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Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)

 CEAM1_MOUSE             Reviewed;         521 AA.
P31809; Q61350; Q61353;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
27-SEP-2017, entry version 161.
RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 1 {ECO:0000250|UniProtKB:P13688};
AltName: Full=Biliary glycoprotein 1 {ECO:0000250|UniProtKB:P13688};
Short=BGP-1;
AltName: Full=Biliary glycoprotein D;
AltName: Full=MHVR1;
AltName: Full=Murine hepatitis virus receptor;
Short=MHV-R;
AltName: CD_antigen=CD66a;
Flags: Precursor;
Name=Ceacam1 {ECO:0000312|MGI:MGI:1347245};
Synonyms=Bgp {ECO:0000303|PubMed:8500759}, Bgp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH MHV SPIKE
GLYCOPROTEIN (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL
INFECTION).
STRAIN=BALB/cJ, and CD-1; TISSUE=Colon, and Liver;
PubMed=1719235;
Dveksler G.S., Pensiero M.N., Cardellichio C.B., Williams R.K.,
Jiang G.-S., Holmes K.V., Dieffenbach C.W.;
"Cloning of the mouse hepatitis virus (MHV) receptor: expression in
human and hamster cell lines confers susceptibility to MHV.";
J. Virol. 65:6881-6891(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
FUNCTION.
STRAIN=CD-1; TISSUE=Colon;
PubMed=1633107;
McCuaig K., Turbide C., Beauchemin N.;
"mmCGM1a: a mouse carcinoembryonic antigen gene family member,
generated by alternative splicing, functions as an adhesion
molecule.";
Cell Growth Differ. 3:165-174(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND ALTERNATIVE
SPLICING.
STRAIN=CD-1; TISSUE=Colon;
PubMed=8500759; DOI=10.1016/0378-1119(93)90716-G;
McCuaig K., Rosenberg M., Nedellec P., Turbide C., Beauchemin N.;
"Expression of the Bgp gene and characterization of mouse colon
biliary glycoprotein isoforms.";
Gene 127:173-183(1993).
[4]
PROTEIN SEQUENCE OF 35-59.
PubMed=1648219; DOI=10.1073/pnas.88.13.5533;
Williams R.K., Jiang G.-S., Holmes K.V.;
"Receptor for mouse hepatitis virus is a member of the
carcinoembryonic antigen family of glycoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 88:5533-5536(1991).
[5]
PROTEIN SEQUENCE OF 116-130, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND INTERACTION WITH MHV
SPIKE GLYCOPROTEIN (MICROBIAL INFECTION).
STRAIN=CD-1; TISSUE=Colon;
PubMed=8380065;
Dveksler G.S., Dieffenback C.B., Cardellichio C.B., McCuaig K.,
Pensiero M.N., Jiang G.-S., Beauchemin N., Holmes K.V.;
"Several members of the mouse carcinoembryonic antigen-related
glycoprotein family are functional receptors for the coronavirus mouse
hepatitis virus-A59.";
J. Virol. 67:1-8(1993).
[7]
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).
[8]
INTERACTION WITH PTPN11 AND PTPN6, PHOSPHORYLATION AT TYR-488 AND
TYR-515 BY SRC, REGION, AND MUTAGENESIS OF TYR-488; TYR-515;
519-LYS--LYS-521 AND VAL-518.
PubMed=9867848; DOI=10.1074/jbc.274.1.335;
Huber M., Izzi L., Grondin P., Houde C., Kunath T., Veillette A.,
Beauchemin N.;
"The carboxyl-terminal region of biliary glycoprotein controls its
tyrosine phosphorylation and association with protein-tyrosine
phosphatases SHP-1 and SHP-2 in epithelial cells.";
J. Biol. Chem. 274:335-344(1999).
[9]
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).
[10]
INTERACTION WITH SHC1, AND FUNCTION.
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).
[11]
FUNCTION (MICROBIAL INFECTION).
PubMed=15331748; DOI=10.1128/JVI.78.18.10156-10165.2004;
Hemmila E., Turbide C., Olson M., Jothy S., Holmes K.V.,
Beauchemin N.;
"Ceacam1a-/- mice are completely resistant to infection by murine
coronavirus mouse hepatitis virus A59.";
J. Virol. 78:10156-10165(2004).
[12]
FUNCTION, AND MUTAGENESIS OF TYR-488 AND TYR-515.
PubMed=17081782; DOI=10.1016/j.immuni.2006.08.026;
Nagaishi T., Pao L., Lin S.H., Iijima H., Kaser A., Qiao S.W.,
Chen Z., Glickman J., Najjar S.M., Nakajima A., Neel B.G.,
Blumberg R.S.;
"SHP1 phosphatase-dependent T cell inhibition by CEACAM1 adhesion
molecule isoforms.";
Immunity 25:769-781(2006).
[13]
MUTAGENESIS OF TYR-488 AND SER-503, AND FUNCTION.
PubMed=16680193; DOI=10.1172/JCI24340;
Horst A.K., Ito W.D., Dabelstein J., Schumacher U., Sander H.,
Turbide C., Bruemmer J., Meinertz T., Beauchemin N., Wagener C.;
"Carcinoembryonic antigen-related cell adhesion molecule 1 modulates
vascular remodeling in vitro and in vivo.";
J. Clin. Invest. 116:1596-1605(2006).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[15]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=18544705; DOI=10.2337/db08-0379;
DeAngelis A.M., Heinrich G., Dai T., Bowman T.A., Patel P.R.,
Lee S.J., Hong E.G., Jung D.Y., Assmann A., Kulkarni R.N., Kim J.K.,
Najjar S.M.;
"Carcinoembryonic antigen-related cell adhesion molecule 1: a link
between insulin and lipid metabolism.";
Diabetes 57:2296-2303(2008).
[16]
DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19008452; DOI=10.1182/blood-2008-06-165043;
Wong C., Liu Y., Yip J., Chand R., Wee J.L., Oates L., Nieswandt B.,
Reheman A., Ni H., Beauchemin N., Jackson D.E.;
"CEACAM1 negatively regulates platelet-collagen interactions and
thrombus growth in vitro and in vivo.";
Blood 113:1818-1828(2009).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71; ASN-89; ASN-317;
ASN-333; ASN-375 AND ASN-376.
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).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION BY
CSF3R, AND INTERACTION WITH CSF3R.
PubMed=21029969; DOI=10.1016/j.immuni.2010.10.009;
Pan H., Shively J.E.;
"Carcinoembryonic antigen-related cell adhesion molecule-1 regulates
granulopoiesis by inhibition of granulocyte colony-stimulating factor
receptor.";
Immunity 33:620-631(2010).
[20]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF TYR-488 AND TYR-515,
AND PHOSPHORYLATION AT TYR-488 AND TYR-515.
PubMed=21081647; DOI=10.1242/jcs.073635;
Nouvion A.L., Oubaha M., Leblanc S., Davis E.C., Jastrow H.,
Kammerer R., Breton V., Turbide C., Ergun S., Gratton J.P.,
Beauchemin N.;
"CEACAM1: a key regulator of vascular permeability.";
J. Cell Sci. 123:4221-4230(2010).
[21]
FUNCTION.
PubMed=22962327; DOI=10.1161/ATVBAHA.112.300015;
Bickert T., Marshall R.P., Zhang Z., Ludewig P., Binder M., Klinke A.,
Rottbauer W., Amling M., Wagener C., Ito W.D., Horst A.K.;
"Acceleration of collateral development by carcinoembryonic antigen-
related cell adhesion molecule 1 expression on CD11b/[?]Gr-1[?]
myeloid cells--brief report.";
Arterioscler. Thromb. Vasc. Biol. 32:2566-2568(2012).
[22]
TISSUE SPECIFICITY, FUNCTION, AND INDUCTION.
PubMed=23123061; DOI=10.1016/j.immuni.2012.07.016;
Chen L., Chen Z., Baker K., Halvorsen E.M., da Cunha A.P., Flak M.B.,
Gerber G., Huang Y.H., Hosomi S., Arthur J.C., Dery K.J., Nagaishi T.,
Beauchemin N., Holmes K.V., Ho J.W., Shively J.E., Jobin C.,
Onderdonk A.B., Bry L., Weiner H.L., Higgins D.E., Blumberg R.S.;
"The short isoform of the CEACAM1 receptor in intestinal T cells
regulates mucosal immunity and homeostasis via Tfh cell induction.";
Immunity 37:930-946(2012).
[23]
FUNCTION, INTERACTION WITH SYK, PTPN6; TLR4 AND LYN, AND MUTAGENESIS
OF TYR-488 AND TYR-515.
PubMed=22496641; DOI=10.1371/journal.ppat.1002597;
Lu R., Pan H., Shively J.E.;
"CEACAM1 negatively regulates IL-1beta production in LPS activated
neutrophils by recruiting SHP-1 to a SYK-TLR4-CEACAM1 complex.";
PLoS Pathog. 8:E1002597-E1002597(2012).
[24]
FUNCTION, AND INDUCTION.
PubMed=23696226; DOI=10.1002/eji.201242676;
Hosomi S., Chen Z., Baker K., Chen L., Huang Y.H., Olszak T.,
Zeissig S., Wang J.H., Mandelboim O., Beauchemin N., Lanier L.L.,
Blumberg R.S.;
"CEACAM1 on activated NK cells inhibits NKG2D-mediated cytolytic
function and signaling.";
Eur. J. Immunol. 43:2473-2483(2013).
[25]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND
FUNCTION.
PubMed=25490771; DOI=10.1371/journal.pone.0114360;
Heckt T., Bickert T., Jeschke A., Seitz S., Schulze J., Ito W.D.,
Zimmermann W., Amling M., Schinke T., Horst A.K., Keller J.;
"Increased osteoclastogenesis in mice lacking the carcinoembryonic
antigen-related cell adhesion molecule 1.";
PLoS ONE 9:E114360-E114360(2014).
[26]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=25908210; DOI=10.1111/gtc.12247;
Kitamura Y., Murata Y., Park J.H., Kotani T., Imada S., Saito Y.,
Okazawa H., Azuma T., Matozaki T.;
"Regulation by gut commensal bacteria of carcinoembryonic antigen-
related cell adhesion molecule expression in the intestinal
epithelium.";
Genes Cells 20:578-589(2015).
[27]
INTERACTION WITH HAVCR2.
PubMed=25363763; DOI=10.1038/nature13848;
Huang Y.H., Zhu C., Kondo Y., Anderson A.C., Gandhi A., Russell A.,
Dougan S.K., Petersen B.S., Melum E., Pertel T., Clayton K.L.,
Raab M., Chen Q., Beauchemin N., Yazaki P.J., Pyzik M.,
Ostrowski M.A., Glickman J.N., Rudd C.E., Ploegh H.L., Franke A.,
Petsko G.A., Kuchroo V.K., Blumberg R.S.;
"CEACAM1 regulates TIM-3-mediated tolerance and exhaustion.";
Nature 517:386-390(2015).
[28]
X-RAY CRYSTALLOGRAPHY (3.32 ANGSTROMS) OF 35-236 (ISOFORM 3),
GLYCOSYLATION AT ASN-71; ASN-89; ASN-104 AND ASN-333, DISULFIDE BOND,
AND INTERACTION WITH MURINE CORONAVIRUS MHV S1 SPIKE GLYCOPROTEIN
(MICROBIAL INFECTION).
PubMed=11980704; DOI=10.1093/emboj/21.9.2076;
Tan K., Zelus B.D., Meijers R., Liu J.-H., Bergelson J.M., Duke N.,
Zhang R., Joachimiak A., Holmes K.V., Wang J.-H.;
"Crystal structure of murine sCEACAM1a[1,4]: a coronavirus receptor in
the CEA family.";
EMBO J. 21:2076-2086(2002).
-!- FUNCTION: Isoform 1: Cell adhesion protein that mediates
homophilic cell adhesion in a calcium-independent manner (By
similarity). Plays a role as coinhibitory receptor in immune
response, insulin action and functions also as an activator during
angiogenesis (PubMed:16680193, PubMed:17081782, PubMed:18544705,
PubMed:21029969, PubMed:21081647, PubMed:22496641,
PubMed:22962327, PubMed:23696226). Its coinhibitory receptor
function is phosphorylation- and PTPN6 -dependent, which in turn,
suppress signal transduction of associated receptors by
dephosphorylation of their downstream effectors (PubMed:17081782,
PubMed:21029969, PubMed:22496641). Plays a role in immune
response, of T-cells, natural killer (NK) and neutrophils
(PubMed:17081782, PubMed:23696226, PubMed:22496641,
PubMed:21029969). 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 (PubMed:22496641). 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 (PubMed:17081782). 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
(PubMed:23696226). 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 (PubMed:22496641). Downregulates neutrophil
production by acting as a coinhibitory receptor for CSF3R by
downregulating the CSF3R-STAT3 pathway through recruitment of
PTPN6 that dephosphorylates CSF3R (PubMed:21029969). Also
regulates insulin action by promoting INS clearance and regulating
lipogenesis in liver through regulating insulin signaling
(PubMed:18544705). Upon INS stimulation, undergoes phosphorylation
by INSR leading to INS clearance by increasing receptor-mediated
insulin endocytosis. 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. 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 (By
similarity). 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
(PubMed:16680193, PubMed:22962327). Also regulates vascular
permeability through the VEGFR2 signaling pathway resulting in
control of nitric oxide production (PubMed:21081647).
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 (PubMed:19008452).
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 (By similarity). Negatively
regulates osteoclastogenesis (PubMed:25490771).
{ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573,
ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16680193,
ECO:0000269|PubMed:17081782, ECO:0000269|PubMed:18544705,
ECO:0000269|PubMed:19008452, ECO:0000269|PubMed:21029969,
ECO:0000269|PubMed:21081647, ECO:0000269|PubMed:22496641,
ECO:0000269|PubMed:22962327, ECO:0000269|PubMed:23696226,
ECO:0000269|PubMed:25490771}.
-!- FUNCTION: Isoform 2: Cell adhesion protein that mediates
homophilic cell adhesion in a calcium-independent manner
(PubMed:1633107). Promotes populations of T-cells regulating IgA
production and secretion associated with control of the commensal
microbiota and resistance to enteropathogens (PubMed:23123061).
{ECO:0000269|PubMed:1633107, ECO:0000269|PubMed:23123061}.
-!- FUNCTION: (Microbial infection) In case of murine coronavirus
(MHV) infection, serves as receptor for MHV S1 spike glycoprotein.
{ECO:0000269|PubMed:15331748, ECO:0000269|PubMed:1719235}.
-!- SUBUNIT: (Microbial infection) Interacts with MHV S1 spike
glycoprotein. {ECO:0000269|PubMed:11980704,
ECO:0000269|PubMed:1719235, ECO:0000269|PubMed:8380065}.
-!- SUBUNIT: Monomer. Oligomer. Heterodimer. Homodimer. 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. Interacts
(via cytoplasmic domain) with calmodulin in a calcium dependent
manner; reduces homophilic cell adhesion through dissociation of
dimer (By similarity). 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:9867848). Isoform 1 interacts with LYN
(PubMed:22496641). Isoform 1 interacts (via cytoplasmic domain)
with SRC (via SH2 domain); this interaction is regulated by trans-
homophilic cell adhesion (By similarity). Isoform 1 interacts with
LCK; mediates phosphorylation at Tyr-488 and Tyr-515 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:15467833).
Isoform 1 interacts with EGFR; the interaction is indirect (By
similarity). Isoform 1 interacts with CSF3R; down-regulates the
CSF3R-STAT3 pathway through recruitment of PTPN6 that
dephosphorylates CSF3R (PubMed:21029969). 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 (PubMed:22496641). Isoform
1 interacts with FLNA; inhibits cell migration and cell scattering
by interfering with the interaction of FLNA with RALA. 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 (By similarity). 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 (By similarity) (PubMed:25363763). 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:P16573,
ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:21029969,
ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:25363763,
ECO:0000269|PubMed:9867848}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:19008452, ECO:0000269|PubMed:8380065}; Single-
pass type I membrane protein {ECO:0000250|UniProtKB:P16573}.
Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell
membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane
{ECO:0000250|UniProtKB:P16573}. Cell junction
{ECO:0000250|UniProtKB:P16573}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:P16573}. Note=Canalicular domain of
hepatocyte plasma membranes. 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.
Found as dimer in the solution. Predominantly localized to the
lateral cell membranes. {ECO:0000250|UniProtKB:P16573}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:1633107, ECO:0000269|PubMed:8380065}; Single-
pass type I membrane protein {ECO:0000250|UniProtKB:P16573}.
Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell
membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane
{ECO:0000250|UniProtKB:P16573}. Cell junction
{ECO:0000250|UniProtKB:P16573}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:P16573}. Cytoplasmic vesicle, secretory
vesicle {ECO:0000250|UniProtKB:P13688}. Note=Predominantly
localized to the lateral cell membranes. 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 (By similarity). Co-localizes with ANXA2 in
secretory vesicles and with S100A10/p11 at the plasma membrane (By
similarity). {ECO:0000250|UniProtKB:P13688,
ECO:0000250|UniProtKB:P16573}.
-!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
{ECO:0000269|PubMed:25908210}; Single-pass type I membrane protein
{ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:25908210};
Single-pass type I membrane protein {ECO:0000305}.
Note=Colocalizes with CEACAM20 at the apical brush border of
intestinal cells. {ECO:0000269|PubMed:25908210}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Ceacam1-4L {ECO:0000303|PubMed:11501563}, Bgpd;
IsoId=P31809-1; Sequence=Displayed;
Name=2; Synonyms=Ceacam1-4S {ECO:0000303|PubMed:11501563}, Bgpa,
mmCGM1a;
IsoId=P31809-2; Sequence=VSP_002484, VSP_002485;
Name=3; Synonyms=Ceacam1-2L {ECO:0000303|PubMed:11501563}, Bgpg;
IsoId=P31809-3; Sequence=VSP_036040, VSP_036041;
Name=4; Synonyms=Ceacam1-2S {ECO:0000303|PubMed:11501563}, Bgpc;
IsoId=P31809-4; Sequence=VSP_058517, VSP_002484, VSP_002485;
-!- TISSUE SPECIFICITY: Expressed in granulocytes, lymphocytes,
granulocytes, B cells, and T-cells (PubMed:11994468). Expressed in
bone. Highly expressed in liver and femur (PubMed:25490771).
Highly expressed in neutrophils, and to a lesser extent
inmonocytes, and macrophages. Slightly higher expressed in
peripheral blood neutrophils (PBNs) (PubMed:21029969). Intestinal
T-cells predominantly express isoform 2 while extraintestinal T-
cells mainly express isoform 1 (PubMed:23123061). Expressed in
small intestine and colon (PubMed:25908210).
{ECO:0000269|PubMed:11994468, ECO:0000269|PubMed:21029969,
ECO:0000269|PubMed:23123061, ECO:0000269|PubMed:25490771,
ECO:0000269|PubMed:25908210}.
-!- DEVELOPMENTAL STAGE: Expression increases during the early stages
of osteoblast differentiation, and decreases towards terminal
osteoblast differentiation. In addition, expression markedly
decreases during the course of osteoclastogenesis.
{ECO:0000269|PubMed:25490771}.
-!- INDUCTION: In intestinal epithelium, up-regulated in the presence
of Gram-positive commensal gut bacteria (PubMed:25908210). May
also be up-regulated by interferon gamma (IFNG) and TNF (TNF-
alpha) (PubMed:25908210). Isoform 2: Expression is promoted and
maintained by the mucosal environment (PubMed:23123061). Induced
by IL2 on natural killer cell (PubMed:23696226).
{ECO:0000269|PubMed:23123061, ECO:0000269|PubMed:23696226,
ECO:0000269|PubMed:25908210}.
-!- 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:0000250|UniProtKB:P16573}.
-!- PTM: Isoform 1: Phosphorylated on serine and tyrosine (By
similarity). 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:9867848, PubMed:21029969). Phosphorylated
at Ser-503; mediates activity. Phosphorylated at Tyr-488;
regulates activity (By similarity). Phosphorylated at Tyr-488 by
EGFR and INSR upon stimulation; this phosphorylation is Ser-503-
phosphorylation-dependent; mediates cellular internalization;
increases interaction with FASN (By similarity). Phosphorylated at
Tyr-488 and Tyr-515 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-515;
mediates interaction with PTPN11 (PubMed:9867848).
{ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573,
ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:9867848}.
-!- PTM: Isoform 2: Phosphorylated on serine and threonine.
{ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573}.
-!- DISRUPTION PHENOTYPE: Knockout mice exhibit impairment of insulin
clearance and hyperinsulinemia, which cause insulin resistance;
develop insulin resistance primarily in liver (PubMed:18544705).
Display normal white blood cell, red blood cell, hemoglobin and
platelet. On the other hand, mice have a high number of
neutrophils. Display also increased thrombus growth, and enhanced
susceptibility to type I collagen induced pulmonary
thromboembolism (PubMed:19008452). Spontaneously develop systemic
neutrophilia. Upon Listeria Monocytogenes (LM) infection mice die
dramatically faster within 7 days and dispaly an improved
bacterial clearance accompanied by severe tissue damage and
necrosis in the liver (PubMed:21029969). Knockout mice present an
increased basal permeability (PubMed:21081647). Knockout mice show
a reduced bone mass namely a decreased trabecular bone volume
accompanied by a reduction in trabecular number and an increase in
trabecular separation (PubMed:25490771).
{ECO:0000269|PubMed:18544705, ECO:0000269|PubMed:19008452,
ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:21081647,
ECO:0000269|PubMed:25490771}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M77196; AAA37858.1; -; mRNA.
EMBL; X15351; CAA33409.1; -; mRNA.
EMBL; X67278; CAA47695.1; -; mRNA.
EMBL; X67279; CAA47696.1; -; mRNA.
EMBL; X67282; CAA47699.1; -; mRNA.
CCDS; CCDS20984.1; -. [P31809-1]
CCDS; CCDS20985.1; -. [P31809-3]
CCDS; CCDS39839.1; -. [P31809-2]
CCDS; CCDS85244.1; -. [P31809-4]
PIR; JC1505; WMMSR1.
PIR; JC1508; JC1508.
PIR; JC1511; JC1511.
RefSeq; NP_001034274.1; NM_001039185.1.
RefSeq; NP_001034275.1; NM_001039186.1. [P31809-2]
UniGene; Mm.322502; -.
UniGene; Mm.439731; -.
PDB; 1L6Z; X-ray; 3.32 A; A=35-416.
PDB; 3R4D; X-ray; 3.10 A; A/C=35-416.
PDBsum; 1L6Z; -.
PDBsum; 3R4D; -.
ProteinModelPortal; P31809; -.
SMR; P31809; -.
CORUM; P31809; -.
DIP; DIP-61461N; -.
IntAct; P31809; 1.
MINT; MINT-4590618; -.
STRING; 10090.ENSMUSP00000096266; -.
iPTMnet; P31809; -.
PhosphoSitePlus; P31809; -.
MaxQB; P31809; -.
PaxDb; P31809; -.
PeptideAtlas; P31809; -.
PRIDE; P31809; -.
Ensembl; ENSMUST00000098666; ENSMUSP00000096263; ENSMUSG00000074272. [P31809-2]
Ensembl; ENSMUST00000206171; ENSMUSP00000145584; ENSMUSG00000074272. [P31809-2]
Ensembl; ENSMUST00000206687; ENSMUSP00000146066; ENSMUSG00000074272. [P31809-4]
GeneID; 26365; -.
KEGG; mmu:26365; -.
UCSC; uc009fsv.1; mouse. [P31809-2]
UCSC; uc009fta.1; mouse. [P31809-1]
CTD; 634; -.
MGI; MGI:1347245; Ceacam1.
eggNOG; ENOG410IFE1; Eukaryota.
eggNOG; ENOG410YR1P; LUCA.
GeneTree; ENSGT00760000119187; -.
HOGENOM; HOG000233417; -.
HOVERGEN; HBG007922; -.
InParanoid; P31809; -.
KO; K06499; -.
PhylomeDB; P31809; -.
Reactome; R-MMU-1566977; Fibronectin matrix formation.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-6798695; Neutrophil degranulation.
EvolutionaryTrace; P31809; -.
PRO; PR:P31809; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000074272; -.
CleanEx; MM_CEACAM1; -.
ExpressionAtlas; P31809; baseline and differential.
Genevisible; P31809; MM.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
GO; GO:0031526; C:brush border membrane; IDA:MGI.
GO; GO:0030054; C:cell junction; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0060170; C:ciliary membrane; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0015125; F:bile acid transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0031005; F:filamin binding; ISO:MGI.
GO; GO:0005130; F:granulocyte colony-stimulating factor receptor binding; IPI:UniProtKB.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0035325; F:Toll-like receptor binding; IPI:UniProtKB.
GO; GO:0046790; F:virion binding; IDA:MGI.
GO; GO:0001618; F:virus receptor activity; IDA:MGI.
GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
GO; GO:0001568; P:blood vessel development; IMP:UniProtKB.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:MGI.
GO; GO:0045216; P:cell-cell junction organization; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0035726; P:common myeloid progenitor cell proliferation; IMP:UniProtKB.
GO; GO:0038158; P:granulocyte colony-stimulating factor signaling pathway; IMP:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:MGI.
GO; GO:1901143; P:insulin catabolic process; IMP:UniProtKB.
GO; GO:0038016; P:insulin receptor internalization; ISS:UniProtKB.
GO; GO:0044828; P:negative regulation by host of viral genome replication; IMP:MGI.
GO; GO:0044793; P:negative regulation by host of viral process; IDA:MGI.
GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
GO; GO:0001818; P:negative regulation of cytokine production; IMP:MGI.
GO; GO:0043318; P:negative regulation of cytotoxic T cell degranulation; ISS:UniProtKB.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:UniProtKB.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; IMP:UniProtKB.
GO; GO:2000346; P:negative regulation of hepatocyte proliferation; IMP:UniProtKB.
GO; GO:0032692; P:negative regulation of interleukin-1 production; IMP:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:MGI.
GO; GO:0046329; P:negative regulation of JNK cascade; IMP:MGI.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IMP:UniProtKB.
GO; GO:0002859; P:negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:UniProtKB.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:UniProtKB.
GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; IMP:UniProtKB.
GO; GO:0048541; P:Peyer's patch development; IMP:MGI.
GO; GO:0044794; P:positive regulation by host of viral process; IMP:MGI.
GO; GO:0070237; P:positive regulation of activation-induced cell death of T cells; IMP:MGI.
GO; GO:2000516; P:positive regulation of CD4-positive, alpha-beta T cell activation; IMP:MGI.
GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; IMP:MGI.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; IMP:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
GO; GO:0051533; P:positive regulation of NFAT protein import into nucleus; IMP:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
GO; GO:2001214; P:positive regulation of vasculogenesis; IMP:UniProtKB.
GO; GO:0060312; P:regulation of blood vessel remodeling; IMP:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
GO; GO:0045601; P:regulation of endothelial cell differentiation; IDA:UniProtKB.
GO; GO:0010594; P:regulation of endothelial cell migration; IDA: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; ISS:UniProtKB.
GO; GO:1903385; P:regulation of homophilic cell adhesion; ISS:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:1903670; P:regulation of sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0046718; P:viral entry into host cell; IDA:MGI.
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.
Pfam; PF13895; Ig_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 34 {ECO:0000269|PubMed:1648219}.
CHAIN 35 521 Carcinoembryonic antigen-related cell
adhesion molecule 1.
/FTId=PRO_0000014563.
TOPO_DOM 35 428 Extracellular. {ECO:0000255}.
TRANSMEM 429 447 Helical. {ECO:0000255}.
TOPO_DOM 448 521 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 142 Ig-like V-type.
DOMAIN 147 234 Ig-like C2-type 1.
DOMAIN 239 319 Ig-like C2-type 2.
DOMAIN 323 411 Ig-like C2-type 3.
REGION 39 142 Required for homophilic binding.
{ECO:0000250|UniProtKB:P16573}.
REGION 445 457 Interaction with calmodulin.
{ECO:0000250|UniProtKB:P16573}.
REGION 447 521 Interaction with FLNA.
{ECO:0000250|UniProtKB:P16573}.
REGION 484 521 Required for interaction with PTPN11 and
PTPN6 and for control of phosphorylation
level. {ECO:0000269|PubMed:9867848}.
REGION 515 518 Essential for interaction with PTPN11 and
PTPN6. {ECO:0000269|PubMed:9867848}.
MOD_RES 488 488 Phosphotyrosine; by SRC, LCK, INSR and
EGFR. {ECO:0000269|PubMed:21081647,
ECO:0000269|PubMed:9867848}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000250|UniProtKB:P16573}.
MOD_RES 515 515 Phosphotyrosine; by INSR, SRC and LCK.
{ECO:0000269|PubMed:21081647,
ECO:0000269|PubMed:9867848}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11980704,
ECO:0000269|PubMed:19349973}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11980704,
ECO:0000269|PubMed:19349973}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11980704}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P13688}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P13688}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P13688}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11980704,
ECO:0000269|PubMed:19349973}.
CARBOHYD 375 375 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
DISULFID 167 217 {ECO:0000305|PubMed:11980704}.
DISULFID 261 301 {ECO:0000305|PubMed:11980704}.
DISULFID 346 394 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11980704}.
VAR_SEQ 142 322 PILLKPNITSNNSNPVEGDDSVSLTCDSYTDPDNINYLWSR
NGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVCETRNPV
SVNRSDPFSLNIIYGPDTPIISPSDIYLHPGSNLNLSCHAA
SNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNN
SVTGLSRTTVKNITVLE -> Q (in isoform 4).
{ECO:0000303|PubMed:8500759}.
/FTId=VSP_058517.
VAR_SEQ 142 142 P -> Q (in isoform 3).
{ECO:0000303|PubMed:8500759}.
/FTId=VSP_036040.
VAR_SEQ 143 322 Missing (in isoform 3).
{ECO:0000303|PubMed:8500759}.
/FTId=VSP_036041.
VAR_SEQ 455 458 GSDQ -> SGSF (in isoform 2 and isoform
4). {ECO:0000303|PubMed:1633107,
ECO:0000303|PubMed:1719235,
ECO:0000303|PubMed:8500759}.
/FTId=VSP_002484.
VAR_SEQ 459 521 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:1633107,
ECO:0000303|PubMed:1719235,
ECO:0000303|PubMed:8500759}.
/FTId=VSP_002485.
MUTAGEN 488 488 Y->F: Phosphorylated on tyrosine.
Abrogates interaction with PTPN11.
Abrogates interaction with PTPN11 and
phosphorylation; when associated with F-
515. Reduces endothelial cell migration
and differentiation. Suppresses T cell
proliferation; when associated with F-
515. Increases cytokine production; when
associated with F-515. Activates JNK
cascade; when associated with F-515.
Abrogates CEACAM1-L phosphorylation in
endothelial cells and decreases amounts
of released nitric oxide upon VEGF
stimulation. Impairs interaction with and
inactivation of SYK; when associated with
F-515. {ECO:0000269|PubMed:16680193,
ECO:0000269|PubMed:17081782,
ECO:0000269|PubMed:21081647,
ECO:0000269|PubMed:22496641,
ECO:0000269|PubMed:9867848}.
MUTAGEN 503 503 S->A: Reduces endothelial cell migration
and differentiation.
{ECO:0000269|PubMed:16680193}.
MUTAGEN 515 515 Y->F: Phosphorylated on tyrosine.
Abrogates interaction with PTPN11.
Abrogates interaction with PTPN11 and
phosphorylation; when associated with F-
488. Suppresses T cell proliferation;
when associated with F-488. Increases
cytokine production; when associated with
F-488. Activates JNK cascade; when
associated with F-488. Abrogates CEACAM1-
L phosphorylation in endothelial cells
upon VEGF stimulation. Impairs
interaction with and inactivation of SYK;
when associated with F-488.
{ECO:0000269|PubMed:17081782,
ECO:0000269|PubMed:21081647,
ECO:0000269|PubMed:22496641,
ECO:0000269|PubMed:9867848}.
MUTAGEN 518 518 V->A: Impairs interaction with PTPN11 and
PTPN6. Doesn't affect phosphorylation.
{ECO:0000269|PubMed:9867848}.
MUTAGEN 519 521 Missing: Reduces Tyr phosphorylation by
at least 50% and almost completely
abrogates interaction with PTPN11 and
PTPN6. {ECO:0000269|PubMed:9867848}.
CONFLICT 361 362 SQ -> RE (in Ref. 3; CAA47699/CAA47695).
{ECO:0000305}.
STRAND 37 46 {ECO:0000244|PDB:3R4D}.
STRAND 51 56 {ECO:0000244|PDB:3R4D}.
STRAND 63 71 {ECO:0000244|PDB:3R4D}.
HELIX 75 77 {ECO:0000244|PDB:3R4D}.
STRAND 78 83 {ECO:0000244|PDB:3R4D}.
HELIX 84 86 {ECO:0000244|PDB:3R4D}.
STRAND 88 91 {ECO:0000244|PDB:3R4D}.
STRAND 97 101 {ECO:0000244|PDB:3R4D}.
STRAND 107 109 {ECO:0000244|PDB:3R4D}.
HELIX 114 116 {ECO:0000244|PDB:3R4D}.
STRAND 118 125 {ECO:0000244|PDB:3R4D}.
STRAND 130 141 {ECO:0000244|PDB:3R4D}.
STRAND 328 332 {ECO:0000244|PDB:3R4D}.
STRAND 334 336 {ECO:0000244|PDB:1L6Z}.
STRAND 342 347 {ECO:0000244|PDB:3R4D}.
STRAND 354 359 {ECO:0000244|PDB:3R4D}.
STRAND 368 373 {ECO:0000244|PDB:3R4D}.
TURN 374 377 {ECO:0000244|PDB:3R4D}.
STRAND 378 383 {ECO:0000244|PDB:3R4D}.
HELIX 386 388 {ECO:0000244|PDB:3R4D}.
STRAND 390 397 {ECO:0000244|PDB:3R4D}.
STRAND 408 410 {ECO:0000244|PDB:3R4D}.
SEQUENCE 521 AA; 57016 MW; 1C8F71FAC47DD54E CRC64;
MELASAHLHK GQVPWGGLLL TASLLASWSP ATTAEVTIEA VPPQVAEDNN VLLLVHNLPL
ALGAFAWYKG NTTAIDKEIA RFVPNSNMNF TGQAYSGREI IYSNGSLLFQ MITMKDMGVY
TLDMTDENYR RTQATVRFHV HPILLKPNIT SNNSNPVEGD DSVSLTCDSY TDPDNINYLW
SRNGESLSEG DRLKLSEGNR TLTLLNVTRN DTGPYVCETR NPVSVNRSDP FSLNIIYGPD
TPIISPSDIY LHPGSNLNLS CHAASNPPAQ YFWLINEKPH ASSQELFIPN ITTNNSGTYT
CFVNNSVTGL SRTTVKNITV LEPVTQPFLQ VTNTTVKELD SVTLTCLSND IGANIQWLFN
SQSLQLTERM TLSQNNSILR IDPIKREDAG EYQCEISNPV SVRRSNSIKL DIIFDPTQGG
LSDGAIAGIV IGVVAGVALI AGLAYFLYSR KSGGGSDQRD LTEHKPSTSN HNLAPSDNSP
NKVDDVAYTV LNFNSQQPNR PTSAPSSPRA TETVYSEVKK K


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