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Carcinoembryonic antigen-related cell adhesion molecule 2 (CEA-related cell adhesion molecule 2) (Biliary glycoprotein 2) (BGP-2)

 CEAM2_MOUSE             Reviewed;         520 AA.
Q925P2; D0VY57; E9QLI9; I7HDK2; Q61349; Q8R1N5;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2013, sequence version 3.
23-MAY-2018, entry version 126.
RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 2;
Short=CEA-related cell adhesion molecule 2;
AltName: Full=Biliary glycoprotein 2;
Short=BGP-2;
Flags: Precursor;
Name=Ceacam2; Synonyms=Bgp2;
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] (ISOFORMS 2 AND 3), INTERACTION WITH MHV
SPIKE GLYCOPROTEIN, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Kidney;
PubMed=8207827;
Nedellec P., Dveksler G.S., Daniels E., Turbide C., Chow B.,
Basile A.A., Holmes K.V., Beauchemin N.;
"Bgp2, a new member of the carcinoembryonic antigen-related gene
family, encodes an alternative receptor for mouse hepatitis viruses.";
J. Virol. 68:4525-4537(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1
AND 3), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=129/SvEv;
PubMed=11284729; DOI=10.1042/0264-6021:3550417;
Han E., Phan D., Lo P., Poy M.N., Behringer R., Najjar S.M.,
Lin S.-H.;
"Differences in tissue-specific and embryonic expression of mouse
Ceacam1 and Ceacam2 genes.";
Biochem. J. 355:417-423(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=SJL/J; TISSUE=Liver;
PubMed=20410265; DOI=10.1128/JVI.02680-09;
Hirai A., Ohtsuka N., Ikeda T., Taniguchi R., Blau D., Nakagaki K.,
Miura H.S., Ami Y., Yamada Y.K., Itohara S., Holmes K.V., Taguchi F.;
"Role of mouse hepatitis virus (MHV) receptor murine CEACAM1 in the
resistance of mice to MHV infection: studies of mice with chimeric
mCEACAM1a and mCEACAM1b.";
J. Virol. 84:6654-6666(2010).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
STRAIN=ddY; TISSUE=Testis;
PubMed=23070997; DOI=10.1002/mrd.22123;
Salaheldeen E., Kurio H., Howida A., Iida H.;
"Molecular cloning and localization of a CEACAM2 isoform, CEACAM2-L,
expressed in spermatids in mouse testis.";
Mol. Reprod. Dev. 79:843-852(2012).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Kidney;
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).
[7]
INTERACTION WITH MHV SPIKE GLYCOPROTEIN.
PubMed=9696818;
Zelus B.D., Wessner D.R., Williams R.K., Pensiero M.N., Phibbs F.T.,
deSouza M., Dveksler G.S., Holmes K.V.;
"Purified, soluble recombinant mouse hepatitis virus receptor,
Bgp1(b), and Bgp2 murine coronavirus receptors differ in mouse
hepatitis virus binding and neutralizing activities.";
J. Virol. 72:7237-7244(1998).
[8]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=10491101; DOI=10.1046/j.1432-1327.1999.00660.x;
Robitaille J., Izzi L., Daniels E., Zelus B., Holmes K.V.,
Beauchemin N.;
"Comparison of expression patterns and cell adhesion properties of the
mouse biliary glycoproteins Bbgp1 and Bbgp2.";
Eur. J. Biochem. 264:534-544(1999).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-210.
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).
[10]
FUNCTION, TISSUE SPECIFICITY, INDUCTION BY FASTING, AND DISRUPTION
PHENOTYPE.
PubMed=20381490; DOI=10.1053/j.gastro.2010.03.056;
Heinrich G., Ghosh S., Deangelis A.M., Schroeder-Gloeckler J.M.,
Patel P.R., Castaneda T.R., Jeffers S., Lee A.D., Jung D.Y., Zhang Z.,
Opland D.M., Myers M.G. Jr., Kim J.K., Najjar S.M.;
"Carcinoembryonic antigen-related cell adhesion molecule 2 controls
energy balance and peripheral insulin action in mice.";
Gastroenterology 139:644-652(2010).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22159884; DOI=10.1007/s00125-011-2388-x;
Patel P.R., Ramakrishnan S.K., Kaw M.K., Raphael C.K., Ghosh S.,
Marino J.S., Heinrich G., Lee S.J., Bourey R.E., Hill J.W., Jung D.Y.,
Morgan D.A., Kim J.K., Rahmouni K., Najjar S.M.;
"Increased metabolic rate and insulin sensitivity in male mice lacking
the carcino-embryonic antigen-related cell adhesion molecule 2.";
Diabetologia 55:763-772(2012).
-!- FUNCTION: Controls energy balance and peripheral insulin action.
Involved in the regulation of feeding behavior particularly in the
ventromedial nucleus of hypothalamus (VMH) regulation of food
intake. Has a role in the regulation of metabolic rate and insulin
sensitivity or resistance via effects on brown adipogenesis,
sympathetic nervous outflow to brown adipose tissue, spontaneous
activity and energy expenditure in skeletal muscle. In case of
murine coronavirus (MHV) infection, does probably not serve as
functional receptor for the virus.
-!- FUNCTION: Isoform 2 may be an adhesion molecule contributing to
cell to cell adhesion between elongating spermatids and Sertoli
cells within the seminiferous epithelium.
-!- SUBUNIT: Interacts weakly with MHV spike protein in tissue
culture. {ECO:0000269|PubMed:8207827, ECO:0000269|PubMed:9696818}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23070997};
Single-pass type I membrane protein {ECO:0000269|PubMed:23070997}.
Note=Localizes to sites on the plasma membrane of elongating
spermatids where Sertoli cells make contact.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Bgp2;
IsoId=Q925P2-1; Sequence=Displayed;
Name=2; Synonyms=Bgp2, Bgp2L, Ceacam2-Long, Ceacam2-L;
IsoId=Q925P2-2; Sequence=VSP_025300;
Name=3; Synonyms=Bgp2, Bgp2S, Ceacam2-Short, Ceacam2-S;
IsoId=Q925P2-3; Sequence=VSP_025300, VSP_025301;
-!- TISSUE SPECIFICITY: Isoform 2 is detected in elongating spermatids
within the seminiferous epithelium (at protein level). Expressed
in kidney, colon, uterus, gut mononuclear cells, crypt epithelia
of intestinal tissues, and to a lesser extent, in spleen.
Expressed in brain including VMH, globus pallidus, ventral
pallidum, striatum, olfactory bulb and hippocampus. Also detected
in rectal carcinoma cell line CMT93. Isoform 2 and isoform 3 are
expressed in testis. Isoform 2 is detected in seminiferous tubule,
not detected in epididymal spermatozoa. Also not observed on
spermatogonia, spermatocytes, round spermatids or somatic Sertoli
cells. During stages I-VII of spermatogenesis, detected on the
elongating spermatids. At spermiation (stage VIII) and subsequent
stages IX-XII, levels are drastically reduced or absent in the
seminiferous tubules. Sometimes weakly detected in the apical
region of stage-VIII seminiferous epithelium. Isoform 2 level is
very low in stomach, kidney, intestine, liver and spleen.
{ECO:0000269|PubMed:10491101, ECO:0000269|PubMed:11284729,
ECO:0000269|PubMed:20381490, ECO:0000269|PubMed:23070997,
ECO:0000269|PubMed:8207827}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development.
Isoform 2 first appears faintly in the testis 3 weeks into
postnatal development and its expression level increases after 5
weeks. {ECO:0000269|PubMed:11284729, ECO:0000269|PubMed:23070997}.
-!- INDUCTION: Levels in brain increase at fasting and decrease at 4
and 7 hours of refeeding. {ECO:0000269|PubMed:20381490}.
-!- DISRUPTION PHENOTYPE: Sexually dimorphic effect. Homozygous null
mutant female mice exhibit obesity that results from hyperphagia
and reduced energy expenditure. Hyperphagia leads to peripheral
insulin resistance. Insulin action is normal in liver but is
compromised in skeletal muscle; the mice have incomplete fatty
acid oxidation and impaired glucose uptake and disposal.
Hyperphagia appears to result partly from increased
hyperinsulinemia-induced hypothalamic fatty acid synthase levels
and activity. Hyperinsulinemia is caused by increased insulin
secretion. Homozygous null mutant male mice show total fat mass
reduction, which ows to the hypermetabolic state despite
hyperphagia. They also exhibit insulin sensitivity with elevated
beta-oxidation in skeletal muscle, which is likely to offset the
effects of increased food intake. Both males and females have
increased brown adipogenesis. However, only males have increased
activation of sympathetic tone regulation of adipose tissue and
increased spontaneous activity. {ECO:0000269|PubMed:20381490,
ECO:0000269|PubMed:22159884}.
-!- MISCELLANEOUS: The human orthologous protein seems not to exist.
In mice, both Ceacam1 and Ceacam2 are the paralogs of human
CEACAM1.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF101164; AAC99458.1; -; mRNA.
EMBL; X76085; CAA53699.1; -; mRNA.
EMBL; AF287912; AAK52602.1; -; Genomic_DNA.
EMBL; AB500065; BAI49177.1; -; mRNA.
EMBL; AB731450; BAM29120.1; -; mRNA.
EMBL; AC162443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC024320; AAH24320.1; -; mRNA.
CCDS; CCDS20986.1; -. [Q925P2-3]
CCDS; CCDS52152.1; -. [Q925P2-2]
CCDS; CCDS52153.1; -. [Q925P2-1]
PIR; I48268; I48268.
RefSeq; NP_001106839.1; NM_001113368.1. [Q925P2-1]
RefSeq; NP_001106840.1; NM_001113369.1. [Q925P2-2]
RefSeq; NP_031569.1; NM_007543.4. [Q925P2-3]
UniGene; Mm.439731; -.
ProteinModelPortal; Q925P2; -.
STRING; 10090.ENSMUSP00000048118; -.
iPTMnet; Q925P2; -.
PhosphoSitePlus; Q925P2; -.
PaxDb; Q925P2; -.
PeptideAtlas; Q925P2; -.
PRIDE; Q925P2; -.
Ensembl; ENSMUST00000044547; ENSMUSP00000048118; ENSMUSG00000054385. [Q925P2-1]
Ensembl; ENSMUST00000064862; ENSMUSP00000068540; ENSMUSG00000054385. [Q925P2-3]
Ensembl; ENSMUST00000066503; ENSMUSP00000064255; ENSMUSG00000054385. [Q925P2-2]
GeneID; 26367; -.
KEGG; mmu:26367; -.
UCSC; uc009ftc.2; mouse. [Q925P2-3]
UCSC; uc012ffv.1; mouse. [Q925P2-1]
UCSC; uc012ffw.1; mouse. [Q925P2-2]
CTD; 26367; -.
MGI; MGI:1347246; Ceacam2.
eggNOG; ENOG410IFE1; Eukaryota.
eggNOG; ENOG410YR1P; LUCA.
GeneTree; ENSGT00760000119187; -.
HOGENOM; HOG000233417; -.
HOVERGEN; HBG007922; -.
InParanoid; Q925P2; -.
KO; K06499; -.
OMA; NISHEPP; -.
OrthoDB; EOG091G0AMM; -.
TreeFam; TF336859; -.
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.
PRO; PR:Q925P2; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000054385; -.
CleanEx; MM_CEACAM2; -.
Genevisible; Q925P2; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0031005; F:filamin binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
GO; GO:0097009; P:energy homeostasis; IMP:MGI.
GO; GO:0070348; P:negative regulation of brown fat cell proliferation; IMP:MGI.
GO; GO:2000252; P:negative regulation of feeding behavior; IMP:MGI.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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.
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 membrane; Complete proteome;
Disulfide bond; Glycoprotein; Host-virus interaction;
Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 520 Carcinoembryonic antigen-related cell
adhesion molecule 2.
/FTId=PRO_0000287095.
TOPO_DOM 35 422 Extracellular. {ECO:0000255}.
TRANSMEM 423 443 Helical. {ECO:0000255}.
TOPO_DOM 444 520 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 141 Ig-like V-type.
DOMAIN 145 234 Ig-like C2-type 1.
DOMAIN 239 319 Ig-like C2-type 2.
DOMAIN 327 411 Ig-like C2-type 3.
MOD_RES 487 487 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31809}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000250|UniProtKB:P16573}.
MOD_RES 514 514 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31809}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 167 217 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 261 301 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 346 394 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 142 322 TLLLKSNITSNNSNPVEGDDSVSLTCDSYTDPDNITYLWSR
NGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVCETRNPV
SVNRSDPFSLNIIYGPDTPIISPSDIYLHPGSNLNLSCHAA
SNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNN
SVTGLSRTTVKNITVLE -> K (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:20410265,
ECO:0000303|PubMed:23070997,
ECO:0000303|PubMed:8207827}.
/FTId=VSP_025300.
VAR_SEQ 453 520 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:20410265,
ECO:0000303|PubMed:8207827}.
/FTId=VSP_025301.
CONFLICT 16 16 F -> V (in Ref. 2; AAK52602 and 3;
BAI49177). {ECO:0000305}.
CONFLICT 63 63 S -> L (in Ref. 2; AAK52602).
{ECO:0000305}.
CONFLICT 100 100 T -> A (in Ref. 2; AAK52602).
{ECO:0000305}.
CONFLICT 128 128 N -> D (in Ref. 2; AAK52602).
{ECO:0000305}.
CONFLICT 302 302 F -> L (in Ref. 2; AAK52602).
{ECO:0000305}.
CONFLICT 351 351 R -> S (in Ref. 2; AAK52602).
{ECO:0000305}.
CONFLICT 421 421 S -> L (in Ref. 2; AAK52602).
{ECO:0000305}.
CONFLICT 467 467 A -> T (in Ref. 1; AAC99458).
{ECO:0000305}.
SEQUENCE 520 AA; 57202 MW; C55CA7D26F57C19A CRC64;
MELASAHLHK GQVPWFGLLL TASLLASWSP PTTAQVTVMA FPLHAAEGNN VILVVYNMMK
GVSAFSWHKG STTSTNAEIV RFVTGTNKTI KGPVHSGRET LYSNGSLLIQ RVTMKDTGVY
TIEMTDQNYR RRVLTGQFHV HTLLLKSNIT SNNSNPVEGD DSVSLTCDSY TDPDNITYLW
SRNGESLSEG DRLKLSEGNR TLTLLNVTRN DTGPYVCETR NPVSVNRSDP FSLNIIYGPD
TPIISPSDIY LHPGSNLNLS CHAASNPPAQ YFWLINEKPH ASSQELFIPN ITTNNSGTYT
CFVNNSVTGL SRTTVKNITV LEPVTQPSLQ VTNTTVKELD SVTLTCLSKD RQAHIHWIFN
NDTLLITEKM TTSQAGLILK IDPIKREDAG EYQCEISNPV SVKRSNSIKL EVIFDSTYDI
SDVPIAVIIT GAVAGVILIA GLAYRLCSRK SRWGSDQRDL TEHKPSASNH NLAPSDNSPN
KVDDVAYTVL NFNSQQPNRP TSAPSSPRAT ETVYSEVKKK


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