CEAM2_MOUSE
ID CEAM2_MOUSE Reviewed; 520 AA.
AC Q925P2; D0VY57; E9QLI9; I7HDK2; Q61349; Q8R1N5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 2;
DE Short=CEA-related cell adhesion molecule 2;
DE AltName: Full=Biliary glycoprotein 2;
DE Short=BGP-2;
DE Flags: Precursor;
GN Name=Ceacam2; Synonyms=Bgp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH MHV SPIKE
RP GLYCOPROTEIN, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=8207827; DOI=10.1128/jvi.68.7.4525-4537.1994;
RA Nedellec P., Dveksler G.S., Daniels E., Turbide C., Chow B., Basile A.A.,
RA Holmes K.V., Beauchemin N.;
RT "Bgp2, a new member of the carcinoembryonic antigen-related gene family,
RT encodes an alternative receptor for mouse hepatitis viruses.";
RL J. Virol. 68:4525-4537(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 3),
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/SvEv;
RX PubMed=11284729; DOI=10.1042/0264-6021:3550417;
RA Han E., Phan D., Lo P., Poy M.N., Behringer R., Najjar S.M., Lin S.-H.;
RT "Differences in tissue-specific and embryonic expression of mouse Ceacam1
RT and Ceacam2 genes.";
RL Biochem. J. 355:417-423(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=SJL/J; TISSUE=Liver;
RX PubMed=20410265; DOI=10.1128/jvi.02680-09;
RA Hirai A., Ohtsuka N., Ikeda T., Taniguchi R., Blau D., Nakagaki K.,
RA Miura H.S., Ami Y., Yamada Y.K., Itohara S., Holmes K.V., Taguchi F.;
RT "Role of mouse hepatitis virus (MHV) receptor murine CEACAM1 in the
RT resistance of mice to MHV infection: studies of mice with chimeric
RT mCEACAM1a and mCEACAM1b.";
RL J. Virol. 84:6654-6666(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=ddY; TISSUE=Testis;
RX PubMed=23070997; DOI=10.1002/mrd.22123;
RA Salaheldeen E., Kurio H., Howida A., Iida H.;
RT "Molecular cloning and localization of a CEACAM2 isoform, CEACAM2-L,
RT expressed in spermatids in mouse testis.";
RL Mol. Reprod. Dev. 79:843-852(2012).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH MHV SPIKE GLYCOPROTEIN.
RX PubMed=9696818; DOI=10.1128/jvi.72.9.7237-7244.1998;
RA Zelus B.D., Wessner D.R., Williams R.K., Pensiero M.N., Phibbs F.T.,
RA deSouza M., Dveksler G.S., Holmes K.V.;
RT "Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1(b), and
RT Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding
RT and neutralizing activities.";
RL J. Virol. 72:7237-7244(1998).
RN [8]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=10491101; DOI=10.1046/j.1432-1327.1999.00660.x;
RA Robitaille J., Izzi L., Daniels E., Zelus B., Holmes K.V., Beauchemin N.;
RT "Comparison of expression patterns and cell adhesion properties of the
RT mouse biliary glycoproteins Bbgp1 and Bbgp2.";
RL Eur. J. Biochem. 264:534-544(1999).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-210.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY FASTING, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20381490; DOI=10.1053/j.gastro.2010.03.056;
RA Heinrich G., Ghosh S., Deangelis A.M., Schroeder-Gloeckler J.M.,
RA Patel P.R., Castaneda T.R., Jeffers S., Lee A.D., Jung D.Y., Zhang Z.,
RA Opland D.M., Myers M.G. Jr., Kim J.K., Najjar S.M.;
RT "Carcinoembryonic antigen-related cell adhesion molecule 2 controls energy
RT balance and peripheral insulin action in mice.";
RL Gastroenterology 139:644-652(2010).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22159884; DOI=10.1007/s00125-011-2388-x;
RA Patel P.R., Ramakrishnan S.K., Kaw M.K., Raphael C.K., Ghosh S.,
RA Marino J.S., Heinrich G., Lee S.J., Bourey R.E., Hill J.W., Jung D.Y.,
RA Morgan D.A., Kim J.K., Rahmouni K., Najjar S.M.;
RT "Increased metabolic rate and insulin sensitivity in male mice lacking the
RT carcino-embryonic antigen-related cell adhesion molecule 2.";
RL Diabetologia 55:763-772(2012).
CC -!- FUNCTION: Controls energy balance and peripheral insulin action.
CC Involved in the regulation of feeding behavior particularly in the
CC ventromedial nucleus of hypothalamus (VMH) regulation of food intake.
CC Has a role in the regulation of metabolic rate and insulin sensitivity
CC or resistance via effects on brown adipogenesis, sympathetic nervous
CC outflow to brown adipose tissue, spontaneous activity and energy
CC expenditure in skeletal muscle. In case of murine coronavirus (MHV)
CC infection, does probably not serve as functional receptor for the
CC virus.
CC -!- FUNCTION: Isoform 2 may be an adhesion molecule contributing to cell to
CC cell adhesion between elongating spermatids and Sertoli cells within
CC the seminiferous epithelium.
CC -!- SUBUNIT: Interacts weakly with MHV spike protein in tissue culture.
CC {ECO:0000269|PubMed:8207827, ECO:0000269|PubMed:9696818}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23070997};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:23070997}.
CC Note=Localizes to sites on the plasma membrane of elongating spermatids
CC where Sertoli cells make contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Bgp2;
CC IsoId=Q925P2-1; Sequence=Displayed;
CC Name=2; Synonyms=Bgp2, Bgp2L, Ceacam2-Long, Ceacam2-L;
CC IsoId=Q925P2-2; Sequence=VSP_025300;
CC Name=3; Synonyms=Bgp2, Bgp2S, Ceacam2-Short, Ceacam2-S;
CC IsoId=Q925P2-3; Sequence=VSP_025300, VSP_025301;
CC -!- TISSUE SPECIFICITY: Isoform 2 is detected in elongating spermatids
CC within the seminiferous epithelium (at protein level). Expressed in
CC kidney, colon, uterus, gut mononuclear cells, crypt epithelia of
CC intestinal tissues, and to a lesser extent, in spleen. Expressed in
CC brain including VMH, globus pallidus, ventral pallidum, striatum,
CC olfactory bulb and hippocampus. Also detected in rectal carcinoma cell
CC line CMT93. Isoform 2 and isoform 3 are expressed in testis. Isoform 2
CC is detected in seminiferous tubule, not detected in epididymal
CC spermatozoa. Also not observed on spermatogonia, spermatocytes, round
CC spermatids or somatic Sertoli cells. During stages I-VII of
CC spermatogenesis, detected on the elongating spermatids. At spermiation
CC (stage VIII) and subsequent stages IX-XII, levels are drastically
CC reduced or absent in the seminiferous tubules. Sometimes weakly
CC detected in the apical region of stage-VIII seminiferous epithelium.
CC Isoform 2 level is very low in stomach, kidney, intestine, liver and
CC spleen. {ECO:0000269|PubMed:10491101, ECO:0000269|PubMed:11284729,
CC ECO:0000269|PubMed:20381490, ECO:0000269|PubMed:23070997,
CC ECO:0000269|PubMed:8207827}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development.
CC Isoform 2 first appears faintly in the testis 3 weeks into postnatal
CC development and its expression level increases after 5 weeks.
CC {ECO:0000269|PubMed:11284729, ECO:0000269|PubMed:23070997}.
CC -!- INDUCTION: Levels in brain increase at fasting and decrease at 4 and 7
CC hours of refeeding. {ECO:0000269|PubMed:20381490}.
CC -!- DISRUPTION PHENOTYPE: Sexually dimorphic effect. Homozygous null mutant
CC female mice exhibit obesity that results from hyperphagia and reduced
CC energy expenditure. Hyperphagia leads to peripheral insulin resistance.
CC Insulin action is normal in liver but is compromised in skeletal
CC muscle; the mice have incomplete fatty acid oxidation and impaired
CC glucose uptake and disposal. Hyperphagia appears to result partly from
CC increased hyperinsulinemia-induced hypothalamic fatty acid synthase
CC levels and activity. Hyperinsulinemia is caused by increased insulin
CC secretion. Homozygous null mutant male mice show total fat mass
CC reduction, which ows to the hypermetabolic state despite hyperphagia.
CC They also exhibit insulin sensitivity with elevated beta-oxidation in
CC skeletal muscle, which is likely to offset the effects of increased
CC food intake. Both males and females have increased brown adipogenesis.
CC However, only males have increased activation of sympathetic tone
CC regulation of adipose tissue and increased spontaneous activity.
CC {ECO:0000269|PubMed:20381490, ECO:0000269|PubMed:22159884}.
CC -!- MISCELLANEOUS: The human orthologous protein seems not to exist. In
CC mice, both Ceacam1 and Ceacam2 are the paralogs of human CEACAM1.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC {ECO:0000305}.
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DR EMBL; AF101164; AAC99458.1; -; mRNA.
DR EMBL; X76085; CAA53699.1; -; mRNA.
DR EMBL; AF287912; AAK52602.1; -; Genomic_DNA.
DR EMBL; AB500065; BAI49177.1; -; mRNA.
DR EMBL; AB731450; BAM29120.1; -; mRNA.
DR EMBL; AC162443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024320; AAH24320.1; -; mRNA.
DR CCDS; CCDS20986.1; -. [Q925P2-3]
DR CCDS; CCDS52152.1; -. [Q925P2-2]
DR CCDS; CCDS52153.1; -. [Q925P2-1]
DR PIR; I48268; I48268.
DR RefSeq; NP_001106839.1; NM_001113368.1. [Q925P2-1]
DR RefSeq; NP_001106840.1; NM_001113369.1. [Q925P2-2]
DR RefSeq; NP_031569.1; NM_007543.4. [Q925P2-3]
DR AlphaFoldDB; Q925P2; -.
DR SMR; Q925P2; -.
DR GlyGen; Q925P2; 16 sites.
DR iPTMnet; Q925P2; -.
DR PhosphoSitePlus; Q925P2; -.
DR MaxQB; Q925P2; -.
DR PaxDb; Q925P2; -.
DR PeptideAtlas; Q925P2; -.
DR PRIDE; Q925P2; -.
DR ProteomicsDB; 280049; -. [Q925P2-1]
DR ProteomicsDB; 280050; -. [Q925P2-2]
DR ProteomicsDB; 280051; -. [Q925P2-3]
DR ABCD; Q925P2; 23 sequenced antibodies.
DR DNASU; 26367; -.
DR Ensembl; ENSMUST00000044547; ENSMUSP00000048118; ENSMUSG00000054385. [Q925P2-1]
DR Ensembl; ENSMUST00000064862; ENSMUSP00000068540; ENSMUSG00000054385. [Q925P2-3]
DR Ensembl; ENSMUST00000066503; ENSMUSP00000064255; ENSMUSG00000054385. [Q925P2-2]
DR GeneID; 26367; -.
DR KEGG; mmu:26367; -.
DR UCSC; uc009ftc.2; mouse. [Q925P2-3]
DR UCSC; uc012ffv.1; mouse. [Q925P2-1]
DR UCSC; uc012ffw.1; mouse. [Q925P2-2]
DR CTD; 26367; -.
DR MGI; MGI:1347246; Ceacam2.
DR VEuPathDB; HostDB:ENSMUSG00000054385; -.
DR GeneTree; ENSGT00960000186634; -.
DR HOGENOM; CLU_024555_4_0_1; -.
DR InParanoid; Q925P2; -.
DR OMA; WENSENY; -.
DR OrthoDB; 998214at2759; -.
DR PhylomeDB; Q925P2; -.
DR TreeFam; TF336859; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 26367; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q925P2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q925P2; protein.
DR Bgee; ENSMUSG00000054385; Expressed in spermatid and 58 other tissues.
DR Genevisible; Q925P2; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0031225; C:anchored component of membrane; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
DR GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0031005; F:filamin binding; ISO:MGI.
DR GO; GO:0034235; F:GPI anchor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0097009; P:energy homeostasis; IMP:MGI.
DR GO; GO:1901143; P:insulin catabolic process; ISO:MGI.
DR GO; GO:0038016; P:insulin receptor internalization; ISO:MGI.
DR GO; GO:0070348; P:negative regulation of brown fat cell proliferation; IMP:MGI.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:2000252; P:negative regulation of feeding behavior; IMP:MGI.
DR GO; GO:2000346; P:negative regulation of hepatocyte proliferation; ISO:MGI.
DR GO; GO:1903387; P:positive regulation of homophilic cell adhesion; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:1903385; P:regulation of homophilic cell adhesion; ISO:MGI.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..520
FT /note="Carcinoembryonic antigen-related cell adhesion
FT molecule 2"
FT /id="PRO_0000287095"
FT TOPO_DOM 35..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..141
FT /note="Ig-like V-type"
FT DOMAIN 145..234
FT /note="Ig-like C2-type 1"
FT DOMAIN 239..319
FT /note="Ig-like C2-type 2"
FT DOMAIN 327..411
FT /note="Ig-like C2-type 3"
FT REGION 457..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 487
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31809"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16573"
FT MOD_RES 514
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31809"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 261..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 346..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 142..322
FT /note="TLLLKSNITSNNSNPVEGDDSVSLTCDSYTDPDNITYLWSRNGESLSEGDRL
FT KLSEGNRTLTLLNVTRNDTGPYVCETRNPVSVNRSDPFSLNIIYGPDTPIISPSDIYLH
FT PGSNLNLSCHAASNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNNSVTGLS
FT RTTVKNITVLE -> K (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:20410265, ECO:0000303|PubMed:23070997,
FT ECO:0000303|PubMed:8207827"
FT /id="VSP_025300"
FT VAR_SEQ 453..520
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:20410265, ECO:0000303|PubMed:8207827"
FT /id="VSP_025301"
FT CONFLICT 16
FT /note="F -> V (in Ref. 2; AAK52602 and 3; BAI49177)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="S -> L (in Ref. 2; AAK52602)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="T -> A (in Ref. 2; AAK52602)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="N -> D (in Ref. 2; AAK52602)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="F -> L (in Ref. 2; AAK52602)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="R -> S (in Ref. 2; AAK52602)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="S -> L (in Ref. 2; AAK52602)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="A -> T (in Ref. 1; AAC99458)"
FT /evidence="ECO:0000305"
SQ 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
