eggNOGi | ENOG502QW63, Eukaryota |
InParanoidi | P51866 |
OrthoDBi | 419506at2759 |
Family and domain databases
Gene3Di | 2.60.40.10, 6 hits |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR040878, Ig_C17orf99 IPR003599, Ig_sub |
Pfami | View protein in Pfam PF13895, Ig_2, 3 hits PF17736, Ig_C17orf99, 1 hit |
SMARTi | View protein in SMART SM00409, IG, 5 hits |
SUPFAMi | SSF48726, SSF48726, 5 hits |
PROSITEi | View protein in PROSITE PS50835, IG_LIKE, 4 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PECA1_BOVIN | |
Accessioni | P51866Primary (citable) accession number: P51866 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | April 7, 2021 | |
This is version 119 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |