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Platelet endothelial cell adhesion molecule (PECAM-1) (EndoCAM) (GPIIA') (PECA1) (CD antigen CD31)

 PECA1_HUMAN             Reviewed;         738 AA.
P16284; A0A075B738; A8K3S7; D3DU31; Q6LDA9; Q8TBH1; Q96RF5; Q96RF6;
Q9NP65; Q9NPB7; Q9NPG9; Q9NQS9; Q9NQT0; Q9NQT1; Q9NQT2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 2.
07-NOV-2018, entry version 210.
RecName: Full=Platelet endothelial cell adhesion molecule;
Short=PECAM-1;
AltName: Full=EndoCAM;
AltName: Full=GPIIA';
AltName: Full=PECA1;
AltName: CD_antigen=CD31;
Flags: Precursor;
Name=PECAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=2351935; DOI=10.1084/jem.171.6.2147;
Simmons D.L., Walker C., Power C., Pigott R.;
"Molecular cloning of CD31, a putative intercellular adhesion molecule
closely related to carcinoembryonic antigen.";
J. Exp. Med. 171:2147-2152(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANTS ASN-563 AND
GLY-670.
PubMed=1700999;
Stockinger H., Gadd S.J., Eher R., Majdic O., Kasinrek W.,
Schreiber W., Strass B., Schnabl E., Knapp W.;
"Molecular characterization and functional analysis of the leukocyte
surface protein CD31.";
J. Immunol. 145:3889-3897(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT LEU-125.
PubMed=1690453; DOI=10.1126/science.1690453;
Newman P.J., Berndt M.C., Gorski J., White J.C. II, Lyman S.,
Paddock C., Muller W.A.;
"PECAM-1 (CD31) cloning and relation to adhesion molecules of the
immunoglobulin gene superfamily.";
Science 247:1219-1222(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=1874786; DOI=10.1083/jcb.114.5.1059;
Albelda S.M., Muller W.A., Buck C.A., Newman P.J.;
"Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel
vascular cell-cell adhesion molecule.";
J. Cell Biol. 114:1059-1068(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), AND VARIANT ASN-563.
PubMed=7994021;
Kirschbaum N.E., Gumina R.J., Newman P.J.;
"Organization of the gene for human platelet/endothelial cell adhesion
molecule-1 shows alternatively spliced isoforms and a functionally
complex cytoplasmic domain.";
Blood 84:4028-4037(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANTS ASN-563 AND
GLY-670.
Wang R.-Y., Lun Y.-Z., Jiang Z.-X., Li X.;
"Gene cloning and sequence analysis of human nasopharyngeal carcinoma
resistance cells CNE1/R platelet/endothelial cell adhesion molecule.";
Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANTS
ASN-563 AND GLY-670.
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ASN-563
AND GLY-670.
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANTS
ASN-563 AND GLY-670.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-734 (ISOFORM LONG), AND VARIANTS
LEU-125; ASN-563 AND GLY-670.
PubMed=17212705; DOI=10.1111/j.1399-0039.2006.00722.x;
Robbins F.-M., Hartzman R.J.;
"CD31/PECAM-1 genotyping and haplotype analyses show population
diversity.";
Tissue Antigens 69:28-37(2007).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 507-584.
PubMed=8226797;
Tang D.G., Chen Y.Q., Newman P.J., Shi L., Gao X., Diglio C.A.,
Honn K.V.;
"Identification of PECAM-1 in solid tumor cells and its potential
involvement in tumor cell adhesion to endothelium.";
J. Biol. Chem. 268:22883-22894(1993).
[13]
PHOSPHORYLATION AT TYR-713.
PubMed=9298995; DOI=10.1083/jcb.138.6.1425;
Famiglietti J., Sun J., DeLisser H.M., Albelda S.M.;
"Tyrosine residue in exon 14 of the cytoplasmic domain of platelet
endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligand
binding specificity.";
J. Cell Biol. 138:1425-1435(1997).
[14]
FUNCTION.
PubMed=12110892; DOI=10.1038/nature00811;
Brown S., Heinisch I., Ross E., Shaw K., Buckley C.D., Savill J.;
"Apoptosis disables CD31-mediated cell detachment from phagocytes
promoting binding and engulfment.";
Nature 418:200-203(2002).
[15]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=12433657; DOI=10.1152/ajpheart.00600.2002;
Wang Y., Su X., Sorenson C.M., Sheibani N.;
"Tissue-specific distributions of alternatively spliced human PECAM-1
isoforms.";
Am. J. Physiol. 284:H1008-H1017(2003).
[16]
PALMITOYLATION AT CYS-622, MUTAGENESIS OF CYS-622, AND SUBCELLULAR
LOCATION.
PubMed=17139370;
Sardjono C.T., Harbour S.N., Yip J.C., Paddock C., Tridandapani S.,
Newman P.J., Jackson D.E.;
"Palmitoylation at Cys595 is essential for PECAM-1 localisation into
membrane microdomains and for efficient PECAM-1-mediated
cytoprotection.";
Thromb. Haemost. 96:756-766(2006).
[17]
FUNCTION, INTERACTION WITH CD177, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=17580308; DOI=10.1074/jbc.M701120200;
Sachs U.J., Andrei-Selmer C.L., Maniar A., Weiss T., Paddock C.,
Orlova V.V., Choi E.Y., Newman P.J., Preissner K.T., Chavakis T.,
Santoso S.;
"The neutrophil-specific antigen CD177 is a counter-receptor for
platelet endothelial cell adhesion molecule-1 (CD31).";
J. Biol. Chem. 282:23603-23612(2007).
[18]
FUNCTION, AND INTERACTION WITH BDKRB2 AND GNAQ.
PubMed=18672896; DOI=10.1021/bi8003846;
Yeh J.C., Otte L.A., Frangos J.A.;
"Regulation of G protein-coupled receptor activities by the platelet-
endothelial cell adhesion molecule, PECAM-1.";
Biochemistry 47:9029-9039(2008).
[19]
PHOSPHORYLATION.
PubMed=18710921; DOI=10.1083/jcb.200801062;
Chiu Y.J., McBeath E., Fujiwara K.;
"Mechanotransduction in an extracted cell model: Fyn drives
stretch- and flow-elicited PECAM-1 phosphorylation.";
J. Cell Biol. 182:753-763(2008).
[20]
ALTERNATIVE SPLICING (ISOFORMS DELTA14-15 AND DELTA15), FUNCTION
(ISOFORM DELTA15), SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
MUTAGENESIS OF TYR-690 AND TYR-713, AND INTERACTION WITH PTPN11.
PubMed=18388311; DOI=10.1242/jcs.025163;
Bergom C., Paddock C., Gao C., Holyst T., Newman D.K., Newman P.J.;
"An alternatively spliced isoform of PECAM-1 is expressed at high
levels in human and murine tissues, and suggests a novel role for the
C-terminus of PECAM-1 in cytoprotective signaling.";
J. Cell Sci. 121:1235-1242(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[22]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT
TYR-690 AND TYR-713, MUTAGENESIS OF LYS-89; TYR-690 AND TYR-713, AND
INTERACTION WITH PTPN11.
PubMed=19342684; DOI=10.4049/jimmunol.0803192;
Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.;
"A novel and critical role for tyrosine 663 in platelet endothelial
cell adhesion molecule-1 trafficking and transendothelial migration.";
J. Immunol. 182:5041-5051(2009).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151; ASN-320 AND ASN-453.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-320 AND ASN-551.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
PALMITOYLATION BY ZDHHC21, AND SUBCELLULAR LOCATION.
PubMed=22496122; DOI=10.1161/CIRCRESAHA.112.269514;
Marin E.P., Derakhshan B., Lam T.T., Davalos A., Sessa W.C.;
"Endothelial cell palmitoylproteomic identifies novel lipid-modified
targets and potential substrates for protein acyl transferases.";
Circ. Res. 110:1336-1344(2012).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
STRUCTURE BY NMR OF 686-738, TISSUE SPECIFICITY, MOTIF,
PHOSPHORYLATION AT TYR-690; TYR-713; SER-729 AND SER-734, AND
MUTAGENESIS OF TYR-690 AND TYR-713.
PubMed=21464369; DOI=10.1182/blood-2010-11-317867;
Paddock C., Lytle B.L., Peterson F.C., Holyst T., Newman P.J.,
Volkman B.F., Newman D.K.;
"Residues within a lipid-associated segment of the PECAM-1 cytoplasmic
domain are susceptible to inducible, sequential phosphorylation.";
Blood 117:6012-6023(2011).
[30]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 28-229, SUBUNIT,
GLYCOSYLATION AT ASN-52; ASN-84 AND ASN-151, AND DISULFIDE BONDS.
PubMed=26702061; DOI=10.1182/blood-2015-07-660092;
Paddock C., Zhou D., Lertkiatmongkol P., Newman P.J., Zhu J.;
"Structural basis for PECAM-1 homophilic binding.";
Blood 127:1052-1061(2016).
[31]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 28-232, FUNCTION, SUBUNIT,
DISULFIDE BONDS, AND MUTAGENESIS OF ASN-52; LEU-74; ASN-84; ILE-112;
ASN-151; PHE-188 AND ILE-190.
PubMed=27958302; DOI=10.1038/srep38655;
Hu M., Zhang H., Liu Q., Hao Q.;
"Structural basis for human PECAM-1-mediated trans-homophilic cell
adhesion.";
Sci. Rep. 6:38655-38655(2016).
[32]
VARIANT LEU-125.
PubMed=8532023; DOI=10.1056/NEJM199602013340502;
Behar E., Chao N.J., Hiraki D.D., Krishnaswamy S., Brown B.W.,
Zehnder J.L., Grumet F.C.;
"Polymorphism of adhesion molecule CD31 and its role in acute graft-
versus-host disease.";
N. Engl. J. Med. 334:286-291(1996).
[33]
VARIANT LEU-125.
PubMed=11791967;
Casals-Pascual C., Allen S., Allen A., Kai O., Lowe B., Pain A.,
Roberts D.J.;
"Codon 125 polymorphism of CD31 and susceptibility to malaria.";
Am. J. Trop. Med. Hyg. 65:736-737(2001).
-!- FUNCTION: Cell adhesion molecule which is required for leukocyte
transendothelial migration (TEM) under most inflammatory
conditions (PubMed:19342684, PubMed:17580308). Tyr-690 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 (PubMed:19342684). Trans-homophilic
interaction may play a role in endothelial cell-cell adhesion via
cell junctions (PubMed:27958302). Heterophilic interaction with
CD177 plays a role in transendothelial migration of neutrophils
(PubMed:17580308). Homophilic ligation of PECAM1 prevents
macrophage-mediated phagocytosis of neighboring viable leukocytes
by transmitting a detachment signal (PubMed:12110892). 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
(PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation
(PubMed:18672896). Regulates bradykinin- and hyperosmotic shock-
induced ERK1/2 activation in endothelial cells (PubMed:18672896).
Induces susceptibility to atherosclerosis (By similarity).
{ECO:0000250|UniProtKB:Q08481, ECO:0000269|PubMed:12110892,
ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18672896,
ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:27958302}.
-!- FUNCTION: Isoform Delta15: Does not protect against apoptosis.
{ECO:0000269|PubMed:18388311}.
-!- SUBUNIT: Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-
type 2 domains); trans-homodimerization is required for cell-cell
interaction (PubMed:26702061, PubMed:27958302). Forms a complex
with BDKRB2 and GNAQ (PubMed:18672896). Interacts with BDKRB2 and
GNAQ (PubMed:18672896).Interacts with PTPN11; Tyr-713 is critical
for PTPN11 recruitment (PubMed:18388311, PubMed:19342684).
Interacts with FER (By similarity). Interacts (via Ig-like C2-type
domain 6) with CD177; the interaction is Ca(2+)-dependent; the
interaction is direct (PubMed:17580308).
{ECO:0000250|UniProtKB:P51866, ECO:0000269|PubMed:17580308,
ECO:0000269|PubMed:18388311, ECO:0000269|PubMed:18672896,
ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:26702061,
ECO:0000269|PubMed:27958302}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=3; IntAct=EBI-716404, EBI-491549;
P14923:JUP; NbExp=7; IntAct=EBI-716404, EBI-702484;
Q06124:PTPN11; NbExp=7; IntAct=EBI-716404, EBI-297779;
P29350:PTPN6; NbExp=4; IntAct=EBI-716404, EBI-78260;
P12931:SRC; NbExp=3; IntAct=EBI-716404, EBI-621482;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17580308};
Single-pass type I membrane protein {ECO:0000305}. Note=Cell
surface expression on neutrophils is down-regulated upon fMLP or
CXCL8/IL8-mediated stimulation. {ECO:0000269|PubMed:17580308}.
-!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane
{ECO:0000269|PubMed:18388311, ECO:0000269|PubMed:19342684};
Single-pass type I membrane protein {ECO:0000305|PubMed:18388311}.
Membrane raft {ECO:0000269|PubMed:17139370,
ECO:0000269|PubMed:22496122}. Cell junction
{ECO:0000269|PubMed:18388311}. Note=Localizes to the lateral
border recycling compartment (LBRC) and recycles from the LBRC to
the junction in resting endothelial cells.
{ECO:0000269|PubMed:19342684}.
-!- SUBCELLULAR LOCATION: Isoform Delta15: Cell junction
{ECO:0000269|PubMed:18388311}. Note=Localizes to the lateral
border recycling compartment (LBRC) and recycles from the LBRC to
the junction in resting endothelial cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=Long;
IsoId=P16284-1; Sequence=Displayed;
Name=Delta12;
IsoId=P16284-2; Sequence=VSP_011806;
Name=Delta13;
IsoId=P16284-3; Sequence=VSP_011807;
Name=Delta14;
IsoId=P16284-4; Sequence=VSP_011809;
Name=Delta14-15;
IsoId=P16284-5; Sequence=VSP_011808, VSP_011811;
Name=Delta15;
IsoId=P16284-6; Sequence=VSP_011810, VSP_011811;
-!- TISSUE SPECIFICITY: Expressed on platelets and leukocytes and is
primarily concentrated at the borders between endothelial cells
(PubMed:18388311, PubMed:21464369). Expressed in human umbilical
vein endothelial cells (HUVECs) (at protein level)
(PubMed:19342684, PubMed:17580308). Expressed on neutrophils (at
protein level) (PubMed:17580308). Isoform Long predominates in all
tissues examined (PubMed:12433657). Isoform Delta12 is detected
only in trachea (PubMed:12433657). Isoform Delta14-15 is only
detected in lung (PubMed:12433657). Isoform Delta14 is detected in
all tissues examined with the strongest expression in heart
(PubMed:12433657). Isoform Delta15 is expressed in brain, testis,
ovary, cell surface of platelets, human umbilical vein endothelial
cells (HUVECs), Jurkat T-cell leukemia, human erythroleukemia
(HEL) and U-937 histiocytic lymphoma cell lines (at protein level)
(PubMed:12433657, PubMed:18388311). {ECO:0000269|PubMed:12433657,
ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18388311,
ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:21464369}.
-!- DOMAIN: The Ig-like C2-type domains 2 and 3 contribute to
formation of the complex with BDKRB2 and in regulation of its
activity.
-!- PTM: Phosphorylated on Ser and Tyr residues after cellular
activation by src kinases (PubMed:21464369, PubMed:9298995,
PubMed:19342684, PubMed:18710921). Upon activation, phosphorylated
on Ser-729 which probably initiates the dissociation of the
membrane-interaction segment (residues 709-729) from the cell
membrane allowing the sequential phosphorylation of Tyr-713 and
Tyr-690 (PubMed:21464369). Constitutively phosphorylated on Ser-
734 in resting platelets (PubMed:21464369). Phosphorylated on
tyrosine residues by FER and FES in response to FCER1 activation
(By similarity). In endothelial cells Fyn mediates mechanical-
force (stretch or pull) induced tyrosine phosphorylation
(PubMed:18710921). {ECO:0000250|UniProtKB:Q08481,
ECO:0000269|PubMed:18710921, ECO:0000269|PubMed:19342684,
ECO:0000269|PubMed:21464369, ECO:0000269|PubMed:9298995}.
-!- PTM: Palmitoylation by ZDHHC21 is necessary for cell surface
expression in endothelial cells and enrichment in membrane rafts.
{ECO:0000269|PubMed:17139370, ECO:0000269|PubMed:22496122}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PECAM-1";
-!- WEB RESOURCE: Name=Wikipedia; Note=CD31 entry;
URL="https://en.wikipedia.org/wiki/CD31";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=PECAM-1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_265";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M37780; AAA36186.1; -; mRNA.
EMBL; M28526; AAA36429.1; -; mRNA.
EMBL; L34657; AAA60057.1; -; Genomic_DNA.
EMBL; L34631; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34637; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34638; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34639; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34640; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34641; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34642; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34644; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34645; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34649; AAA60057.1; JOINED; Genomic_DNA.
EMBL; L34655; AAA60057.1; JOINED; Genomic_DNA.
EMBL; JQ287500; AFA36630.1; -; mRNA.
EMBL; AK290692; BAF83381.1; -; mRNA.
EMBL; AC016489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC234063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94207.1; -; Genomic_DNA.
EMBL; CH471109; EAW94208.1; -; Genomic_DNA.
EMBL; BC022512; AAH22512.1; -; mRNA.
EMBL; BC051822; AAH51822.1; -; mRNA.
EMBL; AF281287; AAF91446.1; -; mRNA.
EMBL; AF281288; AAF91447.1; -; mRNA.
EMBL; AF281289; AAF91448.1; -; mRNA.
EMBL; AF281290; AAF91449.1; -; mRNA.
EMBL; AF281291; AAF91450.1; -; mRNA.
EMBL; AF281292; AAF91451.1; -; mRNA.
EMBL; AF281293; AAF91452.1; -; mRNA.
EMBL; AF281294; AAF91453.1; -; mRNA.
EMBL; AF281295; AAF91454.1; -; mRNA.
EMBL; AF281296; AAF91455.1; -; mRNA.
EMBL; AF281297; AAF91456.1; -; mRNA.
EMBL; AF281298; AAF91457.1; -; mRNA.
EMBL; AF281299; AAF91458.1; -; mRNA.
EMBL; AF281300; AAF91459.1; -; mRNA.
EMBL; AF281301; AAF91460.1; -; mRNA.
EMBL; AF393676; AAK84009.1; -; mRNA.
EMBL; AF393677; AAK84010.1; -; mRNA.
EMBL; AF393678; AAK84011.1; -; mRNA.
EMBL; S66450; AAB28645.1; -; mRNA.
CCDS; CCDS74132.1; -. [P16284-1]
PIR; A40096; A40096.
RefSeq; NP_000433.4; NM_000442.4. [P16284-1]
RefSeq; XP_005276937.1; XM_005276880.1. [P16284-6]
RefSeq; XP_005276938.1; XM_005276881.1. [P16284-4]
RefSeq; XP_005276939.1; XM_005276882.1. [P16284-3]
RefSeq; XP_011523191.1; XM_011524889.2. [P16284-1]
RefSeq; XP_011523192.1; XM_011524890.1. [P16284-1]
RefSeq; XP_016880227.1; XM_017024738.1. [P16284-1]
RefSeq; XP_016880228.1; XM_017024739.1. [P16284-2]
RefSeq; XP_016880229.1; XM_017024740.1. [P16284-4]
UniGene; Hs.376675; -.
UniGene; Hs.514412; -.
UniGene; Hs.722648; -.
PDB; 2KY5; NMR; -; A=686-738.
PDB; 5C14; X-ray; 2.80 A; A/B=28-229.
PDB; 5GNI; X-ray; 3.01 A; A/B=28-232.
PDBsum; 2KY5; -.
PDBsum; 5C14; -.
PDBsum; 5GNI; -.
ProteinModelPortal; P16284; -.
SMR; P16284; -.
BioGrid; 111201; 22.
IntAct; P16284; 20.
MINT; P16284; -.
GlyConnect; 1610; -.
iPTMnet; P16284; -.
PhosphoSitePlus; P16284; -.
SwissPalm; P16284; -.
DMDM; 129747; -.
UCD-2DPAGE; P16284; -.
EPD; P16284; -.
PeptideAtlas; P16284; -.
PRIDE; P16284; -.
ProteomicsDB; 53335; -.
ProteomicsDB; 53336; -. [P16284-2]
ProteomicsDB; 53337; -. [P16284-3]
ProteomicsDB; 53338; -. [P16284-4]
ProteomicsDB; 53339; -. [P16284-5]
ProteomicsDB; 53340; -. [P16284-6]
TopDownProteomics; P16284-1; -. [P16284-1]
DNASU; 5175; -.
Ensembl; ENST00000563924; ENSP00000457421; ENSG00000261371. [P16284-1]
GeneID; 5175; -.
KEGG; hsa:5175; -.
CTD; 5175; -.
DisGeNET; 5175; -.
EuPathDB; HostDB:ENSG00000261371.5; -.
GeneCards; PECAM1; -.
HGNC; HGNC:8823; PECAM1.
HPA; HPA004690; -.
MIM; 173445; gene.
neXtProt; NX_P16284; -.
OpenTargets; ENSG00000261371; -.
PharmGKB; PA33167; -.
GeneTree; ENSGT00440000034155; -.
HOVERGEN; HBG059434; -.
InParanoid; P16284; -.
KO; K06471; -.
OMA; YTCKVEA; -.
OrthoDB; EOG091G033M; -.
PhylomeDB; P16284; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; PECAM1; human.
EvolutionaryTrace; P16284; -.
GeneWiki; CD31; -.
GenomeRNAi; 5175; -.
PMAP-CutDB; P16284; -.
PRO; PR:P16284; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000261371; Expressed in 238 organ(s), highest expression level in tendon of biceps brachii.
GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
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; IDA:UniProtKB.
GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0030485; C:smooth muscle contractile fiber; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0008037; P:cell recognition; TAS:ProtInc.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
GO; GO:0050904; P:diapedesis; IDA:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
GO; GO:0090673; P:endothelial cell-matrix adhesion; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0072011; P:glomerular endothelium development; IEP:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0072672; P:neutrophil extravasation; IMP:UniProtKB.
GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 4.
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; 1.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phagocytosis;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 27
CHAIN 28 738 Platelet endothelial cell adhesion
molecule.
/FTId=PRO_0000014895.
TOPO_DOM 28 601 Extracellular. {ECO:0000255}.
TRANSMEM 602 620 Helical. {ECO:0000255}.
TOPO_DOM 621 738 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 121 Ig-like C2-type 1.
DOMAIN 145 233 Ig-like C2-type 2.
DOMAIN 236 315 Ig-like C2-type 3.
DOMAIN 328 401 Ig-like C2-type 4.
DOMAIN 424 493 Ig-like C2-type 5.
DOMAIN 499 591 Ig-like C2-type 6.
REGION 709 729 Membrane-bound segment which detaches
upon phosphorylation.
{ECO:0000269|PubMed:21464369}.
REGION 721 738 May play a role in cytoprotective
signaling.
MOTIF 688 693 ITIM motif 1.
{ECO:0000305|PubMed:27958302}.
MOTIF 711 716 ITIM motif 2.
{ECO:0000305|PubMed:27958302}.
MOD_RES 690 690 Phosphotyrosine; by FER.
{ECO:0000269|PubMed:19342684,
ECO:0000269|PubMed:21464369}.
MOD_RES 713 713 Phosphotyrosine; by FER.
{ECO:0000269|PubMed:19342684,
ECO:0000269|PubMed:21464369,
ECO:0000269|PubMed:9298995}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000269|PubMed:21464369}.
MOD_RES 734 734 Phosphoserine.
{ECO:0000269|PubMed:21464369}.
LIPID 622 622 S-palmitoyl cysteine.
{ECO:0000269|PubMed:17139370}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5C14,
ECO:0000269|PubMed:26702061}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5C14,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:26702061}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5C14,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:26702061}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 57 109 {ECO:0000244|PDB:5C14,
ECO:0000244|PDB:5GNI,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:26702061,
ECO:0000269|PubMed:27958302}.
DISULFID 152 206 {ECO:0000244|PDB:5C14,
ECO:0000244|PDB:5GNI,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:26702061,
ECO:0000269|PubMed:27958302}.
DISULFID 256 304 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 347 386 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 431 476 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 523 572 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 664 681 Missing (in isoform Delta12).
{ECO:0000305}.
/FTId=VSP_011806.
VAR_SEQ 682 702 Missing (in isoform Delta13).
{ECO:0000305}.
/FTId=VSP_011807.
VAR_SEQ 703 729 Missing (in isoform Delta14-15).
{ECO:0000305}.
/FTId=VSP_011808.
VAR_SEQ 703 721 Missing (in isoform Delta14).
{ECO:0000305}.
/FTId=VSP_011809.
VAR_SEQ 722 729 Missing (in isoform Delta15).
{ECO:0000305}.
/FTId=VSP_011810.
VAR_SEQ 730 738 RTEGSLDGT -> ENGRLP (in isoform Delta14-
15 and isoform Delta15). {ECO:0000305}.
/FTId=VSP_011811.
VARIANT 125 125 V -> L (in dbSNP:rs281865545).
{ECO:0000269|PubMed:11791967,
ECO:0000269|PubMed:1690453,
ECO:0000269|PubMed:17212705,
ECO:0000269|PubMed:8532023}.
/FTId=VAR_013145.
VARIANT 304 304 C -> Y (in dbSNP:rs7209607).
/FTId=VAR_059402.
VARIANT 563 563 S -> I (in dbSNP:rs12953).
/FTId=VAR_059403.
VARIANT 563 563 S -> N (in dbSNP:rs12953).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1700999,
ECO:0000269|PubMed:17212705,
ECO:0000269|PubMed:7994021,
ECO:0000269|Ref.6, ECO:0000269|Ref.9}.
/FTId=VAR_059404.
VARIANT 670 670 R -> G (in dbSNP:rs1131012).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1700999,
ECO:0000269|PubMed:17212705,
ECO:0000269|Ref.6, ECO:0000269|Ref.9}.
/FTId=VAR_059405.
MUTAGEN 52 52 N->Q: Probable loss of N-glycosylation.
No effect on homophilic cell adhesion;
when associated with Q-84 and Q-151.
{ECO:0000269|PubMed:27958302}.
MUTAGEN 74 74 L->E: Reduced homophilic cell adhesion;
when associated with E-112; E-188 and E-
190. {ECO:0000269|PubMed:27958302}.
MUTAGEN 84 84 N->Q: Probable loss of N-glycosylation.
No effect on homophilic cell adhesion;
when associated with Q-52 and Q-151.
{ECO:0000269|PubMed:27958302}.
MUTAGEN 89 89 K->A: Lacks homophilic binding ability
and is distributed over the entire plasma
membrane. {ECO:0000269|PubMed:19342684}.
MUTAGEN 112 112 I->E: Reduced homophilic cell adhesion;
when associated with E-74; E-188 and E-
190. {ECO:0000269|PubMed:27958302}.
MUTAGEN 151 151 N->Q: Probable loss of N-glycosylation.
No effect on homophilic cell adhesion;
when associated with Q-52 and Q-84.
{ECO:0000269|PubMed:27958302}.
MUTAGEN 188 188 F->E: Reduced homophilic cell adhesion;
when associated with E-74; E-112 and E-
190. {ECO:0000269|PubMed:27958302}.
MUTAGEN 190 190 I->E: Reduced homophilic cell adhesion;
when associated with E-74; E-112 and E-
188. {ECO:0000269|PubMed:27958302}.
MUTAGEN 622 622 C->A: 6-fold decrease in association with
membrane microdomains.
{ECO:0000269|PubMed:17139370}.
MUTAGEN 690 690 Y->F: No effect on Tyr-713
phosphorylation. Inhibits targeted
recycling of PECAM1 from the lateral
border recycling compartment (LBRC)
around transmigrating monocytes.
Decreases phosphorylation. No effect on
interaction with PTPN11. Loss of
phosphorylation and loss of binding to
PTPN11; when associated with F-713.
{ECO:0000269|PubMed:18388311,
ECO:0000269|PubMed:19342684,
ECO:0000269|PubMed:21464369}.
MUTAGEN 713 713 Y->F: Loss of Tyr-690 phosphorylation.
Does not inhibit targeted recycling of
PECAM1 from the lateral border recycling
compartment (LBRC) around transmigrating
monocytes. Decreases phosphorylation.
Loss of interaction with PTPN11. Loss of
phosphorylation and loss of binding to
PTPN11; when associated with F-690.
{ECO:0000269|PubMed:18388311,
ECO:0000269|PubMed:19342684,
ECO:0000269|PubMed:21464369}.
CONFLICT 6 6 A -> T (in Ref. 7; BAF83381).
{ECO:0000305}.
CONFLICT 8 12 GATMW -> ADV (in Ref. 1). {ECO:0000305}.
CONFLICT 80 80 V -> M (in Ref. 11; AAK84009).
{ECO:0000305}.
CONFLICT 97 97 P -> L (in Ref. 11; AAK84011).
{ECO:0000305}.
CONFLICT 329 329 E -> K (in Ref. 11; AAF91460).
{ECO:0000305}.
CONFLICT 430 430 R -> H (in Ref. 11; AAF91451).
{ECO:0000305}.
STRAND 32 43 {ECO:0000244|PDB:5C14}.
STRAND 45 48 {ECO:0000244|PDB:5C14}.
STRAND 53 64 {ECO:0000244|PDB:5C14}.
STRAND 71 77 {ECO:0000244|PDB:5C14}.
STRAND 80 98 {ECO:0000244|PDB:5C14}.
HELIX 101 103 {ECO:0000244|PDB:5C14}.
STRAND 105 115 {ECO:0000244|PDB:5C14}.
STRAND 117 119 {ECO:0000244|PDB:5C14}.
STRAND 123 128 {ECO:0000244|PDB:5C14}.
STRAND 134 138 {ECO:0000244|PDB:5C14}.
STRAND 140 142 {ECO:0000244|PDB:5GNI}.
STRAND 147 153 {ECO:0000244|PDB:5C14}.
STRAND 161 169 {ECO:0000244|PDB:5C14}.
TURN 170 173 {ECO:0000244|PDB:5GNI}.
STRAND 174 182 {ECO:0000244|PDB:5C14}.
STRAND 184 194 {ECO:0000244|PDB:5C14}.
STRAND 200 218 {ECO:0000244|PDB:5C14}.
STRAND 222 227 {ECO:0000244|PDB:5GNI}.
HELIX 709 728 {ECO:0000244|PDB:2KY5}.
STRAND 731 733 {ECO:0000244|PDB:2KY5}.
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


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E0363m ELISA Mouse,Mus musculus,Pecam,Pecam1,PECAM-1,Pecam-1,Platelet endothelial cell adhesion molecule 96T
U0363m CLIA Mouse,Mus musculus,Pecam,Pecam1,PECAM-1,Pecam-1,Platelet endothelial cell adhesion molecule 96T
20-272-190860 CD31 ( FITC ) - Mouse monoclonal [WM - 59] to CD31 ( FITC ); PECAM-1; EndoCAM; GPIIA'; CD31 antigen Monoclonal 50 TESTS
U0363r CLIA Pecam,Pecam1,PECAM-1,Platelet endothelial cell adhesion molecule,Rat,Rattus norvegicus 96T
E0363r ELISA kit Pecam,Pecam1,PECAM-1,Platelet endothelial cell adhesion molecule,Rat,Rattus norvegicus 96T
E0363r ELISA Pecam,Pecam1,PECAM-1,Platelet endothelial cell adhesion molecule,Rat,Rattus norvegicus 96T
GWB-A51657 Platelet endothelial Cell Adhesion Molecule (CD31 ANTIGEN) (PECAM1) Rabbit anti-Mouse Polyclonal (C-Terminus) Antibody
GWB-64D380 Platelet endothelial Cell Adhesion Molecule (CD31 ANTIGEN) (PECAM1) Mouse anti-Human Monoclonal (2F7B2) Antibody
E02P0108 Rat Platelet endothelial cell adhesion molecule-1 ELISA , PECAM-1_CD31 96 Tests/kit
E02P0108 Rat Platelet endothelial cell adhesion molecule-1 ELISA , PECAM-1_CD31


 

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