ID BT3A3_HUMAN Reviewed; 584 AA. AC O00478; B4DWI7; E9PCP5; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 13-FEB-2019, entry version 166. DE RecName: Full=Butyrophilin subfamily 3 member A3; DE Flags: Precursor; GN Name=BTN3A3; Synonyms=BTF3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9149941; RA Ruddy D.A., Kronmal G.S., Lee V.K., Mintier G.A., Quintana L., RA Domingo R. Jr., Meyer N.C., Irrinki A., McClelland E.E., Fullan A., RA Mapa F.A., Moore T., Thomas W., Loeb D.B., Harmon C., Tsuchihashi Z., RA Wolff R.K., Schatzman R.C., Feder J.N.; RT "A 1.1-Mb transcript map of the hereditary hemochromatosis locus."; RL Genome Res. 7:441-456(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 30-44. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [8] RP GLYCOSYLATION, AND TISSUE SPECIFICITY. RX PubMed=20610803; DOI=10.1189/jlb.0309156; RA Yamashiro H., Yoshizaki S., Tadaki T., Egawa K., Seo N.; RT "Stimulation of human butyrophilin 3 molecules results in negative RT regulation of cellular immunity."; RL J. Leukoc. Biol. 88:757-767(2010). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=21918970; DOI=10.1002/eji.201141404; RA Messal N., Mamessier E., Sylvain A., Celis-Gutierrez J., Thibult M.L., RA Chetaille B., Firaguay G., Pastor S., Guillaume Y., Wang Q., RA Hirsch I., Nunes J.A., Olive D.; RT "Differential role for CD277 as a co-regulator of the immune signal in RT T and NK cells."; RL Eur. J. Immunol. 41:3443-3454(2011). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22767497; DOI=10.1182/blood-2012-05-430470; RA Harly C., Guillaume Y., Nedellec S., Peigne C.M., Monkkonen H., RA Monkkonen J., Li J., Kuball J., Adams E.J., Netzer S., RA Dechanet-Merville J., Leger A., Herrmann T., Breathnach R., Olive D., RA Bonneville M., Scotet E.; RT "Key implication of CD277/butyrophilin-3 (BTN3A) in cellular stress RT sensing by a major human gammadelta T-cell subset."; RL Blood 120:2269-2279(2012). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 30-246, SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=22846996; DOI=10.1074/jbc.M112.384354; RA Palakodeti A., Sandstrom A., Sundaresan L., Harly C., Nedellec S., RA Olive D., Scotet E., Bonneville M., Adams E.J.; RT "The molecular basis for modulation of human Vgamma9Vdelta2 T cell RT responses by CD277/butyrophilin-3 (BTN3A)-specific antibodies."; RL J. Biol. Chem. 287:32780-32790(2012). CC -!- FUNCTION: Plays a role in T-cell responses in the adaptive immune CC response. {ECO:0000269|PubMed:22767497}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22846996}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21918970, CC ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00478-1; Sequence=Displayed; CC Name=2; CC IsoId=O00478-2; Sequence=VSP_045063, VSP_045064; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Detected in peripheral blood mononuclear cells CC and in T-cells (at protein level). Detected in spleen and CC lymphocytes. {ECO:0000269|PubMed:20610803}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19349973, CC ECO:0000269|PubMed:20610803}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG CC family. {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; U90548; AAB53426.1; -; mRNA. DR EMBL; BT007251; AAP35915.1; -; mRNA. DR EMBL; AK301553; BAG63049.1; -; mRNA. DR EMBL; AL021917; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015815; AAH15815.1; -; mRNA. DR CCDS; CCDS4611.1; -. [O00478-1] DR CCDS; CCDS4612.2; -. [O00478-2] DR RefSeq; NP_001229732.1; NM_001242803.1. DR RefSeq; NP_008925.1; NM_006994.4. [O00478-1] DR RefSeq; NP_932078.2; NM_197974.2. [O00478-2] DR UniGene; Hs.167741; -. DR PDB; 4F8T; X-ray; 2.38 A; A=30-246. DR PDBsum; 4F8T; -. DR ProteinModelPortal; O00478; -. DR SMR; O00478; -. DR BioGrid; 115657; 9. DR IntAct; O00478; 4. DR STRING; 9606.ENSP00000244519; -. DR GlyConnect; 1050; -. DR iPTMnet; O00478; -. DR PhosphoSitePlus; O00478; -. DR BioMuta; BTN3A3; -. DR EPD; O00478; -. DR jPOST; O00478; -. DR MaxQB; O00478; -. DR PaxDb; O00478; -. DR PeptideAtlas; O00478; -. DR PRIDE; O00478; -. DR ProteomicsDB; 47923; -. DR DNASU; 10384; -. DR Ensembl; ENST00000244519; ENSP00000244519; ENSG00000111801. [O00478-1] DR Ensembl; ENST00000361232; ENSP00000355238; ENSG00000111801. [O00478-2] DR GeneID; 10384; -. DR KEGG; hsa:10384; -. DR UCSC; uc003nhz.3; human. [O00478-1] DR CTD; 10384; -. DR DisGeNET; 10384; -. DR EuPathDB; HostDB:ENSG00000111801.15; -. DR GeneCards; BTN3A3; -. DR HGNC; HGNC:1140; BTN3A3. DR HPA; HPA007904; -. DR HPA; HPA011871; -. DR MIM; 613595; gene. DR neXtProt; NX_O00478; -. DR OpenTargets; ENSG00000111801; -. DR PharmGKB; PA25461; -. DR eggNOG; ENOG410IJI4; Eukaryota. DR eggNOG; ENOG410YA6W; LUCA. DR GeneTree; ENSGT00940000162723; -. DR HOGENOM; HOG000230860; -. DR HOVERGEN; HBG050747; -. DR InParanoid; O00478; -. DR KO; K06712; -. DR OMA; TPFVHRY; -. DR OrthoDB; 522383at2759; -. DR PhylomeDB; O00478; -. DR TreeFam; TF331083; -. DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions. DR GeneWiki; BTN3A3; -. DR GenomeRNAi; 10384; -. DR PRO; PR:O00478; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000111801; Expressed in 217 organ(s), highest expression level in leukocyte. DR ExpressionAtlas; O00478; baseline and differential. DR Genevisible; O00478; HS. 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:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central. DR GO; GO:0002456; P:T cell mediated immunity; IMP:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central. DR CDD; cd15820; SPRY_PRY_BTN3; 1. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR001870; B30.2/SPRY. 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; IPR003877; SPRY_dom. DR InterPro; IPR037954; SPRY_PRY_BTN3. 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; Adaptive immunity; Alternative splicing; Cell membrane; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 29 {ECO:0000269|PubMed:15340161}. FT CHAIN 30 584 Butyrophilin subfamily 3 member A3. FT /FTId=PRO_0000014534. FT TOPO_DOM 30 248 Extracellular. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT TOPO_DOM 270 584 Cytoplasmic. {ECO:0000255}. FT DOMAIN 30 139 Ig-like V-type 1. FT DOMAIN 145 236 Ig-like V-type 2. FT DOMAIN 322 518 B30.2/SPRY. {ECO:0000255|PROSITE- FT ProRule:PRU00548}. FT CARBOHYD 115 115 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19349973}. FT DISULFID 52 126 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:22846996}. FT DISULFID 166 220 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:22846996}. FT VAR_SEQ 1 42 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_045063. FT VAR_SEQ 307 313 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_045064. FT CONFLICT 229 229 L -> P (in Ref. 3; BAG63049). FT {ECO:0000305}. FT STRAND 32 34 {ECO:0000244|PDB:4F8T}. FT STRAND 40 43 {ECO:0000244|PDB:4F8T}. FT STRAND 48 56 {ECO:0000244|PDB:4F8T}. FT STRAND 63 69 {ECO:0000244|PDB:4F8T}. FT TURN 70 73 {ECO:0000244|PDB:4F8T}. FT STRAND 74 80 {ECO:0000244|PDB:4F8T}. FT HELIX 91 93 {ECO:0000244|PDB:4F8T}. FT STRAND 96 100 {ECO:0000244|PDB:4F8T}. FT HELIX 104 106 {ECO:0000244|PDB:4F8T}. FT STRAND 108 115 {ECO:0000244|PDB:4F8T}. FT HELIX 118 120 {ECO:0000244|PDB:4F8T}. FT STRAND 122 130 {ECO:0000244|PDB:4F8T}. FT STRAND 133 145 {ECO:0000244|PDB:4F8T}. FT STRAND 151 158 {ECO:0000244|PDB:4F8T}. FT STRAND 161 173 {ECO:0000244|PDB:4F8T}. FT STRAND 176 181 {ECO:0000244|PDB:4F8T}. FT STRAND 202 210 {ECO:0000244|PDB:4F8T}. FT STRAND 218 224 {ECO:0000244|PDB:4F8T}. FT TURN 225 228 {ECO:0000244|PDB:4F8T}. FT STRAND 229 235 {ECO:0000244|PDB:4F8T}. FT TURN 239 241 {ECO:0000244|PDB:4F8T}. SQ SEQUENCE 584 AA; 65002 MW; 2B279B9141E0327F CRC64; MKMASSLAFL LLNFHVSLFL VQLLTPCSAQ FSVLGPSGPI LAMVGEDADL PCHLFPTMSA ETMELRWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL RDGITAGKAA LRIHNVTASD SGKYLCYFQD GDFYEKALVE LKVAALGSDL HIEVKGYEDG GIHLECRSTG WYPQPQIKWS DTKGENIPAV EAPVVADGVG LYAVAASVIM RGSSGGGVSC IIRNSLLGLE KTASISIADP FFRSAQPWIA ALAGTLPISL LLLAGASYFL WRQQKEKIAL SRETEREREM KEMGYAATEQ EISLREKLQE ELKWRKIQYM ARGEKSLAYH EWKMALFKPA DVILDPDTAN AILLVSEDQR SVQRAEEPRD LPDNPERFEW RYCVLGCENF TSGRHYWEVE VGDRKEWHIG VCSKNVERKK GWVKMTPENG YWTMGLTDGN KYRALTEPRT NLKLPEPPRK VGIFLDYETG EISFYNATDG SHIYTFPHAS FSEPLYPVFR ILTLEPTALT ICPIPKEVES SPDPDLVPDH SLETPLTPGL ANESGEPQAE VTSLLLPAHP GAEVSPSATT NQNHKLQART EALY //