UniProtKB - Q3SWT0 (PECA1_RAT)
Protein
Platelet endothelial cell adhesion molecule
Gene
Pecam1
Organism
Rattus norvegicus (Rat)
Status
Functioni
Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-660 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. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis.By similarity
GO - Molecular functioni
- protein homodimerization activity Source: RGD
- protein phosphatase binding Source: RGD
- transmembrane signaling receptor activity Source: GO_Central
GO - Biological processi
- angiogenesis Source: RGD
- bicellular tight junction assembly Source: RGD
- cell adhesion Source: RGD
- cell-cell adhesion Source: RGD
- cell-cell adhesion via plasma-membrane adhesion molecules Source: RGD
- cell surface receptor signaling pathway Source: GO_Central
- cellular response to interferon-gamma Source: RGD
- cellular response to organic cyclic compound Source: RGD
- cellular response to transforming growth factor beta stimulus Source: RGD
- diapedesis Source: RGD
- endothelial cell-matrix adhesion Source: RGD
- endothelial cell migration Source: RGD
- endothelial cell morphogenesis Source: RGD
- establishment of endothelial barrier Source: RGD
- glomerular endothelium development Source: RGD
- homophilic cell adhesion via plasma membrane adhesion molecules Source: RGD
- leukocyte cell-cell adhesion Source: RGD
- monocyte extravasation Source: RGD
- negative regulation of actin filament polymerization Source: RGD
- negative regulation of GTPase activity Source: RGD
- negative regulation of peptidyl-tyrosine phosphorylation Source: RGD
- neutrophil extravasation Source: RGD
- phagocytosis Source: RGD
- positive regulation of cell migration Source: RGD
- positive regulation of cellular extravasation Source: RGD
- positive regulation of leukocyte migration Source: RGD
- positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
- positive regulation of protein localization to cell-cell junction Source: RGD
- positive regulation of protein phosphorylation Source: RGD
- positive regulation of tyrosine phosphorylation of STAT protein Source: RGD
- regulation of cell migration Source: RGD
- Rho protein signal transduction Source: RGD
- wound healing Source: RGD
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 Synonyms:Pecam |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 61927, Pecam1 |
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
Extracellular region or secreted
- extracellular space Source: RGD
Plasma Membrane
- external side of plasma membrane Source: RGD
- integral component of plasma membrane Source: GO_Central
- plasma membrane Source: RGD
Other locations
- cell periphery Source: RGD
- cell surface Source: RGD
- cell-cell contact zone Source: RGD
- cell-cell junction Source: RGD
- cytoplasm Source: RGD
- membrane Source: RGD
- membrane raft Source: RGD
- protein-containing complex Source: RGD
- ruffle Source: RGD
- smooth muscle contractile fiber Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 18 – 589 | ExtracellularSequence analysisAdd BLAST | 572 | |
Transmembranei | 590 – 610 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 611 – 678 | CytoplasmicSequence analysisAdd BLAST | 68 |
Keywords - Cellular componenti
Cell junction, Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 17 | Sequence analysisAdd BLAST | 17 | |
ChainiPRO_0000045176 | 18 – 678 | Platelet endothelial cell adhesion moleculeAdd BLAST | 661 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 47 ↔ 99 | PROSITE-ProRule annotation | ||
Glycosylationi | 74 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 141 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 142 ↔ 195 | PROSITE-ProRule annotation | ||
Disulfide bondi | 245 ↔ 293 | PROSITE-ProRule annotation | ||
Glycosylationi | 309 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 336 ↔ 375 | PROSITE-ProRule annotation | ||
Glycosylationi | 345 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 360 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 420 ↔ 465 | PROSITE-ProRule annotation | ||
Glycosylationi | 424 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 512 ↔ 561 | PROSITE-ProRule annotation | ||
Glycosylationi | 540 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 660 | Phosphotyrosine; by FERBy similarity | 1 |
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
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.By similarity
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
PaxDbi | Q3SWT0 |
PRIDEi | Q3SWT0 |
PTM databases
GlyGeni | Q3SWT0, 7 sites |
iPTMneti | Q3SWT0 |
PhosphoSitePlusi | Q3SWT0 |
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.
Forms a complex with BDKRB2 and GNAQ.
Interacts with BDKRB2 and GNAQ.
Interacts with PTPN11.
Interacts with FER.
Interacts with CD177; the interaction is Ca2+-dependent; the interaction is direct.
By similarityGO - Molecular functioni
- protein homodimerization activity Source: RGD
- protein phosphatase binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000044403 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 40 – 126 | Ig-like C2-type 1Add BLAST | 87 | |
Domaini | 135 – 213 | Ig-like C2-type 2Add BLAST | 79 | |
Domaini | 225 – 309 | Ig-like C2-type 3Add BLAST | 85 | |
Domaini | 315 – 391 | Ig-like C2-type 4Add BLAST | 77 | |
Domaini | 413 – 472 | Ig-like C2-type 5Add BLAST | 60 | |
Domaini | 488 – 577 | Ig-like C2-type 6Add BLAST | 90 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 658 – 663 | ITIM motifBy similarity | 6 |
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
Keywords - Domaini
Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502QW63, Eukaryota |
InParanoidi | Q3SWT0 |
OrthoDBi | 419506at2759 |
PhylomeDBi | Q3SWT0 |
Family and domain databases
Gene3Di | 2.60.40.10, 4 hits |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR003599, Ig_sub IPR003598, Ig_sub2 IPR013151, Immunoglobulin |
Pfami | View protein in Pfam PF00047, ig, 1 hit PF13895, Ig_2, 1 hit |
SMARTi | View protein in SMART SM00409, IG, 4 hits SM00408, IGc2, 2 hits |
SUPFAMi | SSF48726, SSF48726, 4 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
Q3SWT0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLLALLLTML LYASLQAQEN SFTINSIHME SRPSWEVSNG QKLTLQCLVD
60 70 80 90 100
ISTTSKSRPQ HQVLFYKDDA LVYNVSSSEH TESFVIPQSR VFHAGKYKCT
110 120 130 140 150
VILNSKEKTT IEYQLTVNGV PMPEVTVDKK EVTEGGIVTV NCSMQEEKPP
160 170 180 190 200
IYFKIEKVEL GTKNVKLSRE KTSNMNFVLI EFPIEEQDHL LVFRCQAGVL
210 220 230 240 250
SGIKMQTSEF IRSEYVTVQE FFSTPKFQIQ PPEMIIEGNQ LHIKCSVQVA
260 270 280 290 300
HLAQEFPEII IQKDKAIVAT SKQSKEAVYS VMALVEHSGH YTCKVESNRI
310 320 330 340 350
SKASSILVNI TELFPRPKLE LSSSRLDQGE MLDLSCSVSG APVANFTIQK
360 370 380 390 400
EETVLSQYQN FSKIAEERDS GLYSCTAGIG KVVKRSNLVP VQVCEMLSKP
410 420 430 440 450
RIFHDAKFEI IKGQIIGISC QSVNGTAPIT YRLLRAKSNF QTVQKNSNDP
460 470 480 490 500
VTFTDKPTRD MEYQCIVDNC HSHPEVRSEI LRVKVIAPVD EVTISILSGN
510 520 530 540 550
DVQSGDEMVL RCSVKEGTGP VTFQFYKEKE GRPFHEETVN DTQVFWHHEQ
560 570 580 590 600
TSKEQEGQYY CTAFNRASIV TSLRSGPLTV RVFLAPWKKG LIAVVVIGVV
610 620 630 640 650
IAALIVAAKY YFLRKAKAKQ KPVEMSRPAV PLLNSNSEKV SEPSVETNSH
660 670
YDSQNMDVEY TEVEVSSLEP HQENGRLP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC104711 mRNA Translation: AAI04712.1 U77697 mRNA Translation: AAB36541.1 |
RefSeqi | NP_113779.1, NM_031591.1 |
Genome annotation databases
GeneIDi | 29583 |
KEGGi | rno:29583 |
UCSCi | RGD:61927, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC104711 mRNA Translation: AAI04712.1 U77697 mRNA Translation: AAB36541.1 |
RefSeqi | NP_113779.1, NM_031591.1 |
3D structure databases
SMRi | Q3SWT0 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000044403 |
PTM databases
GlyGeni | Q3SWT0, 7 sites |
iPTMneti | Q3SWT0 |
PhosphoSitePlusi | Q3SWT0 |
Proteomic databases
PaxDbi | Q3SWT0 |
PRIDEi | Q3SWT0 |
Genome annotation databases
GeneIDi | 29583 |
KEGGi | rno:29583 |
UCSCi | RGD:61927, rat |
Organism-specific databases
CTDi | 5175 |
RGDi | 61927, Pecam1 |
Phylogenomic databases
eggNOGi | ENOG502QW63, Eukaryota |
InParanoidi | Q3SWT0 |
OrthoDBi | 419506at2759 |
PhylomeDBi | Q3SWT0 |
Miscellaneous databases
PROi | PR:Q3SWT0 |
Family and domain databases
Gene3Di | 2.60.40.10, 4 hits |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR003599, Ig_sub IPR003598, Ig_sub2 IPR013151, Immunoglobulin |
Pfami | View protein in Pfam PF00047, ig, 1 hit PF13895, Ig_2, 1 hit |
SMARTi | View protein in SMART SM00409, IG, 4 hits SM00408, IGc2, 2 hits |
SUPFAMi | SSF48726, SSF48726, 4 hits |
PROSITEi | View protein in PROSITE PS50835, IG_LIKE, 4 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PECA1_RAT | |
Accessioni | Q3SWT0Primary (citable) accession number: Q3SWT0 Secondary accession number(s): P97635 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2005 |
Last sequence update: | October 11, 2005 | |
Last modified: | April 7, 2021 | |
This is version 90 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |