ID BT3A2_HUMAN Reviewed; 334 AA. AC P78410; B4DRT7; B4E103; F5H791; F8W6E0; O00477; O15338; O75658; Q76PA0; AC Q9BU81; Q9NR44; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 2. DT 27-MAR-2024, entry version 182. DE RecName: Full=Butyrophilin subfamily 3 member A2; DE Flags: Precursor; GN Name=BTN3A2; Synonyms=BT3.2, BTF3, BTF4; 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 1). 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11170752; DOI=10.1006/geno.2000.6406; RA Rhodes D.A., Stammers M., Malcherek G., Beck S., Trowsdale J.; RT "The cluster of BTN genes in the extended major histocompatibility RT complex."; RL Genomics 71:351-362(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ASP-181; RP THR-182 AND ASN-307. RC TISSUE=Thymus, and Tongue; 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 [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 MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Skin; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-286, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] RP GLYCOSYLATION. 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=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 [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 sensing RT by a major human gammadelta T-cell subset."; RL Blood 120:2269-2279(2012). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 30-239, SUBUNIT, AND DISULFIDE RP 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. Inhibits the release of IFNG from activated T-cells. CC {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22846996}. CC -!- INTERACTION: CC P78410; O00481: BTN3A1; NbExp=3; IntAct=EBI-17564670, EBI-2809309; CC P78410; P57739: CLDN2; NbExp=3; IntAct=EBI-17564670, EBI-751440; CC P78410; Q96CV9: OPTN; NbExp=3; IntAct=EBI-17564670, EBI-748974; 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=3; CC Name=1; CC IsoId=P78410-1; Sequence=Displayed; CC Name=2; CC IsoId=P78410-2; Sequence=VSP_045907; CC Name=3; CC IsoId=P78410-3; Sequence=VSP_045906; CC -!- TISSUE SPECIFICITY: Detected in T-cells and natural killer cells. CC {ECO:0000269|PubMed:21918970}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20610803}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB53424.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAC02652.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAC02655.1; Type=Frameshift; 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; U90546; AAB53424.1; ALT_FRAME; mRNA. DR EMBL; U90144; AAC02652.1; ALT_FRAME; mRNA. DR EMBL; U97499; AAC02655.1; ALT_FRAME; Genomic_DNA. DR EMBL; U97498; AAC02655.1; JOINED; Genomic_DNA. DR EMBL; AF257505; AAF76140.1; -; mRNA. DR EMBL; AK299417; BAG61399.1; -; mRNA. DR EMBL; AK303600; BAG64615.1; -; mRNA. DR EMBL; AL021917; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002832; AAH02832.3; -; mRNA. DR EMBL; BC020214; AAH20214.3; -; mRNA. DR CCDS; CCDS4605.1; -. [P78410-1] DR CCDS; CCDS56399.1; -. [P78410-2] DR CCDS; CCDS56400.1; -. [P78410-3] DR RefSeq; NP_001184175.1; NM_001197246.2. [P78410-1] DR RefSeq; NP_001184176.1; NM_001197247.2. [P78410-1] DR RefSeq; NP_001184177.1; NM_001197248.2. [P78410-2] DR RefSeq; NP_001184178.1; NM_001197249.2. [P78410-3] DR RefSeq; NP_008978.2; NM_007047.4. [P78410-1] DR RefSeq; XP_005248884.1; XM_005248827.3. [P78410-1] DR RefSeq; XP_016865700.1; XM_017010211.1. DR RefSeq; XP_016865701.1; XM_017010212.1. DR RefSeq; XP_016865703.1; XM_017010214.1. DR PDB; 4F8Q; X-ray; 2.38 A; A=30-239. DR PDBsum; 4F8Q; -. DR AlphaFoldDB; P78410; -. DR SMR; P78410; -. DR BioGRID; 116293; 33. DR IntAct; P78410; 8. DR STRING; 9606.ENSP00000366937; -. DR GlyConnect; 1049; 1 N-Linked glycan (1 site). DR GlyCosmos; P78410; 1 site, No reported glycans. DR GlyGen; P78410; 1 site. DR iPTMnet; P78410; -. DR PhosphoSitePlus; P78410; -. DR BioMuta; BTN3A2; -. DR DMDM; 67462189; -. DR EPD; P78410; -. DR jPOST; P78410; -. DR MassIVE; P78410; -. DR MaxQB; P78410; -. DR PaxDb; 9606-ENSP00000348751; -. DR PeptideAtlas; P78410; -. DR ProteomicsDB; 27417; -. DR ProteomicsDB; 29764; -. DR ProteomicsDB; 57615; -. [P78410-1] DR Pumba; P78410; -. DR Antibodypedia; 25604; 133 antibodies from 18 providers. DR DNASU; 11118; -. DR Ensembl; ENST00000356386.6; ENSP00000348751.2; ENSG00000186470.14. [P78410-1] DR Ensembl; ENST00000377708.7; ENSP00000366937.2; ENSG00000186470.14. [P78410-1] DR Ensembl; ENST00000396934.7; ENSP00000380140.3; ENSG00000186470.14. [P78410-2] DR Ensembl; ENST00000396948.5; ENSP00000380152.1; ENSG00000186470.14. [P78410-1] DR Ensembl; ENST00000508906.6; ENSP00000442687.1; ENSG00000186470.14. [P78410-3] DR Ensembl; ENST00000527422.5; ENSP00000432138.1; ENSG00000186470.14. [P78410-1] DR GeneID; 11118; -. DR KEGG; hsa:11118; -. DR MANE-Select; ENST00000377708.7; ENSP00000366937.2; NM_007047.5; NP_008978.2. DR UCSC; uc003nhp.5; human. [P78410-1] DR AGR; HGNC:1139; -. DR CTD; 11118; -. DR DisGeNET; 11118; -. DR GeneCards; BTN3A2; -. DR HGNC; HGNC:1139; BTN3A2. DR HPA; ENSG00000186470; Tissue enhanced (lymphoid). DR MIM; 613594; gene. DR neXtProt; NX_P78410; -. DR OpenTargets; ENSG00000186470; -. DR PharmGKB; PA25460; -. DR VEuPathDB; HostDB:ENSG00000186470; -. DR eggNOG; ENOG502QSRZ; Eukaryota. DR GeneTree; ENSGT00940000162723; -. DR InParanoid; P78410; -. DR OMA; LHTPCSA; -. DR OrthoDB; 2943983at2759; -. DR PhylomeDB; P78410; -. DR TreeFam; TF331083; -. DR PathwayCommons; P78410; -. DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions. DR SignaLink; P78410; -. DR BioGRID-ORCS; 11118; 18 hits in 1140 CRISPR screens. DR ChiTaRS; BTN3A2; human. DR GenomeRNAi; 11118; -. DR Pharos; P78410; Tbio. DR PRO; PR:P78410; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P78410; Protein. DR Bgee; ENSG00000186470; Expressed in granulocyte and 194 other cell types or tissues. DR ExpressionAtlas; P78410; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. 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:0032729; P:positive regulation of type II interferon production; IMP:UniProtKB. DR GO; GO:0001817; P:regulation of cytokine production; 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; cd05713; IgV_MOG_like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. 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 PANTHER; PTHR24100; BUTYROPHILIN; 1. DR PANTHER; PTHR24100:SF115; BUTYROPHILIN SUBFAMILY 3 MEMBER A2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; P78410; HS. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; KW Coiled coil; Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..334 FT /note="Butyrophilin subfamily 3 member A2" FT /id="PRO_0000014533" FT TOPO_DOM 30..248 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 249..269 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 270..334 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..139 FT /note="Ig-like V-type" FT COILED 272..319 FT /evidence="ECO:0000255" FT MOD_RES 282 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 286 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT CARBOHYD 115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" 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 1..42 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_045906" FT VAR_SEQ 1..28 FT /note="MKMASSLAFLLLNFHVSLLLVQLLTPCS -> MGIPR (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045907" FT VARIANT 167 FT /note="R -> T (in dbSNP:rs9379861)" FT /id="VAR_049833" FT VARIANT 181 FT /note="N -> D (in dbSNP:rs9358936)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_026211" FT VARIANT 182 FT /note="A -> T (in dbSNP:rs12205731)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_049834" FT VARIANT 211 FT /note="R -> K (in dbSNP:rs35183513)" FT /id="VAR_049835" FT VARIANT 307 FT /note="S -> N (in dbSNP:rs13216828)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_049836" FT CONFLICT 63 FT /note="M -> L (in Ref. 4; BAG64615)" FT /evidence="ECO:0000305" FT CONFLICT 180 FT /note="S -> G (in Ref. 3; AAF76140)" FT /evidence="ECO:0000305" FT CONFLICT 211..212 FT /note="RG -> KS (in Ref. 3; AAF76140)" FT /evidence="ECO:0000305" FT CONFLICT 327 FT /note="S -> L (in Ref. 2; AAC02655)" FT /evidence="ECO:0000305" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 48..56 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:4F8Q" FT TURN 70..73 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 74..80 FT /evidence="ECO:0007829|PDB:4F8Q" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:4F8Q" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:4F8Q" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:4F8Q" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:4F8Q" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 122..130 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 133..145 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 161..173 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 176..180 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 202..210 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 217..224 FT /evidence="ECO:0007829|PDB:4F8Q" FT TURN 225..228 FT /evidence="ECO:0007829|PDB:4F8Q" FT STRAND 229..236 FT /evidence="ECO:0007829|PDB:4F8Q" SQ SEQUENCE 334 AA; 36428 MW; 940519D57F95EEE4 CRC64; MKMASSLAFL LLNFHVSLLL VQLLTPCSAQ FSVLGPSGPI LAMVGEDADL PCHLFPTMSA ETMELKWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL RDGITAGKAA LRIHNVTASD SGKYLCYFQD GDFYEKALVE LKVAALGSNL HVEVKGYEDG GIHLECRSTG WYPQPQIQWS NAKGENIPAV EAPVVADGVG LYEVAASVIM RGGSGEGVSC IIRNSLLGLE KTASISIADP FFRSAQPWIA ALAGTLPILL LLLAGASYFL WRQQKEITAL SSEIESEQEM KEMGYAATER EISLRESLQE ELKRKKIQYL TRGEESSSDT NKSA //