BT3A1_HUMAN
ID BT3A1_HUMAN Reviewed; 513 AA.
AC O00481; A2A278; A8K2C8; B4DIQ1; B4DRM2; E9PGB4; E9PHG8; Q0P515; Q147X5;
AC Q53F15; Q99420; Q9HCY1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Butyrophilin subfamily 3 member A1;
DE AltName: CD_antigen=CD277;
DE Flags: Precursor;
GN Name=BTN3A1; Synonyms=BTF5;
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] (ISOFORM 2), AND VARIANT ASN-224.
RX PubMed=9382921; DOI=10.1007/s002510050326;
RA Tazi-Ahnini R., Henry J., Offer C., Bouissou-Bouchouata C., Mather I.H.,
RA Pontarotti P.;
RT "Cloning, localization, and structure of new members of the butyrophilin
RT gene family in the juxta-telomeric region of the major histocompatibility
RT complex.";
RL Immunogenetics 47:55-63(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9149941; DOI=10.1101/gr.7.5.441;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANTS
RP HIS-15 AND THR-282.
RC TISSUE=Hippocampus, and Thalamus;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 MRNA] (ISOFORM 1).
RC TISSUE=Synovium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-456.
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 [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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21113407; DOI=10.18632/oncotarget.165;
RA Cubillos-Ruiz J.R., Martinez D., Scarlett U.K., Rutkowski M.R.,
RA Nesbeth Y.C., Camposeco-Jacobs A.L., Conejo-Garcia J.R.;
RT "CD277 is a negative co-stimulatory molecule universally expressed by
RT ovarian cancer microenvironmental cells.";
RL Oncotarget 1:329-338(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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., Hirsch I.,
RA Nunes J.A., Olive D.;
RT "Differential role for CD277 as a co-regulator of the immune signal in T
RT and NK cells.";
RL Eur. J. Immunol. 41:3443-3454(2011).
RN [11]
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 sensing
RT by a major human gammadelta T-cell subset.";
RL Blood 120:2269-2279(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 30-246, FUNCTION, SUBUNIT,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-115.
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 activation and in the adaptive immune
CC response. Regulates the proliferation of activated T-cells. Regulates
CC the release of cytokines and IFNG by activated T-cells. Mediates the
CC response of T-cells toward infected and transformed cells that are
CC characterized by high levels of phosphorylated metabolites, such as
CC isopentenyl pyrophosphate. {ECO:0000269|PubMed:21113407,
CC ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497,
CC ECO:0000269|PubMed:22846996}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22846996}.
CC -!- INTERACTION:
CC O00481; P78410: BTN3A2; NbExp=3; IntAct=EBI-2809309, EBI-17564670;
CC O00481; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2809309, EBI-10976677;
CC O00481; O60437: PPL; NbExp=6; IntAct=EBI-2809309, EBI-368321;
CC O00481; P04155: TFF1; NbExp=3; IntAct=EBI-2809309, EBI-743871;
CC O00481-2; O60437: PPL; NbExp=5; IntAct=EBI-14033666, EBI-368321;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21113407,
CC ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:21113407,
CC ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O00481-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00481-2; Sequence=VSP_012714, VSP_012715;
CC Name=3;
CC IsoId=O00481-3; Sequence=VSP_042034;
CC Name=4;
CC IsoId=O00481-4; Sequence=VSP_045062;
CC -!- TISSUE SPECIFICITY: Detected on T-cells, natural killer cells,
CC dendritic cells and macrophages (at protein level). Ubiquitous. Highly
CC expressed in heart, pancreas and lung, Moderately expressed in
CC placenta, liver and muscle. {ECO:0000269|PubMed:20610803,
CC ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970,
CC ECO:0000269|PubMed:9149941}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20610803,
CC ECO:0000269|PubMed:22846996}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA69164.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y07827; CAA69164.1; ALT_INIT; mRNA.
DR EMBL; U90552; AAB53430.1; -; mRNA.
DR EMBL; AK223474; BAD97194.1; -; mRNA.
DR EMBL; AK290193; BAF82882.1; -; mRNA.
DR EMBL; AK295720; BAG58563.1; -; mRNA.
DR EMBL; AK299327; BAG61334.1; -; mRNA.
DR EMBL; AL021917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55566.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55567.1; -; Genomic_DNA.
DR EMBL; BC118586; AAI18587.1; -; mRNA.
DR EMBL; BC121800; AAI21801.1; -; mRNA.
DR CCDS; CCDS4608.1; -. [O00481-1]
DR CCDS; CCDS4609.1; -. [O00481-2]
DR CCDS; CCDS47388.1; -. [O00481-4]
DR CCDS; CCDS47389.1; -. [O00481-3]
DR RefSeq; NP_001138480.1; NM_001145008.1. [O00481-4]
DR RefSeq; NP_001138481.1; NM_001145009.1. [O00481-3]
DR RefSeq; NP_008979.3; NM_007048.5. [O00481-1]
DR RefSeq; NP_919423.1; NM_194441.2. [O00481-2]
DR RefSeq; XP_005248891.1; XM_005248834.3. [O00481-2]
DR PDB; 4F80; X-ray; 1.94 A; A=30-246.
DR PDB; 4F9L; X-ray; 3.14 A; A/B=30-246.
DR PDB; 4F9P; X-ray; 3.52 A; A/B=30-246.
DR PDB; 4JKW; X-ray; 2.01 A; A=28-143.
DR PDB; 4K55; X-ray; 1.91 A; A=28-143.
DR PDB; 4N7I; X-ray; 1.40 A; A=328-513.
DR PDB; 4N7U; X-ray; 1.46 A; A=328-513.
DR PDB; 4V1P; X-ray; 2.04 A; A=325-512.
DR PDB; 5HM7; X-ray; 1.93 A; A/B=272-513.
DR PDB; 5LYG; X-ray; 1.60 A; A=327-513.
DR PDB; 5LYK; X-ray; 1.70 A; A=327-513.
DR PDB; 5ZXK; X-ray; 1.96 A; A=328-513.
DR PDB; 6ISM; X-ray; 1.25 A; A=328-513.
DR PDB; 6ITA; X-ray; 1.20 A; A=328-513.
DR PDB; 6J06; X-ray; 2.65 A; A/B/C=328-513.
DR PDB; 6XLQ; X-ray; 3.00 A; A/D/G/J=30-255.
DR PDBsum; 4F80; -.
DR PDBsum; 4F9L; -.
DR PDBsum; 4F9P; -.
DR PDBsum; 4JKW; -.
DR PDBsum; 4K55; -.
DR PDBsum; 4N7I; -.
DR PDBsum; 4N7U; -.
DR PDBsum; 4V1P; -.
DR PDBsum; 5HM7; -.
DR PDBsum; 5LYG; -.
DR PDBsum; 5LYK; -.
DR PDBsum; 5ZXK; -.
DR PDBsum; 6ISM; -.
DR PDBsum; 6ITA; -.
DR PDBsum; 6J06; -.
DR PDBsum; 6XLQ; -.
DR AlphaFoldDB; O00481; -.
DR SMR; O00481; -.
DR BioGRID; 116294; 22.
DR IntAct; O00481; 6.
DR STRING; 9606.ENSP00000289361; -.
DR BindingDB; O00481; -.
DR ChEMBL; CHEMBL4105758; -.
DR GlyConnect; 1048; 1 N-Linked glycan (1 site).
DR GlyGen; O00481; 3 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O00481; -.
DR PhosphoSitePlus; O00481; -.
DR BioMuta; BTN3A1; -.
DR EPD; O00481; -.
DR jPOST; O00481; -.
DR MassIVE; O00481; -.
DR MaxQB; O00481; -.
DR PaxDb; O00481; -.
DR PeptideAtlas; O00481; -.
DR PRIDE; O00481; -.
DR ProteomicsDB; 20280; -.
DR ProteomicsDB; 47925; -. [O00481-1]
DR ProteomicsDB; 47926; -. [O00481-2]
DR ProteomicsDB; 47927; -. [O00481-3]
DR ABCD; O00481; 2 sequenced antibodies.
DR Antibodypedia; 2248; 245 antibodies from 31 providers.
DR DNASU; 11119; -.
DR Ensembl; ENST00000289361.11; ENSP00000289361.6; ENSG00000026950.17. [O00481-1]
DR Ensembl; ENST00000414912.2; ENSP00000406667.2; ENSG00000026950.17. [O00481-4]
DR Ensembl; ENST00000425234.6; ENSP00000396684.2; ENSG00000026950.17. [O00481-3]
DR Ensembl; ENST00000476549.6; ENSP00000420010.2; ENSG00000026950.17. [O00481-2]
DR GeneID; 11119; -.
DR KEGG; hsa:11119; -.
DR MANE-Select; ENST00000289361.11; ENSP00000289361.6; NM_007048.6; NP_008979.3.
DR UCSC; uc003nhv.3; human. [O00481-1]
DR CTD; 11119; -.
DR DisGeNET; 11119; -.
DR GeneCards; BTN3A1; -.
DR HGNC; HGNC:1138; BTN3A1.
DR HPA; ENSG00000026950; Low tissue specificity.
DR MIM; 613593; gene.
DR neXtProt; NX_O00481; -.
DR OpenTargets; ENSG00000026950; -.
DR PharmGKB; PA25459; -.
DR VEuPathDB; HostDB:ENSG00000026950; -.
DR eggNOG; ENOG502QSRZ; Eukaryota.
DR GeneTree; ENSGT00940000163036; -.
DR HOGENOM; CLU_013137_8_4_1; -.
DR InParanoid; O00481; -.
DR OMA; CRSARWY; -.
DR OrthoDB; 522383at2759; -.
DR PhylomeDB; O00481; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; O00481; -.
DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
DR SignaLink; O00481; -.
DR BioGRID-ORCS; 11119; 11 hits in 1080 CRISPR screens.
DR ChiTaRS; BTN3A1; human.
DR GeneWiki; Butyrophilin,_subfamily_3,_member_A1; -.
DR GenomeRNAi; 11119; -.
DR Pharos; O00481; Tchem.
DR PRO; PR:O00481; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O00481; protein.
DR Bgee; ENSG00000026950; Expressed in granulocyte and 190 other tissues.
DR ExpressionAtlas; O00481; baseline and differential.
DR Genevisible; O00481; 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:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0050798; P:activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR CDD; cd15820; SPRY_PRY_BTN3; 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; 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 Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..513
FT /note="Butyrophilin subfamily 3 member A1"
FT /id="PRO_0000014532"
FT TOPO_DOM 30..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..139
FT /note="Ig-like V-type 1"
FT DOMAIN 145..236
FT /note="Ig-like V-type 2"
FT DOMAIN 322..513
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22846996"
FT DISULFID 52..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:22846996"
FT DISULFID 166..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:22846996"
FT VAR_SEQ 143..194
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045062"
FT VAR_SEQ 340..513
FT /note="ADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNWHYCVLGCESFI
FT SGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPENGFWTMGLTDGNKYRTLTEPRTN
FT LKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTLEPTALT
FT ICPA -> GPPIGQTQQQTRGQGSPVALSQESAQRTDSWGPEEGGES (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042034"
FT VAR_SEQ 340..352
FT /note="ADVILDPKTANPI -> GEEMLQMRLHFVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9382921"
FT /id="VSP_012714"
FT VAR_SEQ 353..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9382921"
FT /id="VSP_012715"
FT VARIANT 15
FT /note="R -> H (in dbSNP:rs56161420)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061305"
FT VARIANT 224
FT /note="S -> N (in dbSNP:rs1057933)"
FT /evidence="ECO:0000269|PubMed:9382921"
FT /id="VAR_021170"
FT VARIANT 282
FT /note="R -> T (in dbSNP:rs41266839)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061306"
FT VARIANT 456
FT /note="P -> T (in dbSNP:rs4712990)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028788"
FT CONFLICT 13
FT /note="N -> S (in Ref. 3; BAG58563)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="M -> T (in Ref. 4; BAD97194)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="E -> K (in Ref. 3; BAG61334)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="L -> F (in Ref. 1; CAA69164)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="A -> G (in Ref. 1; CAA69164)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..122
FT /note="SG -> RW (in Ref. 1; CAA69164)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="D -> G (in Ref. 3; BAG58563)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="D -> R (in Ref. 1; CAA69164)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="G -> R (in Ref. 2; AAB53430)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="T -> S (in Ref. 2; AAB53430)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:4K55"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4K55"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4K55"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4K55"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:4K55"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:4K55"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:4F80"
FT STRAND 161..173
FT /evidence="ECO:0007829|PDB:4F80"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4F80"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:6XLQ"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:4F80"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:4F80"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:4F80"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:4F80"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4F80"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:5HM7"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:5HM7"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6ISM"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 390..400
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:6ITA"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:6ITA"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6ISM"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:6ITA"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:6ITA"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:6ITA"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:6ITA"
SQ SEQUENCE 513 AA; 57677 MW; 8D834D70526D1F6F CRC64;
MKMASFLAFL LLNFRVCLLL LQLLMPHSAQ FSVLGPSGPI LAMVGEDADL PCHLFPTMSA
ETMELKWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL RDGITAGKAA LRIHNVTASD
SGKYLCYFQD GDFYEKALVE LKVAALGSDL HVDVKGYKDG GIHLECRSTG WYPQPQIQWS
NNKGENIPTV EAPVVADGVG LYAVAASVIM RGSSGEGVSC TIRSSLLGLE KTASISIADP
FFRSAQRWIA ALAGTLPVLL LLLGGAGYFL WQQQEEKKTQ FRKKKREQEL REMAWSTMKQ
EQSTRVKLLE ELRWRSIQYA SRGERHSAYN EWKKALFKPA DVILDPKTAN PILLVSEDQR
SVQRAKEPQD LPDNPERFNW HYCVLGCESF ISGRHYWEVE VGDRKEWHIG VCSKNVQRKG
WVKMTPENGF WTMGLTDGNK YRTLTEPRTN LKLPKPPKKV GVFLDYETGD ISFYNAVDGS
HIHTFLDVSF SEALYPVFRI LTLEPTALTI CPA
