BT1A1_HUMAN
ID BT1A1_HUMAN Reviewed; 526 AA.
AC Q13410; Q4VAN3; Q4VAN4; Q9H458;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Butyrophilin subfamily 1 member A1;
DE Short=BT;
DE Flags: Precursor;
GN Name=BTN1A1; Synonyms=BTN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-213 AND GLU-503.
RC TISSUE=Mammary gland;
RX PubMed=8611614; DOI=10.1016/0167-4781(19)60000-x;
RA Taylor M.R., Peterson J.A., Ceriani R.L., Couto J.R.;
RT "Cloning and sequence analysis of human butyrophilin reveals a potential
RT receptor function.";
RL Biochim. Biophys. Acta 1306:1-4(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS THR-213 AND
RP GLU-503.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-213 AND GLU-503.
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55 AND ASN-215.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Seems to associate with xanthine dehydrogenase/oxidase.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q13410; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2372803, EBI-16439278;
CC Q13410; Q8NHP6: MOSPD2; NbExp=3; IntAct=EBI-2372803, EBI-2812848;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Secreted.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
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DR EMBL; U39576; AAC50489.1; -; mRNA.
DR EMBL; AL121936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55585.1; -; Genomic_DNA.
DR EMBL; BC096312; AAH96312.1; -; mRNA.
DR EMBL; BC096313; AAH96313.1; -; mRNA.
DR CCDS; CCDS4614.1; -.
DR PIR; S70587; S70587.
DR RefSeq; NP_001723.2; NM_001732.2.
DR AlphaFoldDB; Q13410; -.
DR SMR; Q13410; -.
DR BioGRID; 107161; 18.
DR IntAct; Q13410; 6.
DR STRING; 9606.ENSP00000244513; -.
DR GlyConnect; 2933; 33 N-Linked glycans (2 sites).
DR GlyGen; Q13410; 2 sites, 38 N-linked glycans (2 sites).
DR iPTMnet; Q13410; -.
DR PhosphoSitePlus; Q13410; -.
DR BioMuta; BTN1A1; -.
DR DMDM; 317373471; -.
DR EPD; Q13410; -.
DR jPOST; Q13410; -.
DR MassIVE; Q13410; -.
DR MaxQB; Q13410; -.
DR PaxDb; Q13410; -.
DR PeptideAtlas; Q13410; -.
DR PRIDE; Q13410; -.
DR ProteomicsDB; 59393; -.
DR Antibodypedia; 2403; 349 antibodies from 24 providers.
DR DNASU; 696; -.
DR Ensembl; ENST00000244513.10; ENSP00000244513.6; ENSG00000124557.14.
DR Ensembl; ENST00000684113.1; ENSP00000507193.1; ENSG00000124557.14.
DR GeneID; 696; -.
DR KEGG; hsa:696; -.
DR MANE-Select; ENST00000684113.1; ENSP00000507193.1; NM_001732.3; NP_001723.2.
DR UCSC; uc003nif.5; human.
DR CTD; 696; -.
DR DisGeNET; 696; -.
DR GeneCards; BTN1A1; -.
DR HGNC; HGNC:1135; BTN1A1.
DR HPA; ENSG00000124557; Tissue enriched (breast).
DR MIM; 601610; gene.
DR neXtProt; NX_Q13410; -.
DR OpenTargets; ENSG00000124557; -.
DR PharmGKB; PA25455; -.
DR VEuPathDB; HostDB:ENSG00000124557; -.
DR eggNOG; ENOG502QSRZ; Eukaryota.
DR GeneTree; ENSGT00940000161530; -.
DR HOGENOM; CLU_013137_22_2_1; -.
DR InParanoid; Q13410; -.
DR OMA; AHMELRW; -.
DR OrthoDB; 522383at2759; -.
DR PhylomeDB; Q13410; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; Q13410; -.
DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
DR SignaLink; Q13410; -.
DR BioGRID-ORCS; 696; 15 hits in 1066 CRISPR screens.
DR GeneWiki; Butyrophilin,_subfamily_1,_member_A1; -.
DR GenomeRNAi; 696; -.
DR Pharos; Q13410; Tbio.
DR PRO; PR:Q13410; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13410; protein.
DR Bgee; ENSG00000124557; Expressed in lymph node and 23 other tissues.
DR Genevisible; Q13410; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
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 Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..526
FT /note="Butyrophilin subfamily 1 member A1"
FT /id="PRO_0000014527"
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..138
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 REGION 495..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401"
FT DISULFID 50..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 213
FT /note="A -> T (in dbSNP:rs3736781)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8611614, ECO:0000269|Ref.3"
FT /id="VAR_021169"
FT VARIANT 303
FT /note="V -> A (in dbSNP:rs1980600)"
FT /id="VAR_030770"
FT VARIANT 503
FT /note="D -> E (in dbSNP:rs9393728)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8611614, ECO:0000269|Ref.3"
FT /id="VAR_026546"
FT VARIANT 521
FT /note="P -> S (in dbSNP:rs35555795)"
FT /id="VAR_061302"
SQ SEQUENCE 526 AA; 58960 MW; 4585D5CE88A2ECA4 CRC64;
MAVFPSSGLP RCLLTLILLQ LPKLDSAPFD VIGPPEPILA VVGEDAELPC RLSPNASAEH
LELRWFRKKV SPAVLVHRDG REQEAEQMPE YRGRATLVQD GIAKGRVALR IRGVRVSDDG
EYTCFFREDG SYEEALVHLK VAALGSDPHI SMQVQENGEI CLECTSVGWY PEPQVQWRTS
KGEKFPSTSE SRNPDEEGLF TVAASVIIRD TSAKNVSCYI QNLLLGQEKK VEISIPASSL
PRLTPWIVAV AVILMVLGLL TIGSIFFTWR LYNERPRERR NEFSSKERLL EELKWKKATL
HAVDVTLDPD TAHPHLFLYE DSKSVRLEDS RQKLPEKTER FDSWPCVLGR ETFTSGRHYW
EVEVGDRTDW AIGVCRENVM KKGFDPMTPE NGFWAVELYG NGYWALTPLR TPLPLAGPPR
RVGIFLDYES GDISFYNMND GSDIYTFSNV TFSGPLRPFF CLWSSGKKPL TICPIADGPE
RVTVIANAQD LSKEIPLSPM GEDSAPRDAD TLHSKLIPTQ PSQGAP
