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Carcinoembryonic antigen-related cell adhesion molecule 1 (ATP-dependent taurocolate-carrier protein) (Cell-CAM 105) (C-CAM 105) (Ecto-ATPase) (GP110) (pp120) (CD antigen CD66a)

 CEAM1_RAT               Reviewed;         519 AA.
P16573; Q63093;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
05-OCT-2016, sequence version 4.
27-SEP-2017, entry version 158.
RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 1 {ECO:0000250|UniProtKB:P13688};
AltName: Full=ATP-dependent taurocolate-carrier protein;
AltName: Full=Cell-CAM 105 {ECO:0000303|PubMed:8504806};
Short=C-CAM 105;
AltName: Full=Ecto-ATPase {ECO:0000303|PubMed:2527235};
AltName: Full=GP110 {ECO:0000303|PubMed:8536699};
AltName: Full=pp120;
AltName: CD_antigen=CD66a;
Flags: Precursor;
Name=Ceacam1 {ECO:0000312|RGD:67396};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A) (ISOFORM 1), AND PROTEIN
SEQUENCE OF 50-68.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=2527235;
Lin S.-H., Guidotti G.;
"Cloning and expression of a cDNA coding for a rat liver plasma
membrane ecto-ATPase. The primary structure of the ecto-ATPase is
similar to that of the human biliary glycoprotein I.";
J. Biol. Chem. 264:14408-14414(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B) (ISOFORM 2), AND VARIANTS
SER-49; THR-55; VAL-70; THR-73; GLY-74; LEU-75; ASN-76; SER-86;
THR-88; GLN-90; GLU-92; VAL-99; GLY-118; PRO-119; ILE-125 AND LYS-127.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1637321; DOI=10.1042/bj2850047;
Culic O., Huang Q., Flanagan D., Hixon D., Lin S.-H.;
"Molecular cloning and expression of a new rat liver cell-CAM105
isoform. Differential phosphorylation of isoforms.";
Biochem. J. 285:47-53(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-454 (ALLELE A) (ISOFORM 1).
TISSUE=Intestine;
PubMed=8240240; DOI=10.1042/bj2950427;
Cheung P.H., Culic O., Qiu Y., Earley K., Thompson N., Hixson D.C.,
Lin S.-H.;
"The cytoplasmic domain of C-CAM is required for C-CAM-mediated
adhesion function: studies of a C-CAM transcript containing an
unspliced intron.";
Biochem. J. 295:427-435(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B) (ISOFORM 2), AND VARIANTS
SER-49; THR-55; VAL-70; THR-73; GLY-74; LEU-75; ASN-76; SER-86;
THR-88; GLN-90; GLU-92; VAL-99; GLY-118; PRO-119; ILE-125 AND LYS-127.
STRAIN=Sprague-Dawley, and Wistar; TISSUE=Liver;
PubMed=8504806; DOI=10.1111/j.1432-1033.1993.tb17860.x;
Edlund M., Gaardsvoll H., Bock E., Oebrink B.;
"Different isoforms and stock-specific variants of the cell adhesion
molecule C-CAM (cell-CAM 105) in rat liver.";
Eur. J. Biochem. 213:1109-1116(1993).
[5]
NUCLEOTIDE SEQUENCE (ALLELE A) (ISOFORM 2), SUBCELLULAR LOCATION, AND
FUNCTION.
STRAIN=Wistar; TISSUE=Liver;
PubMed=8536699; DOI=10.1111/j.1432-1033.1995.527_b.x;
Lucka L., Cichocka I., Baeumler K., Bechler K., Reutter W.;
"A short isoform of carcinoembryonic-antigen-related rat liver cell-
cell adhesion molecule (C-CAM/gp110) mediates intercellular adhesion.
Sequencing and recombinant functional analysis.";
Eur. J. Biochem. 234:527-535(1995).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE B) (ISOFORM 1), AND
VARIANTS SER-49; THR-55; VAL-70; THR-73; GLY-74; LEU-75; ASN-76;
SER-86; THR-88; GLN-90; GLU-92; VAL-99; GLY-118; PRO-119; ILE-125 AND
LYS-127.
TISSUE=Prostate;
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).
[9]
PROTEIN SEQUENCE OF 58-66 AND 119-138.
PubMed=2141577; DOI=10.1016/0014-5793(90)80264-J;
Aurivillius M., Hansen O.C., Lazrek M.B.S., Bock E., Oebrink B.;
"The cell adhesion molecule Cell-CAM 105 is an ecto-ATPase and a
member of the immunoglobulin superfamily.";
FEBS Lett. 264:267-269(1990).
[10]
PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
STRAIN=Wistar; TISSUE=Liver;
PubMed=8513803; DOI=10.1111/j.1432-1033.1993.tb17952.x;
Becker A., Lucka L., Kilian C., Kannicht C., Reutter W.;
"Characterisation of the ATP-dependent taurocholate-carrier protein
(gp110) of the hepatocyte canalicular membrane.";
Eur. J. Biochem. 214:539-548(1993).
[11]
PROTEIN SEQUENCE OF 110-138 AND 148-150, AND PHOSPHORYLATION.
PubMed=8420979;
Sippel C.J., Suchy F.J., Ananthanarayanan M., Perlmutter D.H.;
"The rat liver ecto-ATPase is also a canalicular bile acid transport
protein.";
J. Biol. Chem. 268:2083-2091(1993).
[12]
HOMODIMERIZATION, AND FUNCTION.
PubMed=2373740;
Tingstroem A., Blikstad I., Aurivillius M., Obrink B.;
"C-CAM (cell-CAM 105) is an adhesive cell surface glycoprotein with
homophilic binding properties.";
J. Cell Sci. 96:17-25(1990).
[13]
CHARACTERIZATION.
PubMed=1831973; DOI=10.1042/bj2780155;
Lin S.-H., Culic O., Flanagan D., Hixson D.C.;
"Immunochemical characterization of two isoforms of rat liver ecto-
ATPase that show an immunological and structural identity with a
glycoprotein cell-adhesion molecule with Mr 105,000.";
Biochem. J. 278:155-161(1991).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8454589;
Cheung P.H., Thompson N.L., Earley K., Culic O., Hixson D., Lin S.H.;
"Cell-CAM105 isoforms with different adhesion functions are
coexpressed in adult rat tissues and during liver development.";
J. Biol. Chem. 268:6139-6146(1993).
[15]
ALTERNATIVE SPLICING.
PubMed=8380406;
Najjae S.M., Accili D., Philippe N., Jernberg J., Margolis R.,
Taylor S.I.;
"pp120/ecto-ATPase, an endogenous substrate of the insulin receptor
tyrosine kinase, is expressed as two variably spliced isoforms.";
J. Biol. Chem. 268:1201-1206(1993).
[16]
FUNCTION, PHOSPHORYLATION AT TYR-488 AND SER-503, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF TYR-488 AND 502-THR-SER-503.
PubMed=7518458;
Sippel C.J., Fallon R.J., Perlmutter D.H.;
"Bile acid efflux mediated by the rat liver canalicular bile acid
transport/ecto-ATPase protein requires serine 503 phosphorylation and
is regulated by tyrosine 488 phosphorylation.";
J. Biol. Chem. 269:19539-19545(1994).
[17]
PHOSPHORYLATION AT TYR-488 BY INSR, AND MUTAGENESIS OF TYR-488 AND
SER-503.
PubMed=7626603; DOI=10.1021/bi00029a009;
Najjar S.M., Philippe N., Suzuki Y., Ignacio G.A., Formisano P.,
Accili D., Taylor S.I.;
"Insulin-stimulated phosphorylation of recombinant pp120/HA4, an
endogenous substrate of the insulin receptor tyrosine kinase.";
Biochemistry 34:9341-9349(1995).
[18]
FUNCTION, AND MUTAGENESIS OF TYR-488; SER-503 AND TYR-513.
PubMed=7592607; DOI=10.1074/jbc.270.41.24073;
Formisano P., Najjar S.M., Gross C.N., Philippe N., Oriente F.,
Kern-Buell C.L., Accili D., Gorden P.;
"Receptor-mediated internalization of insulin. Potential role of
pp120/HA4, a substrate of the insulin receptor kinase.";
J. Biol. Chem. 270:24073-24077(1995).
[19]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=7774714; DOI=10.1016/0014-5793(95)00436-D;
Olsson H., Wikstroem K., Kjellstroem G., Obrink B.;
"Cell adhesion activity of the short cytoplasmic domain isoform of C-
CAM (C-CAM2) in CHO cells.";
FEBS Lett. 365:51-56(1995).
[20]
SUBCELLULAR LOCATION, AND HOMODIMERYZATION.
PubMed=9003371; DOI=10.1042/bj3200847;
Hunter I., Sawa H., Edlund M., Obrink B.;
"Evidence for regulated dimerization of cell-cell adhesion molecule
(C-CAM) in epithelial cells.";
Biochem. J. 320:847-853(1996).
[21]
DOMAIN, AND HOMODOMERIZATION.
PubMed=8831574; DOI=10.1006/excr.1996.0285;
Wikstroem K., Kjellstroem G., Obrink B.;
"Homophilic intercellular adhesion mediated by C-CAM is due to a
domain 1-domain 1 reciprocal binding.";
Exp. Cell Res. 227:360-366(1996).
[22]
INTERACTION WITH CALMODULIN, AND REGION.
PubMed=8576129; DOI=10.1074/jbc.271.3.1393;
Edlund M., Blikstad I., Obrink B.;
"Calmodulin binds to specific sequences in the cytoplasmic domain of
C-CAM and down-regulates C-CAM self-association.";
J. Biol. Chem. 271:1393-1399(1996).
[23]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-488; SER-503 AND
TYR-513, AND PHOSPHORYLATION AT TYR-488 BY INSR.
PubMed=9712832; DOI=10.1074/jbc.273.35.22194;
Choice C.V., Howard M.J., Poy M.N., Hankin M.H., Najjar S.M.;
"Insulin stimulates pp120 endocytosis in cells co-expressing insulin
receptors.";
J. Biol. Chem. 273:22194-22200(1998).
[24]
NOMENCLATURE OF ALTERNATIVE SPLICING ISOFORMS.
PubMed=11501563; DOI=10.1006/excr.1999.4610;
Beauchemin N., Draber P., Dveksler G., Gold P., Gray-Owen S.,
Grunert F., Hammarstrom S., Holmes K.V., Karlsson A., Kuroki M.,
Lin S.H., Lucka L., Najjar S.M., Neumaier M., Obrink B., Shively J.E.,
Skubitz K.M., Stanners C.P., Thomas P., Thompson J.A., Virji M.,
von Kleist S., Wagener C., Watt S., Zimmermann W.;
"Redefined nomenclature for members of the carcinoembryonic antigen
family.";
Exp. Cell Res. 252:243-249(1999).
[25]
INTERACTION WITH SHC1, FUNCTION, AND MUTAGENESIS OF TYR-488 AND
SER-503.
PubMed=11694516; DOI=10.1074/jbc.M108415200;
Poy M.N., Ruch R.J., Fernstrom M.A., Okabayashi Y., Najjar S.M.;
"Shc and CEACAM1 interact to regulate the mitogenic action of
insulin.";
J. Biol. Chem. 277:1076-1084(2002).
[26]
TISSUE SPECIFICITY.
PubMed=11994468; DOI=10.4049/jimmunol.168.10.5139;
Singer B.B., Scheffrahn I., Heymann R., Sigmundsson K., Kammerer R.,
Obrink B.;
"Carcinoembryonic antigen-related cell adhesion molecule 1 expression
and signaling in human, mouse, and rat leukocytes: evidence for
replacement of the short cytoplasmic domain isoform by
glycosylphosphatidylinositol-linked proteins in human leukocytes.";
J. Immunol. 168:5139-5146(2002).
[27]
MUTAGENESIS OF SER-503, AND FUNCTION.
PubMed=11850617; DOI=10.1038/ng840;
Poy M.N., Yang Y., Rezaei K., Fernstroem M.A., Lee A.D., Kido Y.,
Erickson S.K., Najjar S.M.;
"CEACAM1 regulates insulin clearance in liver.";
Nat. Genet. 30:270-276(2002).
[28]
PHOSPHORYLATION AT TYR-488 BY EGFR, FUNCTION, MUTAGENESIS OF TYR-488
AND SER-503, AND INTERACTION WITH EGFR.
PubMed=15467833; DOI=10.1172/JCI200421786;
Abou-Rjaily G.A., Lee S.J., May D., Al-Share Q.Y., Deangelis A.M.,
Ruch R.J., Neumaier M., Kalthoff H., Lin S.H., Najjar S.M.;
"CEACAM1 modulates epidermal growth factor receptor--mediated cell
proliferation.";
J. Clin. Invest. 114:944-952(2004).
[29]
INTERACTION WITH FASN, MUTAGENESIS OF TYR-488; SER-503 AND TYR-513,
SUBCELLULAR LOCATION, FUNCTION, AND PHOSPHORYLATION AT TYR-488 AND
TYR-513 BY INSR.
PubMed=16054098; DOI=10.1016/j.cmet.2005.06.001;
Najjar S.M., Yang Y., Fernstroem M.A., Lee S.J., Deangelis A.M.,
Rjaily G.A., Al-Share Q.Y., Dai T., Miller T.A., Ratnam S., Ruch R.J.,
Smith S., Lin S.H., Beauchemin N., Oyarce A.M.;
"Insulin acutely decreases hepatic fatty acid synthase activity.";
Cell Metab. 2:43-53(2005).
[30]
INTERACTION WITH FLNA, AND REGION.
PubMed=16291724; DOI=10.1242/jcs.02660;
Klaile E., Mueller M.M., Kannicht C., Singer B.B., Lucka L.;
"CEACAM1 functionally interacts with filamin A and exerts a dual role
in the regulation of cell migration.";
J. Cell Sci. 118:5513-5524(2005).
[31]
SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH PTPN11; PTPN6 AND SRC,
AND SUBUNIT.
PubMed=19948503; DOI=10.1083/jcb.200904150;
Mueller M.M., Klaile E., Vorontsova O., Singer B.B., Obrink B.;
"Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L
and recruitment of SHP-2 and c-Src.";
J. Cell Biol. 187:569-581(2009).
-!- FUNCTION: Isoform 1: Cell adhesion protein that mediates
homophilic cell adhesion in a calcium-independent manner
(PubMed:8454589, PubMed:2373740). Plays a role as coinhibitory
receptor in immune response, insulin action and functions also as
an activator during angiogenesis (PubMed:11850617). Its
coinhibitory receptor function is phosphorylation- and PTPN6
-dependent, which in turn, suppress signal transduction of
associated receptors by dephosphorylation of their downstream
effectors (By similarity). Plays a role in immune response, of T-
cells, natural killer (NK) and neutrophils (By similarity). Upon
TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by
blocking granule exocytosis by mediating homophilic binding to
adjacent cells, allowing interaction with and phosphorylation by
LCK and interaction with the TCR/CD3 complex which recruits PTPN6
resulting in dephosphorylation of CD247 and ZAP70 (By similarity).
Also inhibits T-cell proliferation and cytokine production through
inhibition of JNK cascade and plays a crucial role in regulating
autoimmunity and anti-tumor immunity by inhibiting T-cell through
its interaction with HAVCR2 (By similarity). Upon natural killer
(NK) cells activation, inhibit KLRK1-mediated cytolysis of
CEACAM1-bearing tumor cells by trans-homophilic interactions with
CEACAM1 on the target cell and lead to cis-interaction between
CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1
dephosphorylation (By similarity). Upon neutrophils activation
negatively regulates IL1B production by recruiting PTPN6 to a SYK-
TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the
production of reactive oxygen species (ROS) and lysosome
disruption, which in turn, reduces the activity of the
inflammasome (By similarity). Downregulates neutrophil production
by acting as a coinhibitory receptor for CSF3R by downregulating
the CSF3R-STAT3 pathway through recruitment of PTPN6 that
dephosphorylates CSF3R (By similarity). Also regulates insulin
action by promoting INS clearance and regulating lipogenesis in
liver through regulating insulin signaling (PubMed:11850617). Upon
INS stimulation, undergoes phosphorylation by INSR leading to INS
clearance by increasing receptor-mediated insulin endocytosis
(PubMed:7592607, PubMed:9712832). This inernalization promotes
interaction with FASN leading to receptor-mediated insulin
degradation and to reduction of FASN activity leading to negative
regulation of fatty acid synthesis (PubMed:7592607,
PubMed:16054098). INSR-mediated phosphorylation also provokes a
down-regulation of cell proliferation through SHC1 interaction
resulting in decrease coupling of SHC1 to the MAPK3/ERK1-
MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways
(PubMed:11694516). Functions as activator in angiogenesis by
promoting blood vessel remodeling through endothelial cell
differentiation and migration and in arteriogenesis by increasing
the number of collateral arteries and collateral vessel calibers
after ischemia (By similarity). Also regulates vascular
permeability through the VEGFR2 signaling pathway resulting in
control of nitric oxide production (By similarity). Downregulates
cell growth in response to EGF through its interaction with SHC1
that mediates interaction with EGFR resulting in decrease coupling
of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (PubMed:15467833).
Negatively regulates platelet aggregation by decreasing platelet
adhesion on type I collagen through the GPVI-FcRgamma complex (By
similarity). Inhibits cell migration and cell scattering through
interaction with FLNA; interfers with the interaction of FLNA with
RALA (By similarity). Mediates bile acid transport activity in a
phosphorylation dependent manner (PubMed:7518458). Negatively
regulates osteoclastogenesis (By similarity).
{ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P31809,
ECO:0000269|PubMed:11694516, ECO:0000269|PubMed:11850617,
ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16054098,
ECO:0000269|PubMed:2373740, ECO:0000269|PubMed:7518458,
ECO:0000269|PubMed:7592607, ECO:0000269|PubMed:8454589,
ECO:0000269|PubMed:9712832}.
-!- FUNCTION: Isoform 2: Cell adhesion proteins that mediates
homophilic cell adhesion in a calcium-independent manner
(PubMed:8536699, PubMed:7774714). Promotes populations of T-cells
regulating IgA production and secretion associated with control of
the commensal microbiota and resistance to enteropathogens (By
similarity). {ECO:0000250|UniProtKB:P31809,
ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:8536699}.
-!- SUBUNIT: Monomer (PubMed:9003371, PubMed:19948503). Oligomer.
Heterodimer. Homodimer (PubMed:19948503). Cis-dimer/oligomer (via
Ig-like C2-type and/or via cytoplasmic domains); induced by trans-
homophilic cell adhesion through an allosteric mechanism
transmitted by the Ig-like V-type domain, and is regulated by
intracellular calcium and calmodulin (PubMed:19948503,
PubMed:2373740, PubMed:8831574, PubMed:9003371). Interacts (via
cytoplasmic domain) with calmodulin in a calcium dependent manner;
reduces homophilic cell adhesion through dissociation of dimer
(PubMed:8576129). Isoform 1 interacts (via cytoplasmic domain)
with PTPN11 (preferentially) and PTPN6; cis-homodimer form is
preferred; this interaction is decreased by formation of isoform 1
/ isoform 2 cis-heterodimers and is dependent on the monomer/dimer
equilibrium; this interaction is phosphorylation-dependent
(PubMed:19948503). Isoform 1 interacts with LYN (By similarity).
Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2
domain); this interaction is regulated by trans-homophilic cell
adhesion (PubMed:19948503). Isoform 1 interacts (via cytoplasmic
domain) with LCK; mediates phosphorylation at Tyr-488 and Tyr-513
resulting in PTPN6 association. Isoform 1 interacts with PTPN6;
this interaction is phosphorylation-dependent and causes a
profound decrease in TCR stimulation-induced CD247 and ZAP70
phosphorylation. Isoform 1 interacts with TCR/CD3 complex through
TCR beta chain and CD3E; colocalizes at the cell surface and upon
stimulation of the TCR/CD3 complex recuits PTPN6 in the TCR/CD3
complex, resulting in dephosphorylation of CD247 and ZAP70 (By
similarity). Isoform 1 interacts (via cytoplasmic domain) with
SHC1 (via SH2 domain); SHC1 mediates interaction with INSR or EGFR
in a Ser-503 phosphorylation-dependent manner (PubMed:11694516).
Isoform 1 interacts with EGFR; the interaction is indirect
(PubMed:15467833). Isoform 1 interacts with CSF3R; down-regulates
the CSF3R-STAT3 pathway through recruitment of PTPN6 that
dephosphorylates CSF3R. Isoform 1 (phosphorylated form) interacts
with TLR4 and SYK; recruits PTPN6 that dephosphorylates SYK,
reducing the production of reactive oxygen species (ROS) and
lysosome disruption, leading to a reduction of the inflammasome
activity (By similarity). Isoform 1 interacts with FLNA; inhibits
cell migration and cell scattering by interfering with the
interaction of FLNA with RALA (PubMed:16291724). Isoform 1
interacts (via cytoplasmic domain) with PXN; the interaction is
phosphotyrosyl-dependent. Isoform 1 interacts with KLRK1; recruits
PTPN6 that dephosphorylates VAV1. Isoform 1 interacts with CEACAM8
(By similarity). Isoform 1 interacts with FASN; this interaction
is insulin and phosphorylation-dependent; reduces fatty-acid
synthase activity (PubMed:16054098). Interacts (via Ig-like V-
type) with HAVCR2 (via Ig-like V-type); facilitates the maturation
and cell surface expression of HAVCR2 thereby regulating T-cell
tolerance induction. Isoform 2 interacts (via the cytoplasmic
domain) with ANXA2; this interaction is regulated by
phosphorylation and appears in the AIIt complex. Interacts (via
Lewis X moieties) with CD209 (via C-type lectin domain); this
interaction is regulated by the glycosylation pattern of CEACAM1
on cell types and regulates contact between dendritic cells and
neutrophils (By similarity). {ECO:0000250|UniProtKB:P13688,
ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:11694516,
ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16054098,
ECO:0000269|PubMed:16291724, ECO:0000269|PubMed:19948503,
ECO:0000269|PubMed:2373740, ECO:0000269|PubMed:8576129,
ECO:0000269|PubMed:8831574, ECO:0000269|PubMed:9003371}.
-!- INTERACTION:
P29353:SHC1 (xeno); NbExp=3; IntAct=EBI-8032148, EBI-78835;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7518458,
ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:8536699,
ECO:0000269|PubMed:9003371, ECO:0000269|PubMed:9712832}; Single-
pass type I membrane protein. Lateral cell membrane
{ECO:0000269|PubMed:7774714}. Apical cell membrane
{ECO:0000269|PubMed:7774714}. Basal cell membrane
{ECO:0000269|PubMed:7774714}. Cell junction
{ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:9003371}. Cell
junction, adherens junction {ECO:0000269|PubMed:19948503}.
Note=Canalicular domain of hepatocyte plasma membranes
(PubMed:8513803). Found as a mixture of monomer, dimer and
oligomer in the plasma membrane. Occurs predominantly as cis-
dimers and/or small cis-oligomers in the cell junction regions
(PubMed:19948503). Found as dimer in the solution
(PubMed:9003371). Predominantly localized to the lateral cell
membranes (PubMed:7774714). {ECO:0000269|PubMed:19948503,
ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:8513803,
ECO:0000269|PubMed:9003371}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:9003371}; Single-
pass type I membrane protein. Lateral cell membrane
{ECO:0000269|PubMed:7774714}. Apical cell membrane
{ECO:0000269|PubMed:7774714}. Basal cell membrane
{ECO:0000269|PubMed:7774714}. Cell junction
{ECO:0000269|PubMed:19948503}. Cell junction, adherens junction
{ECO:0000269|PubMed:19948503}. Cytoplasmic vesicle, secretory
vesicle {ECO:0000250|UniProtKB:P13688}. Note=Predominantly
localized to the lateral cell membranes (PubMed:7774714). Found as
a mixture of monomer, dimer and oligomer in the plasma membrane.
Occurs predominantly as cis-dimers and/or small cis-oligomers in
the cell junction regions (PubMed:19948503). Co-localizes with
ANXA2 in secretory vesicles and with S100A10/p11 at the plasma
membrane (By similarity). {ECO:0000250|UniProtKB:P13688,
ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:7774714}.
-!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
{ECO:0000250|UniProtKB:P31809}; Single-pass type I membrane
protein {ECO:0000305}. Apical cell membrane
{ECO:0000250|UniProtKB:P31809}; Single-pass type I membrane
protein {ECO:0000305}. Note=Colocalizes with CEACAM20 at the
apical brush border of intestinal cells.
{ECO:0000250|UniProtKB:P31809}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=For each isoform it exists 2 allelic variants, named a
and b. The allelic variants differ in 16 amino acids in the
Ig-like V-type domain. {ECO:0000305|PubMed:8504806};
Name=1; Synonyms=CEACAM1-4L {ECO:0000303|PubMed:11501563}, C-CAM1,
L-form Cell-CAM105;
IsoId=P16573-1; Sequence=Displayed;
Note=Allele a.;
Name=2; Synonyms=CEACAM1-4S {ECO:0000303|PubMed:11501563}, C-CAM2,
S-form Cell-CAM105;
IsoId=P16573-2; Sequence=VSP_002504, VSP_002505;
Note=Allele a.;
-!- TISSUE SPECIFICITY: Expressed in epithelia, vessel endothelia,
leukocytes and platelets. Isoform 1 and isoform 2 are highly
expressed in liver and intestine, moderately in lung, and weakly
in muscle, kidney, and spleen (PubMed:8454589). Expressed in
granulocytes, lymphocytes, granulocytes, B cells, and T-cells
(PubMed:11994468). {ECO:0000269|PubMed:11994468,
ECO:0000269|PubMed:8454589}.
-!- DOMAIN: Ig-like V-type domain mediates trans-homophilic cell
adhesion through homodimerization and this active process is
regulated by tyrosine kinase, PTPN11 AND PTPN6. Ig-like C2-type
and/or cytoplasmic domains mediate cis-dimer/oligomer.
{ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:8831574}.
-!- PTM: Isoform 1: Phosphorylated on serine and tyrosine
(PubMed:8420979). Isoform 1 is phosphorylated on tyrosine by Src
family kinases like SRC and LCK and by receptor like CSF3R, EGFR
and INSR upon stimulation (PubMed:15467833, PubMed:7626603,
PubMed:9712832, PubMed:16054098). Phosphorylated at Ser-503;
mediates activity. Phosphorylated at Tyr-488; regulates activity
(PubMed:7518458). Phosphorylated at Tyr-488 by EGFR and INSR upon
stimulation; this phosphorylation is Ser-503-phosphorylation-
dependent; mediates cellular internalization; increases
interaction with FASN (PubMed:16054098, PubMed:15467833,
PubMed:7626603, PubMed:9712832). Phosphorylated at Tyr-488 and
Tyr-513 by LCK; mediates PTPN6 association and is regulated by
homophilic ligation of CEACAM1 in the absence of T-cell activation
(By similarity). Phosphorylated at Tyr-513; mediates interaction
with PTPN11 (By similarity). {ECO:0000250|UniProtKB:P13688,
ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:15467833,
ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7518458,
ECO:0000269|PubMed:7626603, ECO:0000269|PubMed:8420979,
ECO:0000269|PubMed:9712832}.
-!- PTM: Isoform 2: Phosphorylated on serine and threonine.
{ECO:0000269|PubMed:8420979}.
-!- POLYMORPHISM: There are two different allelic variants of CEACAM1,
named a and b. The allelic variants differ in 16 amino acids in
the Ig-like V-type domain. The sequence shown here, corresponds to
allele A. {ECO:0000269|PubMed:8504806}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA16783.1; Type=Miscellaneous discrepancy; Note=Dubious isoform. Probable cloning artifact lacking polyadenylation evidence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J04963; AAA41104.1; -; mRNA.
EMBL; Z12019; CAA78054.1; -; mRNA.
EMBL; M92848; AAA16783.1; ALT_SEQ; mRNA.
EMBL; X71122; CAA50435.1; -; mRNA.
EMBL; X91137; CAA62577.1; -; mRNA.
EMBL; AC134759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473979; EDM08020.1; -; Genomic_DNA.
EMBL; BC061740; AAH61740.1; -; mRNA.
PIR; A44783; A44783.
PIR; S23969; S23969.
PIR; S68177; S68177.
RefSeq; NP_001029032.1; NM_001033860.1. [P16573-1]
RefSeq; NP_001029033.1; NM_001033861.1.
RefSeq; NP_001029034.1; NM_001033862.1. [P16573-2]
RefSeq; NP_113943.1; NM_031755.2.
UniGene; Rn.91235; -.
ProteinModelPortal; P16573; -.
IntAct; P16573; 1.
MINT; MINT-220849; -.
STRING; 10116.ENSRNOP00000046654; -.
TCDB; 8.A.23.1.4; the basigin (basigin) family.
iPTMnet; P16573; -.
PhosphoSitePlus; P16573; -.
PaxDb; P16573; -.
PRIDE; P16573; -.
Ensembl; ENSRNOT00000051892; ENSRNOP00000046654; ENSRNOG00000020578. [P16573-1]
Ensembl; ENSRNOT00000090629; ENSRNOP00000074820; ENSRNOG00000020578. [P16573-2]
GeneID; 81613; -.
KEGG; rno:81613; -.
UCSC; RGD:67396; rat. [P16573-1]
CTD; 634; -.
RGD; 67396; Ceacam1.
eggNOG; ENOG410IFE1; Eukaryota.
eggNOG; ENOG410YR1P; LUCA.
GeneTree; ENSGT00760000119187; -.
HOGENOM; HOG000233417; -.
HOVERGEN; HBG007922; -.
InParanoid; P16573; -.
KO; K06499; -.
OMA; PQIKASK; -.
TreeFam; TF336859; -.
Reactome; R-RNO-1566977; Fibronectin matrix formation.
Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P16573; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000020578; -.
ExpressionAtlas; P16573; baseline and differential.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0015125; F:bile acid transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0015721; P:bile acid and bile salt transport; IDA:UniProtKB.
GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IDA:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:UniProtKB.
GO; GO:0038158; P:granulocyte colony-stimulating factor signaling pathway; ISS:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
GO; GO:1901143; P:insulin catabolic process; IMP:UniProtKB.
GO; GO:0038016; P:insulin receptor internalization; IDA:UniProtKB.
GO; GO:0043318; P:negative regulation of cytotoxic T cell degranulation; ISS:UniProtKB.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:UniProtKB.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISS:UniProtKB.
GO; GO:2000346; P:negative regulation of hepatocyte proliferation; IMP:UniProtKB.
GO; GO:0032692; P:negative regulation of interleukin-1 production; ISS:UniProtKB.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0002859; P:negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; ISS:UniProtKB.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; ISS:UniProtKB.
GO; GO:1903387; P:positive regulation of homophilic cell adhesion; IDA:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:MGI.
GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
GO; GO:0070207; P:protein homotrimerization; IMP:UniProtKB.
GO; GO:0060312; P:regulation of blood vessel remodeling; ISS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0045601; P:regulation of endothelial cell differentiation; ISS:UniProtKB.
GO; GO:0010594; P:regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:1903385; P:regulation of homophilic cell adhesion; IDA:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:1903670; P:regulation of sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:RGD.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Pyrrolidone carboxylic acid; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 519 Carcinoembryonic antigen-related cell
adhesion molecule 1.
/FTId=PRO_0000014564.
TOPO_DOM 35 425 Extracellular. {ECO:0000305}.
TRANSMEM 426 446 Helical. {ECO:0000255}.
TOPO_DOM 447 519 Cytoplasmic. {ECO:0000305}.
DOMAIN 42 140 Ig-like V-type.
DOMAIN 147 232 Ig-like C2-type 1.
DOMAIN 237 317 Ig-like C2-type 2.
DOMAIN 325 403 Ig-like C2-type 3.
REGION 39 142 Required for homophilic binding.
{ECO:0000269|PubMed:8831574}.
REGION 445 457 Interaction with calmodulin.
{ECO:0000269|PubMed:8576129}.
REGION 447 519 Interaction with FLNA.
{ECO:0000269|PubMed:16291724}.
REGION 484 519 Required for interaction with PTPN11 and
PTPN6 and for control of phosphorylation
level. {ECO:0000250|UniProtKB:P31809}.
REGION 513 516 Essential for interaction with PTPN11 and
PTPN6. {ECO:0000250|UniProtKB:P31809}.
MOD_RES 35 35 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P13688}.
MOD_RES 488 488 Phosphotyrosine; by SRC, LCK, INSR and
EGFR. {ECO:0000269|PubMed:15467833,
ECO:0000269|PubMed:16054098,
ECO:0000269|PubMed:7518458,
ECO:0000269|PubMed:7626603,
ECO:0000269|PubMed:9712832}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000269|PubMed:16054098,
ECO:0000269|PubMed:7518458}.
MOD_RES 513 513 Phosphotyrosine; by INSR, SRC and LCK.
{ECO:0000269|PubMed:16054098}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000250|UniProtKB:P31809}.
DISULFID 167 215 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 259 299 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 344 392 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 455 458 GSDH -> SGSF (in isoform 2).
{ECO:0000303|PubMed:1637321,
ECO:0000303|PubMed:8504806,
ECO:0000303|PubMed:8536699}.
/FTId=VSP_002504.
VAR_SEQ 459 519 Missing (in isoform 2).
{ECO:0000303|PubMed:1637321,
ECO:0000303|PubMed:8504806,
ECO:0000303|PubMed:8536699}.
/FTId=VSP_002505.
VARIANT 49 49 K -> S (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 55 55 A -> T (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 70 70 G -> V (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 73 73 L -> T (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 74 74 N -> G (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 75 75 P -> L (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 76 76 D -> N (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 86 86 D -> S (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 88 88 M -> T (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 90 90 K -> Q (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 92 92 G -> E (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 99 99 E -> V (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 118 118 R -> G (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 119 119 A -> P (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 125 125 F -> I (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
VARIANT 127 127 Q -> K (in allele b).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1637321,
ECO:0000269|PubMed:8504806}.
MUTAGEN 488 488 Y->F: Phosphorylated on serine. Decreases
bile acid transport Doesn't
phosphorylated by EGFR. Doesn't increase
interaction with SHC1. Completely
inhibits insulin-stimulated
phosphorylation. No effect on INSR
internalization and INS degradation.
Prevents CEACAM1 phosphorylation and the
increase in its binding to FASN in the
presence of INSR. No effect on cell-
surface expression in response to INS.
Abolishes phosphorylation by INSR.
Abolishes indirect interaction with INSR.
{ECO:0000269|PubMed:15467833,
ECO:0000269|PubMed:16054098,
ECO:0000269|PubMed:7518458,
ECO:0000269|PubMed:7592607,
ECO:0000269|PubMed:7626603,
ECO:0000269|PubMed:9712832}.
MUTAGEN 502 503 TS->AA: Phosphorylated on tyrosine.
Impairs bile acid transport.
{ECO:0000269|PubMed:7518458}.
MUTAGEN 503 503 S->A: Abolishes phosphorylation by EGFR.
Reduces interaction with SHC1. Completely
inhibits insulin-stimulated
phosphorylation. No effect on INSR
internalization and INS degradation. In
L-SACC1; completely inhibits insulin-
stimulated phosphorylation; develops
hyperinsulinemia resulting from impaired
insulin clearance; the hyperinsulinemia
causes secondary insulin resistance with
impaired glucose tolerance and random,
but not fasting, hyperglycemia; insulin
doesn't significantly decrease FASN
activity in liver. Prevents CEACAM1
phosphorylation and the increase in its
binding to FASN in the presence of INSR.
No effect on cell-surface expression in
response to INS.
{ECO:0000269|PubMed:11694516,
ECO:0000269|PubMed:11850617,
ECO:0000269|PubMed:15467833,
ECO:0000269|PubMed:16054098,
ECO:0000269|PubMed:7592607,
ECO:0000269|PubMed:7626603,
ECO:0000269|PubMed:9712832}.
MUTAGEN 503 503 S->D: Preserves the ability of INSR to
induce CEACAM1 phosphorylation.
{ECO:0000269|PubMed:16054098}.
MUTAGEN 513 513 Y->F: Increases INSR internalization and
INS degradation. Phosphorylated by INSR.
Prevents the increase in CEACAM1 binding
to FASN by INSR. Decreases cell-surface
expression in response to INS. Doesn't
affect phosphorylation by INSR.
{ECO:0000269|PubMed:16054098,
ECO:0000269|PubMed:7592607,
ECO:0000269|PubMed:9712832}.
SEQUENCE 519 AA; 57410 MW; 9EFE74FD565E7C29 CRC64;
MELASARLLR GQIPWRGLLL TASLLTYWSP LTTAQVTVDA VPPNVVEEKS VLLLAHNLPQ
EFQVFYWYKG TTLNPDSEIA RYIRSDNMSK TGPAYSGRET IYSNGSLFFQ NVNKTDERAY
TLSVFDQQFN PIQTSVQFRV YPALQKPNVT GNNSNPMEGE PFVSLMCEPY TNNTSYLWSR
NGESLSEGDR VTFSEGNRTL TLLNVRRTDK GYYECEARNP ATFNRSDPFN LDVIYGPDAP
VISPPDIYLH QGSNLNLSCH ADSNPPAQYF WLINEKLQTS SQELFISNIT TNNSGTYACF
VNNTVTGLSR TTVKNITVFE PVTQPSIQIT NTTVKELGSV TLTCFSKDTG VSVRWLFNSQ
SLQLTDRMTL SQDNSTLRID PIKREDAGDY QCEISNPVSF RISHPIKLDV IPDPTQGNSG
LSEGAIAGIV IGSVAGVALI AALAYFLYSR KTGGGSDHRD LTEHKPSTSS HNLGPSDDSP
NKVDDVSYSV LNFNAQQSKR PTSASSSPTE TVYSVVKKK


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