PECA1_PIG
ID PECA1_PIG Reviewed; 740 AA.
AC Q95242;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Platelet endothelial cell adhesion molecule;
DE Short=PECAM-1;
DE AltName: CD_antigen=CD31;
DE Flags: Precursor;
GN Name=PECAM1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RA Nasu K.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell adhesion molecule which is required for leukocyte
CC transendothelial migration (TEM) under most inflammatory conditions.
CC Tyr-692 plays a critical role in TEM and is required for efficient
CC trafficking of PECAM1 to and from the lateral border recycling
CC compartment (LBRC) and is also essential for the LBRC membrane to be
CC targeted around migrating leukocytes. Trans-homophilic interaction may
CC play a role in endothelial cell-cell adhesion via cell junctions.
CC Heterophilic interaction with CD177 plays a role in transendothelial
CC migration of neutrophils. Homophilic ligation of PECAM1 prevents
CC macrophage-mediated phagocytosis of neighboring viable leukocytes by
CC transmitting a detachment signal. Promotes macrophage-mediated
CC phagocytosis of apoptotic leukocytes by tethering them to the
CC phagocytic cells; PECAM1-mediated detachment signal appears to be
CC disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2
CC activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2
CC activation in endothelial cells. Induces susceptibility to
CC atherosclerosis. {ECO:0000250|UniProtKB:P16284,
CC ECO:0000250|UniProtKB:Q08481}.
CC -!- SUBUNIT: Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-type 2
CC domains); trans-homodimerization is required for cell-cell interaction.
CC Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ.
CC Interacts with PTPN11; Tyr-715 is critical for PTPN11 recruitment.
CC Interacts with FER. Interacts with CD177; the interaction is Ca(2+)-
CC dependent; the interaction is direct. {ECO:0000250|UniProtKB:P16284,
CC ECO:0000250|UniProtKB:P51866}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16284};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16284}.
CC Membrane raft {ECO:0000250|UniProtKB:P16284}. Cell junction
CC {ECO:0000250|UniProtKB:P16284}. Note=Localizes to the lateral border
CC recycling compartment (LBRC) and recycles from the LBRC to the junction
CC in resting endothelial cells. Cell surface expression on neutrophils is
CC down-regulated upon fMLP or CXCL8/IL8-mediated stimulation.
CC {ECO:0000250|UniProtKB:P16284}.
CC -!- DOMAIN: The Ig-like C2-type domains 2 and 3 contribute to formation of
CC the complex with BDKRB2 and in regulation of its activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser and Tyr residues by src kinases after
CC cellular activation. Upon activation, phosphorylated on Ser-731 which
CC probably initiates the dissociation of the membrane-interaction segment
CC (residues 711-731) from the cell membrane allowing the sequential
CC phosphorylation of Tyr-715 and Tyr-692. Constitutively phosphorylated
CC on Ser-736 in resting platelets. Phosphorylated on tyrosine residues by
CC FER and FES in response to FCER1 activation. In endothelial cells Fyn
CC mediates mechanical-force (stretch or pull) induced tyrosine
CC phosphorylation. {ECO:0000250|UniProtKB:P16284,
CC ECO:0000250|UniProtKB:Q08481}.
CC -!- PTM: Palmitoylation by ZDHHC21 is necessary for cell surface expression
CC in endothelial cells and enrichment in membrane rafts.
CC {ECO:0000250|UniProtKB:P16284}.
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DR EMBL; X98505; CAA67129.1; -; mRNA.
DR RefSeq; NP_999072.1; NM_213907.1.
DR AlphaFoldDB; Q95242; -.
DR SMR; Q95242; -.
DR STRING; 9823.ENSSSCP00000018307; -.
DR PaxDb; Q95242; -.
DR PeptideAtlas; Q95242; -.
DR PRIDE; Q95242; -.
DR Ensembl; ENSSSCT00025058845; ENSSSCP00025024947; ENSSSCG00025043405.
DR Ensembl; ENSSSCT00025059067; ENSSSCP00025025044; ENSSSCG00025043405.
DR Ensembl; ENSSSCT00025059675; ENSSSCP00025025313; ENSSSCG00025043405.
DR Ensembl; ENSSSCT00040097607; ENSSSCP00040043531; ENSSSCG00040070811.
DR Ensembl; ENSSSCT00060086795; ENSSSCP00060037546; ENSSSCG00060063481.
DR Ensembl; ENSSSCT00065019120; ENSSSCP00065007819; ENSSSCG00065014331.
DR Ensembl; ENSSSCT00070009557; ENSSSCP00070007841; ENSSSCG00070005038.
DR GeneID; 396941; -.
DR KEGG; ssc:396941; -.
DR CTD; 5175; -.
DR eggNOG; ENOG502QW63; Eukaryota.
DR HOGENOM; CLU_024558_0_0_1; -.
DR InParanoid; Q95242; -.
DR OrthoDB; 419506at2759; -.
DR TreeFam; TF338229; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 12.
DR Genevisible; Q95242; SS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040878; Ig_C17orf99.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 2.
DR Pfam; PF17736; Ig_C17orf99; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..740
FT /note="Platelet endothelial cell adhesion molecule"
FT /id="PRO_0000014897"
FT TOPO_DOM 28..602
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..740
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..126
FT /note="Ig-like C2-type 1"
FT DOMAIN 145..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 236..315
FT /note="Ig-like C2-type 3"
FT DOMAIN 328..404
FT /note="Ig-like C2-type 4"
FT DOMAIN 425..494
FT /note="Ig-like C2-type 5"
FT DOMAIN 500..592
FT /note="Ig-like C2-type 6"
FT REGION 697..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..731
FT /note="Membrane-bound segment which detaches upon
FT phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT REGION 723..740
FT /note="May play a role in cytoprotective signaling"
FT /evidence="ECO:0000250"
FT MOTIF 690..695
FT /note="ITIM motif 1"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT MOTIF 713..718
FT /note="ITIM motif 2"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT COMPBIAS 715..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 692
FT /note="Phosphotyrosine; by FER"
FT /evidence="ECO:0000250|UniProtKB:P51866"
FT MOD_RES 715
FT /note="Phosphotyrosine; by FER"
FT /evidence="ECO:0000250|UniProtKB:P51866"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 256..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 347..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 432..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 524..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ 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
