VTM2A_MOUSE
ID VTM2A_MOUSE Reviewed; 236 AA.
AC Q8R0A6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=V-set and transmembrane domain-containing protein 2A {ECO:0000312|MGI:MGI:2384826};
DE Flags: Precursor;
GN Name=Vstm2a {ECO:0000312|MGI:MGI:2384826}; Synonyms=Vstm2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INDUCTION, MUTAGENESIS OF ASN-35 AND ASN-175, AND GLYCOSYLATION AT
RP ASN-35 AND ASN-175.
RX PubMed=28052263; DOI=10.1016/j.celrep.2016.12.015;
RA Secco B., Camire E., Briere M.A., Caron A., Billong A., Gelinas Y.,
RA Lemay A.M., Tharp K.M., Lee P.L., Gobeil S., Guimond J.V., Patey N.,
RA Guertin D.A., Stahl A., Haddad E., Marsolais D., Bosse Y., Birsoy K.,
RA Laplante M.;
RT "Amplification of adipogenic commitment by VSTM2A.";
RL Cell Rep. 18:93-106(2017).
CC -!- FUNCTION: Plays a role in the regulation of the early stage of white
CC and brown preadipocyte cell differentiation. Promotes adipogenic
CC commitment of preadipocytes by increasing gene expression of the
CC transcription factor PPARG in a BMP4-dependent signaling pathway.
CC {ECO:0000269|PubMed:28052263}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28052263}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28052263}.
CC Note=Secreted by adipose precursor cells (PubMed:28052263). Not
CC detected in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8TAG5,
CC ECO:0000269|PubMed:28052263}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Expressed in neurons. Expressed
CC in adipose precursor cells in epididymal white adipose tissue (at
CC protein level). Strongly expressed in adipose precursor cells. Weakly
CC expressed in adipocytes. {ECO:0000269|PubMed:28052263}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo in subcutaneous white adipose
CC tissue from 16.5 days post coitum (dpc) to 4 days postnatal (P4).
CC Expressed early in pups in visceral epididymal white adipose tissue at
CC 4 days postnatal (P4) and strongly decreases from P7 to P56 (at protein
CC level). {ECO:0000269|PubMed:28052263}.
CC -!- INDUCTION: Up-regulated is response to high-fat feeding (at protein
CC level) (PubMed:28052263). Up-regulated by the transcription factor
CC PPARG in a BMP4-signaling dependent manner. Up-regulated during
CC adipocyte differentiation. {ECO:0000269|PubMed:28052263}.
CC -!- PTM: N-glycosylated. N-linked glycosylation on Asn-35 and Asn-175 is
CC critical for secretion but not for preadipocyte cell differentiation
CC activity. {ECO:0000269|PubMed:28052263}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27127.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC027127; AAH27127.1; ALT_INIT; mRNA.
DR CCDS; CCDS24441.2; -.
DR RefSeq; NP_666079.2; NM_145967.2.
DR AlphaFoldDB; Q8R0A6; -.
DR SMR; Q8R0A6; -.
DR BioGRID; 229262; 1.
DR STRING; 10090.ENSMUSP00000105272; -.
DR GlyGen; Q8R0A6; 2 sites.
DR iPTMnet; Q8R0A6; -.
DR PhosphoSitePlus; Q8R0A6; -.
DR PaxDb; Q8R0A6; -.
DR PRIDE; Q8R0A6; -.
DR ProteomicsDB; 297617; -.
DR Antibodypedia; 13746; 87 antibodies from 16 providers.
DR DNASU; 211739; -.
DR Ensembl; ENSMUST00000109645; ENSMUSP00000105272; ENSMUSG00000048834.
DR GeneID; 211739; -.
DR KEGG; mmu:211739; -.
DR UCSC; uc007ibk.2; mouse.
DR CTD; 222008; -.
DR MGI; MGI:2384826; Vstm2a.
DR VEuPathDB; HostDB:ENSMUSG00000048834; -.
DR eggNOG; ENOG502RKWR; Eukaryota.
DR GeneTree; ENSGT00940000160556; -.
DR HOGENOM; CLU_081009_1_0_1; -.
DR InParanoid; Q8R0A6; -.
DR OMA; MWTSHDS; -.
DR OrthoDB; 1216208at2759; -.
DR TreeFam; TF331739; -.
DR BioGRID-ORCS; 211739; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q8R0A6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R0A6; protein.
DR Bgee; ENSMUSG00000048834; Expressed in lateral hypothalamic area and 128 other tissues.
DR ExpressionAtlas; Q8R0A6; baseline and differential.
DR Genevisible; Q8R0A6; MM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISO:MGI.
DR GO; GO:0070352; P:positive regulation of white fat cell proliferation; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..236
FT /note="V-set and transmembrane domain-containing protein
FT 2A"
FT /id="PRO_0000014776"
FT DOMAIN 27..143
FT /note="Ig-like V-type"
FT REGION 168..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:28052263"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:28052263"
FT DISULFID 48..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 35
FT /note="N->Q: Abolishes glycosylation and impairs
FT secretion."
FT /evidence="ECO:0000269|PubMed:28052263"
FT MUTAGEN 175
FT /note="N->Q: Abolishes glycosylation and impairs
FT secretion."
FT /evidence="ECO:0000269|PubMed:28052263"
SQ SEQUENCE 236 AA; 25876 MW; 0A608D52371B9105 CRC64;
MMGIFLASVG FMFFSVLYVQ QGLSSQAKFT ELPRNVTATE GQNVEMSCAF QSGSASVYLE
IQWWFLRGPE DLEQGTEAAG SQVELLPDRD PDNDGTKIST VKVQGNDISH KLQISKVRKK
DEGLYECRVT DANYGELQEH KAQAYLKVNA NSHARRMQAF EASPMWLQDT KPRKNASSVV
PSSVHNSANQ RMHSTSSPQA VAKIPKQSPQ SGARIATSHG LSVLLLVCGF VKGALL
