BT2A2_MOUSE
ID BT2A2_MOUSE Reviewed; 514 AA.
AC A4QPC6; Q811T8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Butyrophilin subfamily 2 member A2;
DE Flags: Precursor;
GN Name=Btn2a2;
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] (ISOFORM 2).
RA Meyer M., Trowsdale J.;
RT "Comparison of the butyrophilin cluster in human and mouse.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=20208008; DOI=10.4049/jimmunol.0900416;
RA Smith I.A., Knezevic B.R., Ammann J.U., Rhodes D.A., Aw D., Palmer D.B.,
RA Mather I.H., Trowsdale J.;
RT "BTN1A1, the mammary gland butyrophilin, and BTN2A2 are both inhibitors of
RT T cell activation.";
RL J. Immunol. 184:3514-3525(2010).
CC -!- FUNCTION: Inhibits the proliferation of CD4 and CD8 T-cells activated
CC by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion.
CC {ECO:0000269|PubMed:20208008}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A4QPC6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4QPC6-2; Sequence=VSP_036621, VSP_036622;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). In the thymus,
CC restricted to the corticomedullary junction, but not confined solely to
CC epithelial cells (at protein level). Significant expression on naive B-
CC cells, splenic natural killer cells, dendritic cells and peritoneal
CC macrophages (at protein level). Negligible expression on naive T-cells
CC up-regulated on activated T-cells (at protein level).
CC {ECO:0000269|PubMed:20208008}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20208008}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
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DR EMBL; AY177686; AAO38196.1; -; mRNA.
DR EMBL; BC139760; AAI39761.1; -; mRNA.
DR CCDS; CCDS36619.1; -. [A4QPC6-1]
DR RefSeq; NP_001276544.1; NM_001289615.1. [A4QPC6-1]
DR RefSeq; NP_787952.2; NM_175938.3. [A4QPC6-1]
DR RefSeq; XP_006516727.1; XM_006516664.1. [A4QPC6-1]
DR AlphaFoldDB; A4QPC6; -.
DR SMR; A4QPC6; -.
DR STRING; 10090.ENSMUSP00000106063; -.
DR GlyGen; A4QPC6; 2 sites.
DR iPTMnet; A4QPC6; -.
DR PhosphoSitePlus; A4QPC6; -.
DR PaxDb; A4QPC6; -.
DR PRIDE; A4QPC6; -.
DR Antibodypedia; 44597; 135 antibodies from 19 providers.
DR DNASU; 238555; -.
DR Ensembl; ENSMUST00000110432; ENSMUSP00000106062; ENSMUSG00000053216. [A4QPC6-1]
DR Ensembl; ENSMUST00000110433; ENSMUSP00000106063; ENSMUSG00000053216. [A4QPC6-1]
DR GeneID; 238555; -.
DR KEGG; mmu:238555; -.
DR UCSC; uc007ptu.1; mouse. [A4QPC6-1]
DR CTD; 10385; -.
DR MGI; MGI:3606486; Btn2a2.
DR VEuPathDB; HostDB:ENSMUSG00000053216; -.
DR eggNOG; ENOG502QSRZ; Eukaryota.
DR GeneTree; ENSGT00940000158017; -.
DR HOGENOM; CLU_013137_22_2_1; -.
DR InParanoid; A4QPC6; -.
DR OMA; AETHHNH; -.
DR OrthoDB; 522383at2759; -.
DR PhylomeDB; A4QPC6; -.
DR TreeFam; TF331083; -.
DR Reactome; R-MMU-8851680; Butyrophilin (BTN) family interactions.
DR BioGRID-ORCS; 238555; 3 hits in 77 CRISPR screens.
DR PRO; PR:A4QPC6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; A4QPC6; protein.
DR Bgee; ENSMUSG00000053216; Expressed in secondary oocyte and 18 other tissues.
DR ExpressionAtlas; A4QPC6; baseline and differential.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IDA:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IGI:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IGI:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IGI:MGI.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IDA:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR CDD; cd15819; SPRY_PRY_BTN1_2; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
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 InterPro; IPR006574; PRY.
DR InterPro; IPR037958; SPRY/PRY_BTN1/2.
DR InterPro; IPR003877; SPRY_dom.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..514
FT /note="Butyrophilin subfamily 2 member A2"
FT /id="PRO_0000367054"
FT TOPO_DOM 30..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..142
FT /note="Ig-like V-type"
FT DOMAIN 150..232
FT /note="Ig-like C2-type"
FT DOMAIN 295..488
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT COILED 281..304
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 166..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 372..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036621"
FT VAR_SEQ 422..451
FT /note="IIPLKERLHRIAVFLDCEGGDISFYNMRDR -> DHTSERASSPYSCLPGL
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036622"
SQ SEQUENCE 514 AA; 58455 MW; 2C988E1520BE11F1 CRC64;
MEPTTSLRSC PIASLLFFLV LSLFVLVSAQ FTVIGPAEPI LAMVGENTTL HCHLSPERNA
EEMEVRWFRW RFFPAVLVYR GHQERPEEQM VAYRGRTTFM RTDISKGRVA LIIHNVTAYD
NGIYCCYFQE GRSYDQATMK LMVASLGSEP LIKMKTLEDG SILLECTSEG WYPEPRAVWR
DPYDEVVPAL EEEYTADREG LFTVTMTIII RDCSVRNMTC SVNNTLLSQE VESVILIPES
FVPSLPLWMV AVAVTLPVVM LILLTSGSIC LVKKHRRKKS ILSAEKEAEY EEKEAARQLQ
EELRWRRTLL HAADVVLDPD TAHPELFLSD DQRSVIRGSS RQSVPDNPER FDCRPCVLGR
ESFSSGKHYW EVEVENVMVW AIGVCRDSVE RKGEALLVPQ NGFWTLEMFG SQYRALSSPE
KIIPLKERLH RIAVFLDCEG GDISFYNMRD RSHIYTCPPV TFTGPLRPFF RLGSDDSPLF
ICPAFTGAQG VTIPEGGLFL YKTRPISQSL VRKP
