ID PECA1_HUMAN Reviewed; 738 AA.
AC P16284; A0A075B738; A8K3S7; D3DU31; Q6LDA9; Q8TBH1; Q96RF5; Q96RF6; Q9NP65;
AC Q9NPB7; Q9NPG9; Q9NQS9; Q9NQT0; Q9NQT1; Q9NQT2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 27-MAR-2024, entry version 242.
DE RecName: Full=Platelet endothelial cell adhesion molecule;
DE Short=PECAM-1;
DE AltName: Full=EndoCAM;
DE AltName: Full=GPIIA';
DE AltName: Full=PECA1;
DE AltName: CD_antigen=CD31;
DE Flags: Precursor;
GN Name=PECAM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=2351935; DOI=10.1084/jem.171.6.2147;
RA Simmons D.L., Walker C., Power C., Pigott R.;
RT "Molecular cloning of CD31, a putative intercellular adhesion molecule
RT closely related to carcinoembryonic antigen.";
RL J. Exp. Med. 171:2147-2152(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANTS ASN-563 AND
RP GLY-670.
RX PubMed=1700999;
RA Stockinger H., Gadd S.J., Eher R., Majdic O., Kasinrek W., Schreiber W.,
RA Strass B., Schnabl E., Knapp W.;
RT "Molecular characterization and functional analysis of the leukocyte
RT surface protein CD31.";
RL J. Immunol. 145:3889-3897(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT LEU-125.
RX PubMed=1690453; DOI=10.1126/science.1690453;
RA Newman P.J., Berndt M.C., Gorski J., White J.C. II, Lyman S., Paddock C.,
RA Muller W.A.;
RT "PECAM-1 (CD31) cloning and relation to adhesion molecules of the
RT immunoglobulin gene superfamily.";
RL Science 247:1219-1222(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=1874786; DOI=10.1083/jcb.114.5.1059;
RA Albelda S.M., Muller W.A., Buck C.A., Newman P.J.;
RT "Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel
RT vascular cell-cell adhesion molecule.";
RL J. Cell Biol. 114:1059-1068(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), AND VARIANT ASN-563.
RX PubMed=7994021;
RA Kirschbaum N.E., Gumina R.J., Newman P.J.;
RT "Organization of the gene for human platelet/endothelial cell adhesion
RT molecule-1 shows alternatively spliced isoforms and a functionally complex
RT cytoplasmic domain.";
RL Blood 84:4028-4037(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANTS ASN-563 AND
RP GLY-670.
RA Wang R.-Y., Lun Y.-Z., Jiang Z.-X., Li X.;
RT "Gene cloning and sequence analysis of human nasopharyngeal carcinoma
RT resistance cells CNE1/R platelet/endothelial cell adhesion molecule.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANTS ASN-563
RP AND GLY-670.
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ASN-563 AND
RP GLY-670.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANTS ASN-563
RP AND GLY-670.
RC TISSUE=Brain;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-734 (ISOFORM LONG), AND VARIANTS LEU-125;
RP ASN-563 AND GLY-670.
RX PubMed=17212705; DOI=10.1111/j.1399-0039.2006.00722.x;
RA Robbins F.-M., Hartzman R.J.;
RT "CD31/PECAM-1 genotyping and haplotype analyses show population
RT diversity.";
RL Tissue Antigens 69:28-37(2007).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 507-584.
RX PubMed=8226797; DOI=10.1016/s0021-9258(18)41609-2;
RA Tang D.G., Chen Y.Q., Newman P.J., Shi L., Gao X., Diglio C.A., Honn K.V.;
RT "Identification of PECAM-1 in solid tumor cells and its potential
RT involvement in tumor cell adhesion to endothelium.";
RL J. Biol. Chem. 268:22883-22894(1993).
RN [13]
RP PHOSPHORYLATION AT TYR-713.
RX PubMed=9298995; DOI=10.1083/jcb.138.6.1425;
RA Famiglietti J., Sun J., DeLisser H.M., Albelda S.M.;
RT "Tyrosine residue in exon 14 of the cytoplasmic domain of platelet
RT endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligand
RT binding specificity.";
RL J. Cell Biol. 138:1425-1435(1997).
RN [14]
RP FUNCTION.
RX PubMed=12110892; DOI=10.1038/nature00811;
RA Brown S., Heinisch I., Ross E., Shaw K., Buckley C.D., Savill J.;
RT "Apoptosis disables CD31-mediated cell detachment from phagocytes promoting
RT binding and engulfment.";
RL Nature 418:200-203(2002).
RN [15]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=12433657; DOI=10.1152/ajpheart.00600.2002;
RA Wang Y., Su X., Sorenson C.M., Sheibani N.;
RT "Tissue-specific distributions of alternatively spliced human PECAM-1
RT isoforms.";
RL Am. J. Physiol. 284:H1008-H1017(2003).
RN [16]
RP PALMITOYLATION AT CYS-622, MUTAGENESIS OF CYS-622, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17139370; DOI=10.1160/th06-08-0459;
RA Sardjono C.T., Harbour S.N., Yip J.C., Paddock C., Tridandapani S.,
RA Newman P.J., Jackson D.E.;
RT "Palmitoylation at Cys595 is essential for PECAM-1 localisation into
RT membrane microdomains and for efficient PECAM-1-mediated cytoprotection.";
RL Thromb. Haemost. 96:756-766(2006).
RN [17]
RP FUNCTION, INTERACTION WITH CD177, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17580308; DOI=10.1074/jbc.m701120200;
RA Sachs U.J., Andrei-Selmer C.L., Maniar A., Weiss T., Paddock C.,
RA Orlova V.V., Choi E.Y., Newman P.J., Preissner K.T., Chavakis T.,
RA Santoso S.;
RT "The neutrophil-specific antigen CD177 is a counter-receptor for platelet
RT endothelial cell adhesion molecule-1 (CD31).";
RL J. Biol. Chem. 282:23603-23612(2007).
RN [18]
RP FUNCTION, AND INTERACTION WITH BDKRB2 AND GNAQ.
RX PubMed=18672896; DOI=10.1021/bi8003846;
RA Yeh J.C., Otte L.A., Frangos J.A.;
RT "Regulation of G protein-coupled receptor activities by the platelet-
RT endothelial cell adhesion molecule, PECAM-1.";
RL Biochemistry 47:9029-9039(2008).
RN [19]
RP PHOSPHORYLATION.
RX PubMed=18710921; DOI=10.1083/jcb.200801062;
RA Chiu Y.J., McBeath E., Fujiwara K.;
RT "Mechanotransduction in an extracted cell model: Fyn drives stretch- and
RT flow-elicited PECAM-1 phosphorylation.";
RL J. Cell Biol. 182:753-763(2008).
RN [20]
RP ALTERNATIVE SPLICING (ISOFORMS DELTA14-15 AND DELTA15), FUNCTION (ISOFORM
RP DELTA15), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-690
RP AND TYR-713, AND INTERACTION WITH PTPN11.
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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT
RP TYR-690 AND TYR-713, MUTAGENESIS OF LYS-89; TYR-690 AND TYR-713, AND
RP INTERACTION WITH PTPN11.
RX PubMed=19342684; DOI=10.4049/jimmunol.0803192;
RA Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.;
RT "A novel and critical role for tyrosine 663 in platelet endothelial cell
RT adhesion molecule-1 trafficking and transendothelial migration.";
RL J. Immunol. 182:5041-5051(2009).
RN [23]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151; ASN-320 AND ASN-453.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-320 AND ASN-551.
RC TISSUE=Leukemic T-cell;
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 [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [26]
RP PALMITOYLATION BY ZDHHC21, AND SUBCELLULAR LOCATION.
RX PubMed=22496122; DOI=10.1161/circresaha.112.269514;
RA Marin E.P., Derakhshan B., Lam T.T., Davalos A., Sessa W.C.;
RT "Endothelial cell palmitoylproteomic identifies novel lipid-modified
RT targets and potential substrates for protein acyl transferases.";
RL Circ. Res. 110:1336-1344(2012).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP STRUCTURE BY NMR OF 686-738, TISSUE SPECIFICITY, MOTIF, PHOSPHORYLATION AT
RP TYR-690; TYR-713; SER-729 AND SER-734, AND MUTAGENESIS OF TYR-690 AND
RP TYR-713.
RX PubMed=21464369; DOI=10.1182/blood-2010-11-317867;
RA Paddock C., Lytle B.L., Peterson F.C., Holyst T., Newman P.J.,
RA Volkman B.F., Newman D.K.;
RT "Residues within a lipid-associated segment of the PECAM-1 cytoplasmic
RT domain are susceptible to inducible, sequential phosphorylation.";
RL Blood 117:6012-6023(2011).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 28-229, SUBUNIT, GLYCOSYLATION AT
RP ASN-52; ASN-84 AND ASN-151, AND DISULFIDE BONDS.
RX PubMed=26702061; DOI=10.1182/blood-2015-07-660092;
RA Paddock C., Zhou D., Lertkiatmongkol P., Newman P.J., Zhu J.;
RT "Structural basis for PECAM-1 homophilic binding.";
RL Blood 127:1052-1061(2016).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 28-232, FUNCTION, SUBUNIT,
RP DISULFIDE BONDS, AND MUTAGENESIS OF ASN-52; LEU-74; ASN-84; ILE-112;
RP ASN-151; PHE-188 AND ILE-190.
RX PubMed=27958302; DOI=10.1038/srep38655;
RA Hu M., Zhang H., Liu Q., Hao Q.;
RT "Structural basis for human PECAM-1-mediated trans-homophilic cell
RT adhesion.";
RL Sci. Rep. 6:38655-38655(2016).
RN [32]
RP VARIANT LEU-125.
RX PubMed=8532023; DOI=10.1056/nejm199602013340502;
RA Behar E., Chao N.J., Hiraki D.D., Krishnaswamy S., Brown B.W.,
RA Zehnder J.L., Grumet F.C.;
RT "Polymorphism of adhesion molecule CD31 and its role in acute graft-versus-
RT host disease.";
RL N. Engl. J. Med. 334:286-291(1996).
RN [33]
RP VARIANT LEU-125.
RX PubMed=11791967; DOI=10.4269/ajtmh.2001.65.736;
RA Casals-Pascual C., Allen S., Allen A., Kai O., Lowe B., Pain A.,
RA Roberts D.J.;
RT "Codon 125 polymorphism of CD31 and susceptibility to malaria.";
RL Am. J. Trop. Med. Hyg. 65:736-737(2001).
CC -!- FUNCTION: Cell adhesion molecule which is required for leukocyte
CC transendothelial migration (TEM) under most inflammatory conditions
CC (PubMed:19342684, PubMed:17580308). Tyr-690 plays a critical role in
CC TEM and is required for efficient trafficking of PECAM1 to and from the
CC lateral border recycling compartment (LBRC) and is also essential for
CC the LBRC membrane to be targeted around migrating leukocytes
CC (PubMed:19342684). Trans-homophilic interaction may play a role in
CC endothelial cell-cell adhesion via cell junctions (PubMed:27958302).
CC Heterophilic interaction with CD177 plays a role in transendothelial
CC migration of neutrophils (PubMed:17580308). Homophilic ligation of
CC PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable
CC leukocytes by transmitting a detachment signal (PubMed:12110892).
CC Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by
CC tethering them to the phagocytic cells; PECAM1-mediated detachment
CC signal appears to be disabled in apoptotic leukocytes
CC (PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation
CC (PubMed:18672896). Regulates bradykinin- and hyperosmotic shock-induced
CC ERK1/2 activation in endothelial cells (PubMed:18672896). Induces
CC susceptibility to atherosclerosis (By similarity).
CC {ECO:0000250|UniProtKB:Q08481, ECO:0000269|PubMed:12110892,
CC ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18672896,
CC ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:27958302}.
CC -!- FUNCTION: [Isoform Delta15]: Does not protect against apoptosis.
CC {ECO:0000269|PubMed:18388311}.
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 (PubMed:26702061, PubMed:27958302). Forms a complex with BDKRB2 and
CC GNAQ (PubMed:18672896). Interacts with BDKRB2 and GNAQ
CC (PubMed:18672896).Interacts with PTPN11; Tyr-713 is critical for PTPN11
CC recruitment (PubMed:18388311, PubMed:19342684). Interacts with FER (By
CC similarity). Interacts (via Ig-like C2-type domain 6) with CD177; the
CC interaction is Ca(2+)-dependent; the interaction is direct
CC (PubMed:17580308). {ECO:0000250|UniProtKB:P51866,
CC ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18388311,
CC ECO:0000269|PubMed:18672896, ECO:0000269|PubMed:19342684,
CC ECO:0000269|PubMed:26702061, ECO:0000269|PubMed:27958302}.
CC -!- INTERACTION:
CC P16284; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-716404, EBI-18899653;
CC P16284; Q8N302-2: AGGF1; NbExp=3; IntAct=EBI-716404, EBI-25838028;
CC P16284; P54819: AK2; NbExp=3; IntAct=EBI-716404, EBI-1056291;
CC P16284; P61966-2: AP1S1; NbExp=3; IntAct=EBI-716404, EBI-12067760;
CC P16284; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-716404, EBI-10254793;
CC P16284; Q9UMX3: BOK; NbExp=3; IntAct=EBI-716404, EBI-7105206;
CC P16284; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-716404, EBI-10178113;
CC P16284; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-716404, EBI-747505;
CC P16284; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-716404, EBI-1383687;
CC P16284; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-716404, EBI-744556;
CC P16284; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-716404, EBI-744045;
CC P16284; O75175: CNOT3; NbExp=3; IntAct=EBI-716404, EBI-743073;
CC P16284; Q9NX09: DDIT4; NbExp=3; IntAct=EBI-716404, EBI-715104;
CC P16284; P49184: DNASE1L1; NbExp=3; IntAct=EBI-716404, EBI-20894690;
CC P16284; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-716404, EBI-25847826;
CC P16284; Q99944: EGFL8; NbExp=3; IntAct=EBI-716404, EBI-3924130;
CC P16284; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-716404, EBI-10213520;
CC P16284; Q99504: EYA3; NbExp=3; IntAct=EBI-716404, EBI-9089567;
CC P16284; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-716404, EBI-11793142;
CC P16284; O15287: FANCG; NbExp=3; IntAct=EBI-716404, EBI-81610;
CC P16284; P14136: GFAP; NbExp=3; IntAct=EBI-716404, EBI-744302;
CC P16284; Q4G1C9-2: GLIPR1L2; NbExp=3; IntAct=EBI-716404, EBI-20835942;
CC P16284; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-716404, EBI-3957665;
CC P16284; O75874: IDH1; NbExp=3; IntAct=EBI-716404, EBI-715695;
CC P16284; Q0VD86: INCA1; NbExp=3; IntAct=EBI-716404, EBI-6509505;
CC P16284; P14923: JUP; NbExp=7; IntAct=EBI-716404, EBI-702484;
CC P16284; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-716404, EBI-739493;
CC P16284; Q96E93: KLRG1; NbExp=3; IntAct=EBI-716404, EBI-750770;
CC P16284; Q6IAA8: LAMTOR1; NbExp=3; IntAct=EBI-716404, EBI-715385;
CC P16284; Q14847-2: LASP1; NbExp=3; IntAct=EBI-716404, EBI-9088686;
CC P16284; P09382: LGALS1; NbExp=4; IntAct=EBI-716404, EBI-1048875;
CC P16284; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-716404, EBI-25830459;
CC P16284; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-716404, EBI-10182361;
CC P16284; Q14728: MFSD10; NbExp=3; IntAct=EBI-716404, EBI-11337904;
CC P16284; Q13405: MRPL49; NbExp=3; IntAct=EBI-716404, EBI-5325200;
CC P16284; I6L9F6: NEFL; NbExp=3; IntAct=EBI-716404, EBI-10178578;
CC P16284; Q9GZQ6: NPFFR1; NbExp=3; IntAct=EBI-716404, EBI-18212103;
CC P16284; Q9HB63: NTN4; NbExp=3; IntAct=EBI-716404, EBI-743459;
CC P16284; Q9P286: PAK5; NbExp=3; IntAct=EBI-716404, EBI-741896;
CC P16284; Q16549: PCSK7; NbExp=3; IntAct=EBI-716404, EBI-8059854;
CC P16284; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-716404, EBI-18063495;
CC P16284; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-716404, EBI-10171633;
CC P16284; Q8NBT0: POC1A; NbExp=3; IntAct=EBI-716404, EBI-2557132;
CC P16284; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-716404, EBI-743880;
CC P16284; Q06124: PTPN11; NbExp=7; IntAct=EBI-716404, EBI-297779;
CC P16284; P29350: PTPN6; NbExp=4; IntAct=EBI-716404, EBI-78260;
CC P16284; Q96I25: RBM17; NbExp=3; IntAct=EBI-716404, EBI-740272;
CC P16284; Q9UJD0: RIMS3; NbExp=3; IntAct=EBI-716404, EBI-3909436;
CC P16284; P61513: RPL37A; NbExp=3; IntAct=EBI-716404, EBI-356793;
CC P16284; Q8NC51: SERBP1; NbExp=3; IntAct=EBI-716404, EBI-523558;
CC P16284; P12757: SKIL; NbExp=3; IntAct=EBI-716404, EBI-2902468;
CC P16284; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-716404, EBI-21504521;
CC P16284; Q12824: SMARCB1; NbExp=3; IntAct=EBI-716404, EBI-358419;
CC P16284; Q7Z614-3: SNX20; NbExp=3; IntAct=EBI-716404, EBI-12336127;
CC P16284; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-716404, EBI-2510414;
CC P16284; Q08AE8: SPIRE1; NbExp=3; IntAct=EBI-716404, EBI-1055655;
CC P16284; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-716404, EBI-2659201;
CC P16284; Q99619: SPSB2; NbExp=3; IntAct=EBI-716404, EBI-2323209;
CC P16284; P12931: SRC; NbExp=3; IntAct=EBI-716404, EBI-621482;
CC P16284; P46977: STT3A; NbExp=3; IntAct=EBI-716404, EBI-719212;
CC P16284; Q9H7C4: SYNC; NbExp=3; IntAct=EBI-716404, EBI-11285923;
CC P16284; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-716404, EBI-11123832;
CC P16284; O15273: TCAP; NbExp=3; IntAct=EBI-716404, EBI-954089;
CC P16284; P15923-3: TCF3; NbExp=3; IntAct=EBI-716404, EBI-12000326;
CC P16284; Q13428-5: TCOF1; NbExp=3; IntAct=EBI-716404, EBI-25832010;
CC P16284; Q5T1C6: THEM4; NbExp=3; IntAct=EBI-716404, EBI-7684443;
CC P16284; Q7Z403: TMC6; NbExp=3; IntAct=EBI-716404, EBI-9088037;
CC P16284; Q96JJ7-2: TMX3; NbExp=3; IntAct=EBI-716404, EBI-25833898;
CC P16284; Q12888: TP53BP1; NbExp=3; IntAct=EBI-716404, EBI-396540;
CC P16284; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-716404, EBI-9088812;
CC P16284; Q08AM6: VAC14; NbExp=3; IntAct=EBI-716404, EBI-2107455;
CC P16284; Q9H270: VPS11; NbExp=3; IntAct=EBI-716404, EBI-373380;
CC P16284; Q5JSH3: WDR44; NbExp=3; IntAct=EBI-716404, EBI-3441235;
CC P16284; P19544-6: WT1; NbExp=3; IntAct=EBI-716404, EBI-11745701;
CC P16284; Q6ZSB9: ZBTB49; NbExp=3; IntAct=EBI-716404, EBI-2859943;
CC P16284; P26651: ZFP36; NbExp=3; IntAct=EBI-716404, EBI-374248;
CC P16284; P17024: ZNF20; NbExp=3; IntAct=EBI-716404, EBI-717634;
CC P16284; Q9BQ29; NbExp=3; IntAct=EBI-716404, EBI-22013570;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17580308};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Cell surface
CC expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-
CC mediated stimulation. {ECO:0000269|PubMed:17580308}.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane
CC {ECO:0000269|PubMed:18388311, ECO:0000269|PubMed:19342684}; Single-pass
CC type I membrane protein {ECO:0000305|PubMed:18388311}. Membrane raft
CC {ECO:0000269|PubMed:17139370, ECO:0000269|PubMed:22496122}. Cell
CC junction {ECO:0000269|PubMed:18388311}. Note=Localizes to the lateral
CC border recycling compartment (LBRC) and recycles from the LBRC to the
CC junction in resting endothelial cells. {ECO:0000269|PubMed:19342684}.
CC -!- SUBCELLULAR LOCATION: [Isoform Delta15]: Cell junction
CC {ECO:0000269|PubMed:18388311}. Note=Localizes to the lateral border
CC recycling compartment (LBRC) and recycles from the LBRC to the junction
CC in resting endothelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=Long;
CC IsoId=P16284-1; Sequence=Displayed;
CC Name=Delta12;
CC IsoId=P16284-2; Sequence=VSP_011806;
CC Name=Delta13;
CC IsoId=P16284-3; Sequence=VSP_011807;
CC Name=Delta14;
CC IsoId=P16284-4; Sequence=VSP_011809;
CC Name=Delta14-15;
CC IsoId=P16284-5; Sequence=VSP_011808, VSP_011811;
CC Name=Delta15;
CC IsoId=P16284-6; Sequence=VSP_011810, VSP_011811;
CC -!- TISSUE SPECIFICITY: Expressed on platelets and leukocytes and is
CC primarily concentrated at the borders between endothelial cells
CC (PubMed:18388311, PubMed:21464369). Expressed in human umbilical vein
CC endothelial cells (HUVECs) (at protein level) (PubMed:19342684,
CC PubMed:17580308). Expressed on neutrophils (at protein level)
CC (PubMed:17580308). Isoform Long predominates in all tissues examined
CC (PubMed:12433657). Isoform Delta12 is detected only in trachea
CC (PubMed:12433657). Isoform Delta14-15 is only detected in lung
CC (PubMed:12433657). Isoform Delta14 is detected in all tissues examined
CC with the strongest expression in heart (PubMed:12433657). Isoform
CC Delta15 is expressed in brain, testis, ovary, cell surface of
CC platelets, human umbilical vein endothelial cells (HUVECs), Jurkat T-
CC cell leukemia, human erythroleukemia (HEL) and U-937 histiocytic
CC lymphoma cell lines (at protein level) (PubMed:12433657,
CC PubMed:18388311). {ECO:0000269|PubMed:12433657,
CC ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18388311,
CC ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:21464369}.
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 -!- PTM: Phosphorylated on Ser and Tyr residues after cellular activation
CC by src kinases (PubMed:21464369, PubMed:9298995, PubMed:19342684,
CC PubMed:18710921). Upon activation, phosphorylated on Ser-729 which
CC probably initiates the dissociation of the membrane-interaction segment
CC (residues 709-729) from the cell membrane allowing the sequential
CC phosphorylation of Tyr-713 and Tyr-690 (PubMed:21464369).
CC Constitutively phosphorylated on Ser-734 in resting platelets
CC (PubMed:21464369). Phosphorylated on tyrosine residues by FER and FES
CC in response to FCER1 activation (By similarity). In endothelial cells
CC Fyn mediates mechanical-force (stretch or pull) induced tyrosine
CC phosphorylation (PubMed:18710921). {ECO:0000250|UniProtKB:Q08481,
CC ECO:0000269|PubMed:18710921, ECO:0000269|PubMed:19342684,
CC ECO:0000269|PubMed:21464369, ECO:0000269|PubMed:9298995}.
CC -!- PTM: Palmitoylation by ZDHHC21 is necessary for cell surface expression
CC in endothelial cells and enrichment in membrane rafts.
CC {ECO:0000269|PubMed:17139370, ECO:0000269|PubMed:22496122}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD31 entry;
CC URL="https://en.wikipedia.org/wiki/CD31";
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_hum_Itlect_265";
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DR EMBL; M37780; AAA36186.1; -; mRNA.
DR EMBL; M28526; AAA36429.1; -; mRNA.
DR EMBL; L34657; AAA60057.1; -; Genomic_DNA.
DR EMBL; L34631; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34637; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34638; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34639; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34640; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34641; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34642; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34644; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34645; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34649; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; L34655; AAA60057.1; JOINED; Genomic_DNA.
DR EMBL; JQ287500; AFA36630.1; -; mRNA.
DR EMBL; AK290692; BAF83381.1; -; mRNA.
DR EMBL; AC016489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC234063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94207.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94208.1; -; Genomic_DNA.
DR EMBL; BC022512; AAH22512.1; -; mRNA.
DR EMBL; BC051822; AAH51822.1; -; mRNA.
DR EMBL; AF281287; AAF91446.1; -; mRNA.
DR EMBL; AF281288; AAF91447.1; -; mRNA.
DR EMBL; AF281289; AAF91448.1; -; mRNA.
DR EMBL; AF281290; AAF91449.1; -; mRNA.
DR EMBL; AF281291; AAF91450.1; -; mRNA.
DR EMBL; AF281292; AAF91451.1; -; mRNA.
DR EMBL; AF281293; AAF91452.1; -; mRNA.
DR EMBL; AF281294; AAF91453.1; -; mRNA.
DR EMBL; AF281295; AAF91454.1; -; mRNA.
DR EMBL; AF281296; AAF91455.1; -; mRNA.
DR EMBL; AF281297; AAF91456.1; -; mRNA.
DR EMBL; AF281298; AAF91457.1; -; mRNA.
DR EMBL; AF281299; AAF91458.1; -; mRNA.
DR EMBL; AF281300; AAF91459.1; -; mRNA.
DR EMBL; AF281301; AAF91460.1; -; mRNA.
DR EMBL; AF393676; AAK84009.1; -; mRNA.
DR EMBL; AF393677; AAK84010.1; -; mRNA.
DR EMBL; AF393678; AAK84011.1; -; mRNA.
DR EMBL; S66450; AAB28645.1; -; mRNA.
DR CCDS; CCDS74132.1; -. [P16284-1]
DR PIR; A40096; A40096.
DR RefSeq; NP_000433.4; NM_000442.4. [P16284-1]
DR RefSeq; XP_005276937.1; XM_005276880.1. [P16284-6]
DR RefSeq; XP_005276938.1; XM_005276881.1. [P16284-4]
DR RefSeq; XP_005276939.1; XM_005276882.1. [P16284-3]
DR RefSeq; XP_011523191.1; XM_011524889.2.
DR RefSeq; XP_011523192.1; XM_011524890.1.
DR RefSeq; XP_016880227.1; XM_017024738.1.
DR RefSeq; XP_016880228.1; XM_017024739.1. [P16284-2]
DR RefSeq; XP_016880229.1; XM_017024740.1.
DR PDB; 2KY5; NMR; -; A=686-738.
DR PDB; 5C14; X-ray; 2.80 A; A/B=28-229.
DR PDB; 5GNI; X-ray; 3.01 A; A/B=28-232.
DR PDBsum; 2KY5; -.
DR PDBsum; 5C14; -.
DR PDBsum; 5GNI; -.
DR AlphaFoldDB; P16284; -.
DR BMRB; P16284; -.
DR SMR; P16284; -.
DR BioGRID; 111201; 32.
DR IntAct; P16284; 95.
DR MINT; P16284; -.
DR STRING; 9606.ENSP00000457421; -.
DR GlyConnect; 1610; 12 N-Linked glycans (5 sites).
DR GlyCosmos; P16284; 10 sites, 14 glycans.
DR GlyGen; P16284; 10 sites, 13 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P16284; -.
DR PhosphoSitePlus; P16284; -.
DR SwissPalm; P16284; -.
DR BioMuta; PECAM1; -.
DR DMDM; 129747; -.
DR UCD-2DPAGE; P16284; -.
DR CPTAC; CPTAC-2602; -.
DR CPTAC; CPTAC-5858; -.
DR CPTAC; CPTAC-5949; -.
DR EPD; P16284; -.
DR jPOST; P16284; -.
DR MassIVE; P16284; -.
DR PaxDb; 9606-ENSP00000457421; -.
DR PeptideAtlas; P16284; -.
DR ProteomicsDB; 53335; -. [P16284-1]
DR ProteomicsDB; 53336; -. [P16284-2]
DR ProteomicsDB; 53337; -. [P16284-3]
DR ProteomicsDB; 53338; -. [P16284-4]
DR ProteomicsDB; 53339; -. [P16284-5]
DR ProteomicsDB; 53340; -. [P16284-6]
DR Pumba; P16284; -.
DR TopDownProteomics; P16284-1; -. [P16284-1]
DR Antibodypedia; 58161; 4612 antibodies from 46 providers.
DR DNASU; 5175; -.
DR Ensembl; ENST00000563924.6; ENSP00000457421.1; ENSG00000261371.6. [P16284-1]
DR GeneID; 5175; -.
DR KEGG; hsa:5175; -.
DR MANE-Select; ENST00000563924.6; ENSP00000457421.1; NM_000442.5; NP_000433.4.
DR AGR; HGNC:8823; -.
DR CTD; 5175; -.
DR DisGeNET; 5175; -.
DR GeneCards; PECAM1; -.
DR HGNC; HGNC:8823; PECAM1.
DR HPA; ENSG00000261371; Tissue enhanced (placenta).
DR MIM; 173445; gene.
DR neXtProt; NX_P16284; -.
DR OpenTargets; ENSG00000261371; -.
DR PharmGKB; PA33167; -.
DR VEuPathDB; HostDB:ENSG00000261371; -.
DR eggNOG; ENOG502QW63; Eukaryota.
DR GeneTree; ENSGT01070000253837; -.
DR InParanoid; P16284; -.
DR OMA; FLSCDYE; -.
DR OrthoDB; 5351925at2759; -.
DR PhylomeDB; P16284; -.
DR PathwayCommons; P16284; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-210990; PECAM1 interactions.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P16284; -.
DR SIGNOR; P16284; -.
DR BioGRID-ORCS; 5175; 11 hits in 233 CRISPR screens.
DR ChiTaRS; PECAM1; human.
DR EvolutionaryTrace; P16284; -.
DR GeneWiki; CD31; -.
DR GenomeRNAi; 5175; -.
DR Pharos; P16284; Tbio.
DR PRO; PR:P16284; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P16284; Protein.
DR Bgee; ENSG00000261371; Expressed in tendon of biceps brachii and 211 other cell types or tissues.
DR ExpressionAtlas; P16284; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:ARUK-UCL.
DR GO; GO:0008037; P:cell recognition; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ARUK-UCL.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0050904; P:diapedesis; IDA:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:ARUK-UCL.
DR GO; GO:0072011; P:glomerular endothelium development; IEP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0035696; P:monocyte extravasation; IMP:ARUK-UCL.
DR GO; GO:0072672; P:neutrophil extravasation; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0150107; P:positive regulation of protein localization to cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR040878; IL-40-like_Ig.
DR PANTHER; PTHR11481:SF114; FC RECEPTOR-LIKE B; 1.
DR PANTHER; PTHR11481; IMMUNOGLOBULIN FC RECEPTOR; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF17736; Ig_C17orf99; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Lipoprotein; Membrane; Palmitate; Phagocytosis; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT CHAIN 28..738
FT /note="Platelet endothelial cell adhesion molecule"
FT /id="PRO_0000014895"
FT TOPO_DOM 28..601
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..121
FT /note="Ig-like C2-type 1"
FT DOMAIN 145..233
FT /note="Ig-like C2-type 2"
FT DOMAIN 236..315
FT /note="Ig-like C2-type 3"
FT DOMAIN 328..401
FT /note="Ig-like C2-type 4"
FT DOMAIN 424..493
FT /note="Ig-like C2-type 5"
FT DOMAIN 499..591
FT /note="Ig-like C2-type 6"
FT REGION 658..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..729
FT /note="Membrane-bound segment which detaches upon
FT phosphorylation"
FT /evidence="ECO:0000269|PubMed:21464369"
FT REGION 721..738
FT /note="May play a role in cytoprotective signaling"
FT MOTIF 688..693
FT /note="ITIM motif 1"
FT /evidence="ECO:0000305|PubMed:27958302"
FT MOTIF 711..716
FT /note="ITIM motif 2"
FT /evidence="ECO:0000305|PubMed:27958302"
FT COMPBIAS 661..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 690
FT /note="Phosphotyrosine; by FER"
FT /evidence="ECO:0000269|PubMed:19342684,
FT ECO:0000269|PubMed:21464369"
FT MOD_RES 713
FT /note="Phosphotyrosine; by FER"
FT /evidence="ECO:0000269|PubMed:19342684,
FT ECO:0000269|PubMed:21464369, ECO:0000269|PubMed:9298995"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21464369"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21464369"
FT LIPID 622
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:17139370"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26702061,
FT ECO:0007744|PDB:5C14"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:26702061, ECO:0007744|PDB:5C14"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:26702061, ECO:0007744|PDB:5C14"
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:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 57..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:26702061, ECO:0000269|PubMed:27958302,
FT ECO:0007744|PDB:5C14, ECO:0007744|PDB:5GNI"
FT DISULFID 152..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:26702061, ECO:0000269|PubMed:27958302,
FT ECO:0007744|PDB:5C14, ECO:0007744|PDB:5GNI"
FT DISULFID 256..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 347..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 523..572
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 664..681
FT /note="Missing (in isoform Delta12)"
FT /evidence="ECO:0000305"
FT /id="VSP_011806"
FT VAR_SEQ 682..702
FT /note="Missing (in isoform Delta13)"
FT /evidence="ECO:0000305"
FT /id="VSP_011807"
FT VAR_SEQ 703..729
FT /note="Missing (in isoform Delta14-15)"
FT /evidence="ECO:0000305"
FT /id="VSP_011808"
FT VAR_SEQ 703..721
FT /note="Missing (in isoform Delta14)"
FT /evidence="ECO:0000305"
FT /id="VSP_011809"
FT VAR_SEQ 722..729
FT /note="Missing (in isoform Delta15)"
FT /evidence="ECO:0000305"
FT /id="VSP_011810"
FT VAR_SEQ 730..738
FT /note="RTEGSLDGT -> ENGRLP (in isoform Delta14-15 and
FT isoform Delta15)"
FT /evidence="ECO:0000305"
FT /id="VSP_011811"
FT VARIANT 125
FT /note="V -> L (in dbSNP:rs281865545)"
FT /evidence="ECO:0000269|PubMed:11791967,
FT ECO:0000269|PubMed:1690453, ECO:0000269|PubMed:17212705,
FT ECO:0000269|PubMed:8532023"
FT /id="VAR_013145"
FT VARIANT 304
FT /note="C -> Y (in dbSNP:rs7209607)"
FT /id="VAR_059402"
FT VARIANT 563
FT /note="S -> I (in dbSNP:rs12953)"
FT /id="VAR_059403"
FT VARIANT 563
FT /note="S -> N (in dbSNP:rs12953)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1700999,
FT ECO:0000269|PubMed:17212705, ECO:0000269|PubMed:7994021,
FT ECO:0000269|Ref.6, ECO:0000269|Ref.9"
FT /id="VAR_059404"
FT VARIANT 670
FT /note="R -> G (in dbSNP:rs1131012)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1700999,
FT ECO:0000269|PubMed:17212705, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.9"
FT /id="VAR_059405"
FT MUTAGEN 52
FT /note="N->Q: Probable loss of N-glycosylation. No effect on
FT homophilic cell adhesion; when associated with Q-84 and Q-
FT 151."
FT /evidence="ECO:0000269|PubMed:27958302"
FT MUTAGEN 74
FT /note="L->E: Reduced homophilic cell adhesion; when
FT associated with E-112; E-188 and E-190."
FT /evidence="ECO:0000269|PubMed:27958302"
FT MUTAGEN 84
FT /note="N->Q: Probable loss of N-glycosylation. No effect on
FT homophilic cell adhesion; when associated with Q-52 and Q-
FT 151."
FT /evidence="ECO:0000269|PubMed:27958302"
FT MUTAGEN 89
FT /note="K->A: Lacks homophilic binding ability and is
FT distributed over the entire plasma membrane."
FT /evidence="ECO:0000269|PubMed:19342684"
FT MUTAGEN 112
FT /note="I->E: Reduced homophilic cell adhesion; when
FT associated with E-74; E-188 and E-190."
FT /evidence="ECO:0000269|PubMed:27958302"
FT MUTAGEN 151
FT /note="N->Q: Probable loss of N-glycosylation. No effect on
FT homophilic cell adhesion; when associated with Q-52 and Q-
FT 84."
FT /evidence="ECO:0000269|PubMed:27958302"
FT MUTAGEN 188
FT /note="F->E: Reduced homophilic cell adhesion; when
FT associated with E-74; E-112 and E-190."
FT /evidence="ECO:0000269|PubMed:27958302"
FT MUTAGEN 190
FT /note="I->E: Reduced homophilic cell adhesion; when
FT associated with E-74; E-112 and E-188."
FT /evidence="ECO:0000269|PubMed:27958302"
FT MUTAGEN 622
FT /note="C->A: 6-fold decrease in association with membrane
FT microdomains."
FT /evidence="ECO:0000269|PubMed:17139370"
FT MUTAGEN 690
FT /note="Y->F: No effect on Tyr-713 phosphorylation. Inhibits
FT targeted recycling of PECAM1 from the lateral border
FT recycling compartment (LBRC) around transmigrating
FT monocytes. Decreases phosphorylation. No effect on
FT interaction with PTPN11. Loss of phosphorylation and loss
FT of binding to PTPN11; when associated with F-713."
FT /evidence="ECO:0000269|PubMed:18388311,
FT ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:21464369"
FT MUTAGEN 713
FT /note="Y->F: Loss of Tyr-690 phosphorylation. Does not
FT inhibit targeted recycling of PECAM1 from the lateral
FT border recycling compartment (LBRC) around transmigrating
FT monocytes. Decreases phosphorylation. Loss of interaction
FT with PTPN11. Loss of phosphorylation and loss of binding to
FT PTPN11; when associated with F-690."
FT /evidence="ECO:0000269|PubMed:18388311,
FT ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:21464369"
FT CONFLICT 6
FT /note="A -> T (in Ref. 7; BAF83381)"
FT /evidence="ECO:0000305"
FT CONFLICT 8..12
FT /note="GATMW -> ADV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="V -> M (in Ref. 11; AAK84009)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="P -> L (in Ref. 11; AAK84011)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="E -> K (in Ref. 11; AAF91460)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="R -> H (in Ref. 11; AAF91451)"
FT /evidence="ECO:0000305"
FT STRAND 32..43
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 80..98
FT /evidence="ECO:0007829|PDB:5C14"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5GNI"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:5C14"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:5GNI"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 184..194
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 200..218
FT /evidence="ECO:0007829|PDB:5C14"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5GNI"
FT HELIX 709..728
FT /evidence="ECO:0007829|PDB:2KY5"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:2KY5"
SQ SEQUENCE 738 AA; 82522 MW; 9D531D2DDCCB7F92 CRC64;
MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD
VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT
AEYQVLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE
KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI
SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG
NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ
KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE
VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN
CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK
EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK
KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN
SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKDLGKKDTE TVYSEVRKAV
PDAVESRYSR TEGSLDGT
//
