PECA1_MOUSE
ID PECA1_MOUSE Reviewed; 727 AA.
AC Q08481; B1ARB1; B1ARB2; Q3TES6; Q922E0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 190.
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, Pecam-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=8516303; DOI=10.1073/pnas.90.12.5569;
RA Xie Y., Muller W.A.;
RT "Molecular cloning and adhesive properties of murine platelet/endothelial
RT cell adhesion molecule 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5569-5573(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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 [6]
RP PROTEIN SEQUENCE OF 18-26.
RC TISSUE=Heart;
RX PubMed=1415479;
RA Bogen S.A., Baldwin H.S., Watkins S.C., Albelda S.M., Abbas A.K.;
RT "Association of murine CD31 with transmigrating lymphocytes following
RT antigenic stimulation.";
RL Am. J. Pathol. 141:843-854(1992).
RN [7]
RP PHOSPHORYLATION AT TYR-679 AND TYR-702 BY FES AND FER, AND MUTAGENESIS OF
RP TYR-679; TYR-702 AND TYR-717.
RX PubMed=16731527; DOI=10.1074/jbc.m604252200;
RA Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.;
RT "Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to
RT platelet-endothelial cell adhesion molecule 1 to limit mast cell
RT activation.";
RL J. Biol. Chem. 281:20949-20957(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-702, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19048083; DOI=10.1242/dmm.000547;
RA Stevens H.Y., Melchior B., Bell K.S., Yun S., Yeh J.C., Frangos J.A.;
RT "PECAM-1 is a critical mediator of atherosclerosis.";
RL Dis. Model. Mech. 1:175-181(2008).
RN [10]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
RX PubMed=18388311; DOI=10.1242/jcs.025163;
RA Bergom C., Paddock C., Gao C., Holyst T., Newman D.K., Newman P.J.;
RT "An alternatively spliced isoform of PECAM-1 is expressed at high levels in
RT human and murine tissues, and suggests a novel role for the C-terminus of
RT PECAM-1 in cytoprotective signaling.";
RL J. Cell Sci. 121:1235-1242(2008).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-141; ASN-360; ASN-424
RP AND ASN-540.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cell adhesion molecule which is required for leukocyte
CC transendothelial migration (TEM) under most inflammatory conditions (By
CC similarity). Tyr-679 plays a critical role in TEM and is required for
CC efficient trafficking of PECAM1 to and from the lateral border
CC recycling compartment (LBRC) and is also essential for the LBRC
CC membrane to be targeted around migrating leukocytes (By similarity).
CC Trans-homophilic interaction may play a role in endothelial cell-cell
CC adhesion via cell junctions (By similarity). Heterophilic interaction
CC with CD177 plays a role in transendothelial migration of neutrophils
CC (By similarity). Homophilic ligation of PECAM1 prevents macrophage-
CC mediated phagocytosis of neighboring viable leukocytes by transmitting
CC a detachment signal (By similarity). 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 (By similarity). Modulates bradykinin
CC receptor BDKRB2 activation (By similarity). Regulates bradykinin- and
CC hyperosmotic shock-induced ERK1/2 activation in endothelial cells (By
CC similarity). Induces susceptibility to atherosclerosis
CC (PubMed:19048083). {ECO:0000250|UniProtKB:P16284,
CC ECO:0000269|PubMed:19048083}.
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-702 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q08481-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08481-2; Sequence=VSP_038724;
CC Name=3;
CC IsoId=Q08481-3; Sequence=VSP_038725;
CC Name=4;
CC IsoId=Q08481-4; Sequence=VSP_038723;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in lung and
CC platelets. {ECO:0000269|PubMed:18388311}.
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 (PubMed:16731527). Upon activation, phosphorylated
CC on Ser-718 which probably initiates the dissociation of the membrane-
CC interaction segment (residues 698-718) from the cell membrane allowing
CC the sequential phosphorylation of Tyr-702 and Tyr-679 (By similarity).
CC Constitutively phosphorylated on Ser-723 in resting platelets (By
CC similarity). Phosphorylated on tyrosine residues by FER and FES in
CC response to FCER1 activation (PubMed:16731527). In endothelial cells
CC Fyn mediates mechanical-force (stretch or pull) induced tyrosine
CC phosphorylation (By similarity). {ECO:0000250|UniProtKB:P16284,
CC ECO:0000269|PubMed:16731527}.
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}.
CC -!- DISRUPTION PHENOTYPE: Mice show reduced atherosclerotic lesions. There
CC is down-regulation of ICAM-1 in endothelial cells at the lesion
CC periphery, and reduced disruption of Cx43 junctional staining at
CC arterial branch points and in the descending aorta.
CC {ECO:0000269|PubMed:19048083}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=PECAM-1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_191";
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DR EMBL; L06039; AAA16230.1; -; mRNA.
DR EMBL; AK169431; BAE41172.1; -; mRNA.
DR EMBL; AL603664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34303.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34304.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34305.1; -; Genomic_DNA.
DR EMBL; BC008519; AAH08519.1; -; mRNA.
DR EMBL; BC085502; AAH85502.1; -; mRNA.
DR CCDS; CCDS25558.1; -. [Q08481-2]
DR CCDS; CCDS25559.1; -. [Q08481-3]
DR CCDS; CCDS79068.1; -. [Q08481-4]
DR CCDS; CCDS79069.1; -. [Q08481-1]
DR RefSeq; NP_001027550.1; NM_001032378.2. [Q08481-2]
DR RefSeq; NP_001292086.1; NM_001305157.1. [Q08481-1]
DR RefSeq; NP_001292087.1; NM_001305158.1. [Q08481-4]
DR RefSeq; NP_032842.2; NM_008816.3. [Q08481-3]
DR RefSeq; XP_011247094.1; XM_011248792.1.
DR AlphaFoldDB; Q08481; -.
DR BioGRID; 202105; 4.
DR IntAct; Q08481; 4.
DR STRING; 10090.ENSMUSP00000079664; -.
DR GlyGen; Q08481; 7 sites.
DR iPTMnet; Q08481; -.
DR PhosphoSitePlus; Q08481; -.
DR SwissPalm; Q08481; -.
DR EPD; Q08481; -.
DR jPOST; Q08481; -.
DR MaxQB; Q08481; -.
DR PaxDb; Q08481; -.
DR PeptideAtlas; Q08481; -.
DR PRIDE; Q08481; -.
DR ProteomicsDB; 288120; -. [Q08481-1]
DR ProteomicsDB; 288121; -. [Q08481-2]
DR ProteomicsDB; 288122; -. [Q08481-3]
DR ProteomicsDB; 288123; -. [Q08481-4]
DR ABCD; Q08481; 44 sequenced antibodies.
DR Antibodypedia; 58161; 3970 antibodies from 45 providers.
DR DNASU; 18613; -.
DR Ensembl; ENSMUST00000080853; ENSMUSP00000079664; ENSMUSG00000020717. [Q08481-3]
DR Ensembl; ENSMUST00000103069; ENSMUSP00000099358; ENSMUSG00000020717. [Q08481-2]
DR Ensembl; ENSMUST00000106796; ENSMUSP00000102408; ENSMUSG00000020717. [Q08481-1]
DR Ensembl; ENSMUST00000183610; ENSMUSP00000138959; ENSMUSG00000020717. [Q08481-4]
DR GeneID; 18613; -.
DR KEGG; mmu:18613; -.
DR UCSC; uc007lze.2; mouse. [Q08481-1]
DR UCSC; uc007lzf.2; mouse. [Q08481-3]
DR UCSC; uc007lzg.2; mouse. [Q08481-2]
DR UCSC; uc007lzh.2; mouse. [Q08481-4]
DR CTD; 5175; -.
DR MGI; MGI:97537; Pecam1.
DR VEuPathDB; HostDB:ENSMUSG00000020717; -.
DR eggNOG; ENOG502QW63; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_024558_0_0_1; -.
DR InParanoid; Q08481; -.
DR OrthoDB; 419506at2759; -.
DR TreeFam; TF338229; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-210990; PECAM1 interactions.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 18613; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Pecam1; mouse.
DR PRO; PR:Q08481; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q08481; protein.
DR Bgee; ENSMUSG00000020717; Expressed in right lung lobe and 174 other tissues.
DR ExpressionAtlas; Q08481; baseline and differential.
DR Genevisible; Q08481; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0030485; C:smooth muscle contractile fiber; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:MGI.
DR GO; GO:0050904; P:diapedesis; ISO:MGI.
DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR GO; GO:0090673; P:endothelial cell-matrix adhesion; IMP:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0035696; P:monocyte extravasation; ISO:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0072672; P:neutrophil extravasation; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0150107; P:positive regulation of protein localization to cell-cell junction; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
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; IPR040878; Ig_C17orf99.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF17736; Ig_C17orf99; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:1415479"
FT CHAIN 18..727
FT /note="Platelet endothelial cell adhesion molecule"
FT /id="PRO_0000014896"
FT TOPO_DOM 18..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..727
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..578
FT /note="Ig-like C2-type 6"
FT REGION 642..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..718
FT /note="Membrane-bound segment which detaches upon
FT phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT REGION 710..727
FT /note="May play a role in cytoprotective signaling"
FT /evidence="ECO:0000250"
FT MOTIF 677..682
FT /note="ITIM motif 1"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT MOTIF 700..705
FT /note="ITIM motif 2"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT MOD_RES 679
FT /note="Phosphotyrosine; by FER"
FT /evidence="ECO:0000305|PubMed:16731527"
FT MOD_RES 702
FT /note="Phosphotyrosine; by FER"
FT /evidence="ECO:0000269|PubMed:16731527,
FT ECO:0007744|PubMed:17947660"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16284"
FT LIPID 611
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
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:0000269|PubMed:19349973"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
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"
FT VAR_SEQ 119..219
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038723"
FT VAR_SEQ 692..727
FT /note="ALGTRATETVYSEIRKVDPNLMENRYSRTEGSLNGT -> ENGRLP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038724"
FT VAR_SEQ 711..727
FT /note="NLMENRYSRTEGSLNGT -> KNGRLP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038725"
FT MUTAGEN 679
FT /note="Y->F: Reduces tyrosine phosphorylation by FER by
FT about 60%."
FT /evidence="ECO:0000269|PubMed:16731527"
FT MUTAGEN 702
FT /note="Y->F: Reduces tyrosine phosphorylation by FER by
FT about 60%."
FT /evidence="ECO:0000269|PubMed:16731527"
FT MUTAGEN 717
FT /note="Y->F: No significant effect on phosphorylation by
FT FER."
FT /evidence="ECO:0000269|PubMed:16731527"
FT CONFLICT 18
FT /note="E -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 81263 MW; 34C04752D199BAA5 CRC64;
MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD ISTTSKSRSQ
HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT VMLNNKEKTT IEYEVKVHGV
SKPKVTLDKK EVTEGGVVTV NCSLQEEKPP IFFKIEKLEV GTKFVKRRID KTSNENFVLM
EFPIEAQDHV LVFRCQAGIL SGFKLQESEP IRSEYVTVQE SFSTPKFEIK PPGMIIEGDQ
LHIRCIVQVT HLVQEFTEII IQKDKAIVAT SKQSSEAVYS VMAMVEYSGH YTCKVESNRI
SKASSIMVNI TELFPKPKLE FSSSRLDQGE LLDLSCSVSG TPVANFTIQK EETVLSQYQN
FSKIAEESDS GEYSCTAGIG KVVKRSGLVP IQVCEMLSKP SIFHDAKSEI IKGHAIGISC
QSENGTAPIT YHLMKAKSDF QTLEVTSNDP ATFTDKPTRD MEYQCRADNC HSHPAVFSEI
LRVRVIAPVD EVVISILSSN EVQSGSEMVL RCSVKEGTSP ITFQFYKEKE DRPFHQAVVN
DTQAFWHNKQ ASKKQEGQYY CTASNRASSM RTSPRSSTLA VRVFLAPWKK GLIAVVVIGV
VIATLIVAAK CYFLRKAKAK QKPVEMSRPA APLLNSNSEK ISEPSVEANS HYGYDDVSGN
DAVKPINQNK DPQNMDVEYT EVEVSSLEPH QALGTRATET VYSEIRKVDP NLMENRYSRT
EGSLNGT
