ID BT3A1_HUMAN Reviewed; 513 AA. AC O00481; A2A278; A8K2C8; B4DIQ1; B4DRM2; E9PGB4; E9PHG8; Q0P515; AC Q147X5; Q53F15; Q99420; Q9HCY1; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 3. DT 13-FEB-2019, entry version 164. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Mather I.H., Pontarotti P.; RT "Cloning, localization, and structure of new members of the RT butyrophilin gene family in the juxta-telomeric region of the major RT histocompatibility complex."; RL Immunogenetics 47:55-63(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND RP VARIANTS 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., 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 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., 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RP 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 RT project: 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; 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., 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 [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 RT sensing 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 CC immune response. Regulates the proliferation of activated T-cells. CC Regulates the release of cytokines and IFNG by activated T-cells. CC Mediates the response of T-cells toward infected and transformed CC cells that are characterized by high levels of phosphorylated CC metabolites, such as isopentenyl pyrophosphate. CC {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, CC ECO:0000269|PubMed:22767497, ECO:0000269|PubMed:22846996}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22846996}. CC -!- INTERACTION: CC O60437:PPL; NbExp=6; IntAct=EBI-2809309, EBI-368321; CC P04155:TFF1; NbExp=3; IntAct=EBI-2809309, EBI-743871; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21113407, CC ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single- CC pass 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 Note=No experimental confirmation available.; CC Name=3; CC IsoId=O00481-3; Sequence=VSP_042034; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O00481-4; Sequence=VSP_045062; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Detected on T-cells, natural killer cells, CC dendritic cells and macrophages (at protein level). Ubiquitous. CC Highly expressed in heart, pancreas and lung, Moderately expressed CC in 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 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA69164.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; 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 UniGene; Hs.191510; -. 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 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 ProteinModelPortal; O00481; -. DR SMR; O00481; -. DR BioGrid; 116294; 14. DR IntAct; O00481; 3. DR STRING; 9606.ENSP00000289361; -. DR GlyConnect; 1048; -. DR iPTMnet; O00481; -. DR PhosphoSitePlus; O00481; -. DR BioMuta; BTN3A1; -. DR EPD; O00481; -. DR jPOST; O00481; -. DR MaxQB; O00481; -. DR PaxDb; O00481; -. DR PeptideAtlas; O00481; -. DR PRIDE; O00481; -. DR ProteomicsDB; 47925; -. DR ProteomicsDB; 47926; -. [O00481-2] DR ProteomicsDB; 47927; -. [O00481-3] DR Ensembl; ENST00000289361; ENSP00000289361; ENSG00000026950. [O00481-1] DR Ensembl; ENST00000414912; ENSP00000406667; ENSG00000026950. [O00481-4] DR Ensembl; ENST00000425234; ENSP00000396684; ENSG00000026950. [O00481-3] DR Ensembl; ENST00000476549; ENSP00000420010; ENSG00000026950. [O00481-2] DR GeneID; 11119; -. DR KEGG; hsa:11119; -. DR UCSC; uc003nhv.3; human. [O00481-1] DR CTD; 11119; -. DR DisGeNET; 11119; -. DR EuPathDB; HostDB:ENSG00000026950.16; -. DR GeneCards; BTN3A1; -. DR HGNC; HGNC:1138; BTN3A1. DR HPA; HPA012565; -. DR MIM; 613593; gene. DR neXtProt; NX_O00481; -. DR OpenTargets; ENSG00000026950; -. DR PharmGKB; PA25459; -. DR eggNOG; ENOG410IJI4; Eukaryota. DR eggNOG; ENOG410YA6W; LUCA. DR GeneTree; ENSGT00940000163036; -. DR HOGENOM; HOG000230860; -. DR HOVERGEN; HBG050747; -. DR InParanoid; O00481; -. DR KO; K06712; -. DR OMA; LENESCW; -. DR OrthoDB; 522383at2759; -. DR PhylomeDB; O00481; -. DR TreeFam; TF331083; -. DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions. DR ChiTaRS; BTN3A1; human. DR GeneWiki; Butyrophilin,_subfamily_3,_member_A1; -. DR GenomeRNAi; 11119; -. DR PRO; PR:O00481; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000026950; Expressed in 213 organ(s), highest expression level in small intestine Peyer's patch. 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:0050663; P:cytokine secretion; IDA:UniProtKB. DR GO; GO:0072643; P:interferon-gamma secretion; IMP:UniProtKB. DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central. DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB. DR CDD; cd15820; SPRY_PRY_BTN3; 1. DR Gene3D; 2.60.40.10; -; 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; Disulfide bond; Glycoprotein; Immunity; KW Immunoglobulin domain; Membrane; Polymorphism; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 513 Butyrophilin subfamily 3 member A1. FT /FTId=PRO_0000014532. FT TOPO_DOM 30 254 Extracellular. {ECO:0000255}. FT TRANSMEM 255 271 Helical. {ECO:0000255}. FT TOPO_DOM 272 513 Cytoplasmic. {ECO:0000255}. FT DOMAIN 30 139 Ig-like V-type 1. FT DOMAIN 145 236 Ig-like V-type 2. FT DOMAIN 322 513 B30.2/SPRY. {ECO:0000255|PROSITE- FT ProRule:PRU00548}. FT CARBOHYD 115 115 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22846996}. 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 143 194 Missing (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_045062. FT VAR_SEQ 340 513 ADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNW FT HYCVLGCESFISGRHYWEVEVGDRKEWHIGVCSKNVQRKGW FT VKMTPENGFWTMGLTDGNKYRTLTEPRTNLKLPKPPKKVGV FT FLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTL FT EPTALTICPA -> GPPIGQTQQQTRGQGSPVALSQESAQR FT TDSWGPEEGGES (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_042034. FT VAR_SEQ 340 352 ADVILDPKTANPI -> GEEMLQMRLHFVK (in FT isoform 2). {ECO:0000303|PubMed:9382921}. FT /FTId=VSP_012714. FT VAR_SEQ 353 513 Missing (in isoform 2). FT {ECO:0000303|PubMed:9382921}. FT /FTId=VSP_012715. FT VARIANT 15 15 R -> H (in dbSNP:rs56161420). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_061305. FT VARIANT 224 224 S -> N (in dbSNP:rs1057933). FT {ECO:0000269|PubMed:9382921}. FT /FTId=VAR_021170. FT VARIANT 282 282 R -> T (in dbSNP:rs41266839). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_061306. FT VARIANT 456 456 P -> T (in dbSNP:rs4712990). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_028788. FT CONFLICT 13 13 N -> S (in Ref. 3; BAG58563). FT {ECO:0000305}. FT CONFLICT 25 25 M -> T (in Ref. 4; BAD97194). FT {ECO:0000305}. FT CONFLICT 46 46 E -> K (in Ref. 3; BAG61334). FT {ECO:0000305}. FT CONFLICT 111 111 L -> F (in Ref. 1; CAA69164). FT {ECO:0000305}. FT CONFLICT 118 118 A -> G (in Ref. 1; CAA69164). FT {ECO:0000305}. FT CONFLICT 121 122 SG -> RW (in Ref. 1; CAA69164). FT {ECO:0000305}. FT CONFLICT 130 130 D -> G (in Ref. 3; BAG58563). FT {ECO:0000305}. FT CONFLICT 239 239 D -> R (in Ref. 1; CAA69164). FT {ECO:0000305}. FT CONFLICT 254 254 G -> R (in Ref. 2; AAB53430). FT {ECO:0000305}. FT CONFLICT 509 509 T -> S (in Ref. 2; AAB53430). FT {ECO:0000305}. FT STRAND 32 34 {ECO:0000244|PDB:4K55}. FT STRAND 40 43 {ECO:0000244|PDB:4K55}. FT STRAND 48 56 {ECO:0000244|PDB:4K55}. FT STRAND 63 69 {ECO:0000244|PDB:4K55}. FT TURN 70 73 {ECO:0000244|PDB:4K55}. FT STRAND 74 80 {ECO:0000244|PDB:4K55}. FT HELIX 86 88 {ECO:0000244|PDB:4K55}. FT HELIX 91 93 {ECO:0000244|PDB:4K55}. FT STRAND 96 100 {ECO:0000244|PDB:4K55}. FT HELIX 104 106 {ECO:0000244|PDB:4K55}. FT STRAND 108 115 {ECO:0000244|PDB:4K55}. FT HELIX 118 120 {ECO:0000244|PDB:4K55}. FT STRAND 122 130 {ECO:0000244|PDB:4K55}. FT STRAND 133 143 {ECO:0000244|PDB:4K55}. FT STRAND 151 158 {ECO:0000244|PDB:4F80}. FT STRAND 161 173 {ECO:0000244|PDB:4F80}. FT STRAND 176 180 {ECO:0000244|PDB:4F80}. FT STRAND 202 210 {ECO:0000244|PDB:4F80}. FT STRAND 218 224 {ECO:0000244|PDB:4F80}. FT TURN 225 228 {ECO:0000244|PDB:4F80}. FT STRAND 229 235 {ECO:0000244|PDB:4F80}. FT TURN 239 241 {ECO:0000244|PDB:4F80}. FT HELIX 308 320 {ECO:0000244|PDB:5HM7}. FT TURN 321 323 {ECO:0000244|PDB:5HM7}. FT HELIX 328 336 {ECO:0000244|PDB:4N7I}. FT STRAND 337 339 {ECO:0000244|PDB:4N7I}. FT HELIX 346 348 {ECO:0000244|PDB:4N7I}. FT STRAND 353 355 {ECO:0000244|PDB:4N7I}. FT STRAND 359 364 {ECO:0000244|PDB:4N7I}. FT STRAND 379 381 {ECO:0000244|PDB:4N7I}. FT STRAND 383 387 {ECO:0000244|PDB:4N7I}. FT STRAND 390 400 {ECO:0000244|PDB:4N7I}. FT STRAND 407 413 {ECO:0000244|PDB:4N7I}. FT HELIX 426 428 {ECO:0000244|PDB:4N7I}. FT STRAND 430 436 {ECO:0000244|PDB:4N7I}. FT TURN 437 439 {ECO:0000244|PDB:4N7I}. FT STRAND 440 443 {ECO:0000244|PDB:4N7I}. FT STRAND 449 451 {ECO:0000244|PDB:4V1P}. FT STRAND 458 465 {ECO:0000244|PDB:4N7I}. FT TURN 466 469 {ECO:0000244|PDB:4N7I}. FT STRAND 470 475 {ECO:0000244|PDB:4N7I}. FT TURN 476 478 {ECO:0000244|PDB:4N7I}. FT STRAND 481 485 {ECO:0000244|PDB:4N7I}. FT STRAND 494 499 {ECO:0000244|PDB:4N7I}. FT STRAND 508 510 {ECO:0000244|PDB:4N7I}. 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 //