BT1A1_MOUSE
ID BT1A1_MOUSE Reviewed; 524 AA.
AC Q62556; P97392; Q8K2H7; Q921K7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Butyrophilin subfamily 1 member A1;
DE Short=BT;
DE Flags: Precursor;
GN Name=Btn1a1; Synonyms=Btn;
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 [GENOMIC DNA].
RC STRAIN=129; TISSUE=Mammary gland;
RX PubMed=8995761; DOI=10.1007/s003359900265;
RA Ogg S.L., Komaragiri M.V.S., Mather I.H.;
RT "Structural organization and mammary-specific expression of the
RT butyrophilin gene.";
RL Mamm. Genome 7:900-905(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 38-524.
RC TISSUE=Mammary gland;
RX PubMed=8541302; DOI=10.1016/0304-4165(95)00102-6;
RA Ishii T., Aoki N., Noda A., Adachi T., Nakamura R., Matsuda T.;
RT "Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically
RT associates with a 150-kDa protein of mammary epithelial cells and milk fat
RT globule membrane.";
RL Biochim. Biophys. Acta 1245:285-292(1995).
RN [4]
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: May function in the secretion of milk-fat droplets. May act
CC as a specific membrane-associated receptor for the association of
CC cytoplasmic droplets with the apical plasma membrane (By similarity).
CC Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3
CC antibodies, T-cell metabolism and IL2 and IFNG secretion. {ECO:0000250,
CC ECO:0000269|PubMed:20208008}.
CC -!- SUBUNIT: Seems to associate with xanthine dehydrogenase/oxidase.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Note=Secreted in association with the milk-fat-globule membrane during
CC lactation.
CC -!- TISSUE SPECIFICITY: Strongly expressed in lactating mammary tissue (at
CC protein level). About 100-fold lower levels in virgin mammary tissue.
CC Also detected in spleen and thymus at 10-20 times lower levels compared
CC to those detected in virgin mammary gland. Very low levels in several
CC other tissues, including brain, heart, kidney, lymph node, lung and
CC small intestine. In the thymus, detected in the stroma, in epithelial
CC cells (at protein level). Most prominent in medullary areas of the
CC thymus and at the corticomedullary junction (at protein level).
CC {ECO:0000269|PubMed:20208008}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during the last half of
CC pregnancy and is maximal during lactation.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20208008}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB35893.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U67065; AAB51034.1; -; Genomic_DNA.
DR EMBL; BC011497; AAH11497.1; -; mRNA.
DR EMBL; BC031459; AAH31459.1; -; mRNA.
DR EMBL; S80642; AAB35893.1; ALT_FRAME; mRNA.
DR CCDS; CCDS26339.1; -.
DR PIR; S65133; S65133.
DR RefSeq; NP_038511.1; NM_013483.3.
DR RefSeq; XP_006516598.1; XM_006516535.1.
DR AlphaFoldDB; Q62556; -.
DR SMR; Q62556; -.
DR STRING; 10090.ENSMUSP00000041013; -.
DR GlyGen; Q62556; 2 sites.
DR iPTMnet; Q62556; -.
DR PhosphoSitePlus; Q62556; -.
DR PaxDb; Q62556; -.
DR PRIDE; Q62556; -.
DR Antibodypedia; 2403; 349 antibodies from 24 providers.
DR DNASU; 12231; -.
DR Ensembl; ENSMUST00000041674; ENSMUSP00000041013; ENSMUSG00000000706.
DR GeneID; 12231; -.
DR KEGG; mmu:12231; -.
DR UCSC; uc007ptq.2; mouse.
DR CTD; 696; -.
DR MGI; MGI:103118; Btn1a1.
DR VEuPathDB; HostDB:ENSMUSG00000000706; -.
DR eggNOG; ENOG502QSRZ; Eukaryota.
DR GeneTree; ENSGT00940000161530; -.
DR HOGENOM; CLU_013137_22_2_1; -.
DR InParanoid; Q62556; -.
DR OMA; AHMELRW; -.
DR OrthoDB; 522383at2759; -.
DR PhylomeDB; Q62556; -.
DR TreeFam; TF317532; -.
DR Reactome; R-MMU-8851680; Butyrophilin (BTN) family interactions.
DR BioGRID-ORCS; 12231; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Btn1a1; mouse.
DR PRO; PR:Q62556; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q62556; protein.
DR Bgee; ENSMUSG00000000706; Expressed in thoracic mammary gland and 34 other tissues.
DR ExpressionAtlas; Q62556; baseline and differential.
DR Genevisible; Q62556; MM.
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: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; IPR013162; CD80_C2-set.
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; PF08205; C2-set_2; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00409; IG; 2.
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 Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..524
FT /note="Butyrophilin subfamily 1 member A1"
FT /id="PRO_0000014528"
FT TOPO_DOM 27..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..141
FT /note="Ig-like V-type 1"
FT DOMAIN 149..235
FT /note="Ig-like V-type 2"
FT DOMAIN 286..480
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 27
FT /note="Missing (in Ref. 2; AAH31459)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="D -> DD (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="T -> K (in Ref. 2; AAH11497)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> F (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="E -> D (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="R -> S (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="V -> E (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="T -> K (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
FT CONFLICT 413..414
FT /note="SL -> FF (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
FT CONFLICT 420..423
FT /note="PRRV -> LAEY (in Ref. 3; AAB35893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 58407 MW; 333F4DE2C7704480 CRC64;
MAVPTNSCLL VCLLTLTVLQ LPTLDSAAPF DVTAPQEPVL ALVGSDAELT CGFSPNASSE
YMELLWFRQT RSTAVLLYRD GQEQEGQQMT EYRGRATLAT AGLLDGRATL LIRDVRVSDQ
GEYRCLFKDN DDFEEAAVYL KVAAVGSDPQ ISMTVQENGE MELECTSSGW YPEPQVQWRT
GNREMLPSTS ESKKHNEEGL FTVAVSMMIR DSSIKNMSCC IQNILLGQGK EVEISLPAPF
VPRLTPWIVA VAIILLALGF LTIGSIFFTW KLYKERSSLR KKEFGSKERL LEELRCKKTV
LHEVDVTLDP DTAHPHLFLY EDSKSVRLED SRQILPDRPE RFDSWPCVLG RETFTSGRHY
WEVEVGDRTD WAIGVCRENV VKKGFDPMTP DNGFWAVELY GNGYWALTPL RTSLRLAGPP
RRVGVFLDYD AGDISFYNMS NGSLIYTFPS ISFSGPLRPF FCLWSCGKKP LTICSTANGP
EKVTVIANVQ DDIPLSPLGE GCTSGDKDTL HSKLIPFSPS QAAP
