PECA1_RAT
ID PECA1_RAT Reviewed; 678 AA.
AC Q3SWT0; P97635;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Platelet endothelial cell adhesion molecule;
DE Short=PECAM-1;
DE AltName: CD_antigen=CD31;
DE Flags: Precursor;
GN Name=Pecam1; Synonyms=Pecam;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 283-624.
RC STRAIN=Sprague-Dawley;
RX PubMed=10878616;
RX DOI=10.1002/1097-0177(200007)218:3<507::aid-dvdy1012>3.0.co;2-5;
RA Pepper M.S., Baetens D., Mandriota S.J., Di Sanza C., Oikemus S.,
RA Lane T.F., Soriano J.V., Montesano R., Iruela-Arispe M.L.;
RT "Regulation of VEGF and VEGF receptor expression in the rodent mammary
RT gland during pregnancy, lactation, and involution.";
RL Dev. Dyn. 218:507-524(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cell adhesion molecule which is required for leukocyte
CC transendothelial migration (TEM) under most inflammatory conditions.
CC Tyr-660 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. Interacts with FER. Interacts with CD177; the
CC interaction is Ca(2+)-dependent; the interaction is direct.
CC {ECO:0000250|UniProtKB:P16284, 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 after cellular activation.
CC In endothelial cells Fyn mediates mechanical-force (stretch or pull)
CC induced tyrosine phosphorylation. Phosphorylated on tyrosine residues
CC by FER and FES in response to FCER1 activation.
CC {ECO:0000250|UniProtKB:P16284, 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; BC104711; AAI04712.1; -; mRNA.
DR EMBL; U77697; AAB36541.1; -; mRNA.
DR RefSeq; NP_113779.1; NM_031591.1.
DR AlphaFoldDB; Q3SWT0; -.
DR SMR; Q3SWT0; -.
DR STRING; 10116.ENSRNOP00000044403; -.
DR GlyGen; Q3SWT0; 7 sites.
DR iPTMnet; Q3SWT0; -.
DR PhosphoSitePlus; Q3SWT0; -.
DR PaxDb; Q3SWT0; -.
DR PRIDE; Q3SWT0; -.
DR GeneID; 29583; -.
DR KEGG; rno:29583; -.
DR UCSC; RGD:61927; rat.
DR CTD; 5175; -.
DR RGD; 61927; Pecam1.
DR eggNOG; ENOG502QW63; Eukaryota.
DR InParanoid; Q3SWT0; -.
DR OrthoDB; 419506at2759; -.
DR PhylomeDB; Q3SWT0; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-210990; PECAM1 interactions.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-432142; Platelet sensitization by LDL.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q3SWT0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0030485; C:smooth muscle contractile fiber; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0050904; P:diapedesis; ISO:RGD.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:0001886; P:endothelial cell morphogenesis; ISO:RGD.
DR GO; GO:0090673; P:endothelial cell-matrix adhesion; ISO:RGD.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0072011; P:glomerular endothelium development; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0035696; P:monocyte extravasation; ISO:RGD.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:RGD.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:RGD.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:0072672; P:neutrophil extravasation; ISO:RGD.
DR GO; GO:0006909; P:phagocytosis; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0150107; P:positive regulation of protein localization to cell-cell junction; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..678
FT /note="Platelet endothelial cell adhesion molecule"
FT /id="PRO_0000045176"
FT TOPO_DOM 18..589
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..126
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..213
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..309
FT /note="Ig-like C2-type 3"
FT DOMAIN 315..391
FT /note="Ig-like C2-type 4"
FT DOMAIN 413..472
FT /note="Ig-like C2-type 5"
FT DOMAIN 488..577
FT /note="Ig-like C2-type 6"
FT REGION 634..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 658..663
FT /note="ITIM motif"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT MOD_RES 660
FT /note="Phosphotyrosine; by FER"
FT /evidence="ECO:0000250|UniProtKB:P51866"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 142..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 245..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 336..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 420..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 512..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 678 AA; 76189 MW; 58062E6CC3FD16E5 CRC64;
MLLALLLTML LYASLQAQEN SFTINSIHME SRPSWEVSNG QKLTLQCLVD ISTTSKSRPQ
HQVLFYKDDA LVYNVSSSEH TESFVIPQSR VFHAGKYKCT VILNSKEKTT IEYQLTVNGV
PMPEVTVDKK EVTEGGIVTV NCSMQEEKPP IYFKIEKVEL GTKNVKLSRE KTSNMNFVLI
EFPIEEQDHL LVFRCQAGVL SGIKMQTSEF IRSEYVTVQE FFSTPKFQIQ PPEMIIEGNQ
LHIKCSVQVA HLAQEFPEII IQKDKAIVAT SKQSKEAVYS VMALVEHSGH YTCKVESNRI
SKASSILVNI TELFPRPKLE LSSSRLDQGE MLDLSCSVSG APVANFTIQK EETVLSQYQN
FSKIAEERDS GLYSCTAGIG KVVKRSNLVP VQVCEMLSKP RIFHDAKFEI IKGQIIGISC
QSVNGTAPIT YRLLRAKSNF QTVQKNSNDP VTFTDKPTRD MEYQCIVDNC HSHPEVRSEI
LRVKVIAPVD EVTISILSGN DVQSGDEMVL RCSVKEGTGP VTFQFYKEKE GRPFHEETVN
DTQVFWHHEQ TSKEQEGQYY CTAFNRASIV TSLRSGPLTV RVFLAPWKKG LIAVVVIGVV
IAALIVAAKY YFLRKAKAKQ KPVEMSRPAV PLLNSNSEKV SEPSVETNSH YDSQNMDVEY
TEVEVSSLEP HQENGRLP
