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Platelet endothelial cell adhesion molecule (PECAM-1) (CD antigen CD31)

 PECA1_PIG               Reviewed;         740 AA.
Q95242;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
12-SEP-2018, entry version 121.
RecName: Full=Platelet endothelial cell adhesion molecule;
Short=PECAM-1;
AltName: CD_antigen=CD31;
Flags: Precursor;
Name=PECAM1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aortic endothelium;
Nasu K.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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. 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. {ECO:0000250|UniProtKB:P16284,
ECO:0000250|UniProtKB:Q08481}.
-!- SUBUNIT: 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; Tyr-715 is critical for
PTPN11 recruitment. Interacts with FER. Interacts with CD177; the
interaction is Ca(2+)-dependent; the interaction is direct.
{ECO:0000250|UniProtKB:P16284, ECO:0000250|UniProtKB:P51866}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P16284}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P16284}. Membrane raft
{ECO:0000250|UniProtKB:P16284}. Cell junction
{ECO:0000250|UniProtKB:P16284}. 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. {ECO:0000250|UniProtKB:P16284}.
-!- DOMAIN: The Ig-like C2-type domains 2 and 3 contribute to
formation of the complex with BDKRB2 and in regulation of its
activity. {ECO:0000250}.
-!- PTM: Phosphorylated on Ser and Tyr residues by src kinases after
cellular activation. Upon activation, phosphorylated on Ser-731
which probably initiates the dissociation of the membrane-
interaction segment (residues 711-731) from the cell membrane
allowing the sequential phosphorylation of Tyr-715 and Tyr-692.
Constitutively phosphorylated on Ser-736 in resting platelets.
Phosphorylated on tyrosine residues by FER and FES in response to
FCER1 activation. In endothelial cells Fyn mediates mechanical-
force (stretch or pull) induced tyrosine phosphorylation.
{ECO:0000250|UniProtKB:P16284, ECO:0000250|UniProtKB:Q08481}.
-!- PTM: Palmitoylation by ZDHHC21 is necessary for cell surface
expression in endothelial cells and enrichment in membrane rafts.
{ECO:0000250|UniProtKB:P16284}.
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EMBL; X98505; CAA67129.1; -; mRNA.
RefSeq; NP_999072.1; NM_213907.1.
UniGene; Ssc.14558; -.
ProteinModelPortal; Q95242; -.
STRING; 9823.ENSSSCP00000018307; -.
PaxDb; Q95242; -.
PeptideAtlas; Q95242; -.
PRIDE; Q95242; -.
GeneID; 396941; -.
KEGG; ssc:396941; -.
CTD; 5175; -.
eggNOG; ENOG410II37; Eukaryota.
eggNOG; ENOG4111F9A; LUCA.
HOGENOM; HOG000049132; -.
HOVERGEN; HBG059434; -.
InParanoid; Q95242; -.
KO; K06471; -.
OMA; ENSFTIN; -.
OrthoDB; EOG091G033M; -.
TreeFam; TF338229; -.
Proteomes; UP000008227; Unplaced.
Bgee; ENSSSCG00000017277; Expressed in 6 organ(s), highest expression level in lung.
ExpressionAtlas; Q95242; baseline and differential.
Genevisible; Q95242; SS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF13895; Ig_2; 2.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 4.
2: Evidence at transcript level;
Cell adhesion; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 27 {ECO:0000250}.
CHAIN 28 740 Platelet endothelial cell adhesion
molecule.
/FTId=PRO_0000014897.
TOPO_DOM 28 602 Extracellular. {ECO:0000255}.
TRANSMEM 603 621 Helical. {ECO:0000255}.
TOPO_DOM 622 740 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 126 Ig-like C2-type 1.
DOMAIN 145 223 Ig-like C2-type 2.
DOMAIN 236 315 Ig-like C2-type 3.
DOMAIN 328 404 Ig-like C2-type 4.
DOMAIN 425 494 Ig-like C2-type 5.
DOMAIN 500 592 Ig-like C2-type 6.
REGION 711 731 Membrane-bound segment which detaches
upon phosphorylation.
{ECO:0000250|UniProtKB:P16284}.
REGION 723 740 May play a role in cytoprotective
signaling. {ECO:0000250}.
MOTIF 690 695 ITIM motif 1.
{ECO:0000250|UniProtKB:P16284}.
MOTIF 713 718 ITIM motif 2.
{ECO:0000250|UniProtKB:P16284}.
MOD_RES 692 692 Phosphotyrosine; by FER.
{ECO:0000250|UniProtKB:P51866}.
MOD_RES 715 715 Phosphotyrosine; by FER.
{ECO:0000250|UniProtKB:P51866}.
MOD_RES 731 731 Phosphoserine.
{ECO:0000250|UniProtKB:P16284}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000250|UniProtKB:P16284}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 436 436 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 456 456 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 552 552 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 152 206 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 256 304 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 347 387 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 432 477 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 524 573 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 740 AA; 82379 MW; F312DC62C4B4A217 CRC64;
MRLRWTQGGN MWLGVLLTLQ LCSSLEGQEN SFTINSIHME MLPGQEVHNG ENLTLQCIVD
VSTTSSVKPQ HQVLFYKDDV LFHNVSSTKN TESYFISEAR VYNSGRYKCT VILNNKEKTT
AEYKVVVEGV SNPRVTLDKK EVIEGGVVKV TCSVPEEKPP VHFIIEKFEL NVRDVKQRRE
KTANNQNSVT LEFTVEEQDR VILFSCQANV IFGTRVEISD SVRSDLVTVR ESFSNPKFHI
SPKGVIIEGD QLLIKCTIQV THQAQSFPEI IIQKDKEIVA HSRNGSEAVY SVMATVEHNS
NYTCKVEASR ISKVSSIMVN ITELFSRPKL KSSATRLDQG ESLRLWCSIP GAPPEANFTI
QKGGMMMLQD QNLTKVASER DSGTYTCVAG IGKVVKRSNE VQIAVCEMLS KPSIFHDSGS
EVIKGQTIEV SCQSINGTSP ISYQLLKGSD LLASQNVSSN EPAVFKDNPT KDVEYQCIAD
NCHSHAGMPS KVLRVKVIAP VEEVKLSILL SEEVESGQAI VLQCSVKEGS GPITYKFYKE
KENKPFHQVT LNDTQAIWHK PKASKDQEGQ YYCLASNRAT PSKNFLQSNI LAVRVYLAPW
KKGLIAVVVI AVIIAVLLLG ARFYFLKKSK AKQMPVEMCR PAAPLLNSNN EKTLSDPNTE
ANRHYGYNED VGNHAMKPLN ENKEPLTLDV EYTEVEVTSP EPHRGLGTKG TETVYSEIRK
ADPDLVENRY SRTEGSLDGT


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