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   27-MAR-2024, entry version 148.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; P18892; 2 sites, No reported glycans.
DR   iPTMnet; P18892; -.
DR   PaxDb; 9913-ENSBTAP00000042450; -.
DR   PeptideAtlas; P18892; -.
DR   GeneID; 282157; -.
DR   KEGG; bta:282157; -.
DR   CTD; 696; -.
DR   eggNOG; ENOG502QSRZ; Eukaryota.
DR   InParanoid; P18892; -.
DR   OrthoDB; 2943983at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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; cd05713; IgV_MOG_like; 1.
DR   CDD; cd15819; SPRY_PRY_BTN1_2; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR24100; BUTYROPHILIN; 1.
DR   PANTHER; PTHR24100:SF145; BUTYROPHILIN SUBFAMILY 1 MEMBER A1; 1.
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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
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
//