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Protein

Platelet endothelial cell adhesion molecule

Gene

Pecam1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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

  • cell adhesion Source: UniProtKB-KW
  • negative regulation of actin filament polymerization Source: RGD
  • negative regulation of GTPase activity Source: RGD
  • negative regulation of peptidyl-tyrosine phosphorylation Source: RGD
  • positive regulation of leukocyte migration Source: RGD
  • response to cytokine Source: RGD
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
Synonyms:Pecam
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61927. Pecam1.

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 589572ExtracellularSequence analysisAdd
BLAST
Transmembranei590 – 61021HelicalSequence analysisAdd
BLAST
Topological domaini611 – 67868CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cell surface Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 678661Platelet endothelial cell adhesion moleculePRO_0000045176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 99PROSITE-ProRule annotation
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi142 ↔ 195PROSITE-ProRule annotation
Disulfide bondi245 ↔ 293PROSITE-ProRule annotation
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi336 ↔ 375PROSITE-ProRule annotation
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi420 ↔ 465PROSITE-ProRule annotation
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence analysis
Disulfide bondi512 ↔ 561PROSITE-ProRule annotation
Glycosylationi540 – 5401N-linked (GlcNAc...)Sequence analysis
Modified residuei660 – 6601Phosphotyrosine; by FERBy similarity

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

PaxDbiQ3SWT0.
PRIDEiQ3SWT0.

PTM databases

iPTMnetiQ3SWT0.
PhosphoSiteiQ3SWT0.

Expressioni

Gene expression databases

BgeeiENSRNOG00000043391.

Interactioni

Subunit structurei

Interacts with PTPN11. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044403.

Structurei

3D structure databases

ProteinModelPortaliQ3SWT0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 12687Ig-like C2-type 1Add
BLAST
Domaini135 – 21379Ig-like C2-type 2Add
BLAST
Domaini225 – 30985Ig-like C2-type 3Add
BLAST
Domaini315 – 39177Ig-like C2-type 4Add
BLAST
Domaini413 – 47260Ig-like C2-type 5Add
BLAST
Domaini488 – 57790Ig-like C2-type 6Add
BLAST

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

HOVERGENiHBG059434.
InParanoidiQ3SWT0.
KOiK06471.
PhylomeDBiQ3SWT0.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q3SWT0-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:678
Mass (Da):76,189
Last modified:October 11, 2005 - v1
Checksum:i58062E6CC3FD16E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC104711 mRNA. Translation: AAI04712.1.
U77697 mRNA. Translation: AAB36541.1.
RefSeqiNP_113779.1. NM_031591.1.
UniGeneiRn.1878.

Genome annotation databases

GeneIDi29583.
KEGGirno:29583.
UCSCiRGD:61927. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC104711 mRNA. Translation: AAI04712.1.
U77697 mRNA. Translation: AAB36541.1.
RefSeqiNP_113779.1. NM_031591.1.
UniGeneiRn.1878.

3D structure databases

ProteinModelPortaliQ3SWT0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044403.

PTM databases

iPTMnetiQ3SWT0.
PhosphoSiteiQ3SWT0.

Proteomic databases

PaxDbiQ3SWT0.
PRIDEiQ3SWT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29583.
KEGGirno:29583.
UCSCiRGD:61927. rat.

Organism-specific databases

CTDi5175.
RGDi61927. Pecam1.

Phylogenomic databases

HOVERGENiHBG059434.
InParanoidiQ3SWT0.
KOiK06471.
PhylomeDBiQ3SWT0.

Miscellaneous databases

PROiQ3SWT0.

Gene expression databases

BgeeiENSRNOG00000043391.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPECA1_RAT
AccessioniPrimary (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: September 7, 2016
This is version 69 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.