BT1A1_BOVIN
ID BT1A1_BOVIN Reviewed; 526 AA.
AC P18892; O18955; O18959; O46535; Q6RUS3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Butyrophilin subfamily 1 member A1;
DE Short=BT;
DE Flags: Precursor;
GN Name=BTN1A1; Synonyms=BTN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-47.
RX PubMed=2387867; DOI=10.1016/s0021-9258(18)77328-6;
RA Jack L.J.W., Mather I.H.;
RT "Cloning and analysis of cDNA encoding bovine butyrophilin, an apical
RT glycoprotein expressed in mammary tissue and secreted in association with
RT the milk-fat globule membrane during lactation.";
RL J. Biol. Chem. 265:14481-14486(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein-Friesian;
RA Davey H.W., Ogg S.L., Husaini Y., Snell R.G., Korobko I.V., Mather I.H.,
RA Wilkins R.J.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RA Seyfert H.-M., Luethen F.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-286.
RA Husaini Y., Wilkins R.J., Davey H.W.;
RT "Identification of five allelic polymorphisms in the bovine butyrophilin
RT gene.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 397-526.
RC TISSUE=Blood;
RA Bhattacharya T.K., Misra S.S., Sheikh F.D., Dayal S., Vohra V., Kumar P.,
RA Sharma A.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GLYCOSYLATION AT ASN-55 AND ASN-215.
RX PubMed=7775382; DOI=10.1093/oxfordjournals.jbchem.a124702;
RA Sato T., Takio K., Kobata A., Greenwalt D.E., Furukawa K.;
RT "Site-specific glycosylation of bovine butyrophilin.";
RL J. Biochem. 117:147-157(1995).
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. Inhibits the
CC proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies,
CC T-cell metabolism and IL2 and IFNG secretion (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Seems to associate with xanthine dehydrogenase/oxidase.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Note=Secreted in association with the milk-fat-globule membrane during
CC lactation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in mammary tissue.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
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DR EMBL; M35551; AAB39766.1; -; mRNA.
DR EMBL; AF005497; AAB62889.1; -; Genomic_DNA.
DR EMBL; Z93323; CAB07533.1; -; Genomic_DNA.
DR EMBL; AF037402; AAB92578.2; -; Genomic_DNA.
DR EMBL; AY491469; AAR85488.1; -; Genomic_DNA.
DR PIR; A37821; A37821.
DR RefSeq; NP_776933.1; NM_174508.2.
DR RefSeq; XP_015315455.1; XM_015459969.1.
DR RefSeq; XP_015324493.1; XM_015469007.1.
DR PDB; 4HH8; X-ray; 2.30 A; A=27-238.
DR PDBsum; 4HH8; -.
DR AlphaFoldDB; P18892; -.
DR SMR; P18892; -.
DR STRING; 9913.ENSBTAP00000042450; -.
DR CarbonylDB; P18892; -.
DR iPTMnet; P18892; -.
DR PeptideAtlas; P18892; -.
DR PRIDE; P18892; -.
DR GeneID; 282157; -.
DR KEGG; bta:282157; -.
DR CTD; 696; -.
DR eggNOG; ENOG502QSRZ; Eukaryota.
DR InParanoid; P18892; -.
DR OrthoDB; 522383at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; 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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2387867"
FT CHAIN 27..526
FT /note="Butyrophilin subfamily 1 member A1"
FT /id="PRO_0000014526"
FT TOPO_DOM 27..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..140
FT /note="Ig-like V-type 1"
FT DOMAIN 148..234
FT /note="Ig-like V-type 2"
FT DOMAIN 285..479
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:7775382"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) (hybrid) asparagine"
FT /evidence="ECO:0000269|PubMed:7775382"
FT DISULFID 50..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 16
FT /note="F -> Y (in Ref. 4; AAB92578)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="Q -> P (in Ref. 3; CAB07533)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="E -> D (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 61..78
FT /evidence="ECO:0007829|PDB:4HH8"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4HH8"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:4HH8"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4HH8"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4HH8"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 160..171
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:4HH8"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:4HH8"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:4HH8"
SQ SEQUENCE 526 AA; 59277 MW; A14126802BD19284 CRC64;
MAVFPNSCLA GCLLIFILLQ LPKLDSAPFD VIGPQEPILA VVGEDAELPC RLSPNVSAKG
MELRWFREKV SPAVFVSREG QEQEGEEMAE YRGRVSLVED HIAEGSVAVR IQEVKASDDG
EYRCFFRQDE NYEEAIVHLK VAALGSDPHI SMKVQESGEI QLECTSVGWY PEPQVQWRTH
RGEEFPSMSE SRNPDEEGLF TVRASVIIRD SSMKNVSCCI RNLLLGQEKE VEVSIPASFF
PRLTPWMVAV AVILVVLGLL TIGSIFFTWR LYKERSRQRR NEFSSKEKLL EELKWKRATL
HAVDVTLDPD TAHPHLFLYE DSKSVRLEDS RQKLPEKPER FDSWPCVMGR EAFTSGRHYW
EVEVGDRTDW AIGVCRENVM KKGFDPMTPE NGFWAVELYG NGYWALTPLR TPLPLAGPPR
RVGVFLDYES GDIFFYNMTD GSHIYTFSKA SFSGPLRPFF CLWSCGKKPL TICPVTDGLE
GVMVVADAKD ISKEIPLSPM GEDSASGDIE TLHSKLIPLQ PSQGVP
