ID GSTO2_HUMAN Reviewed; 243 AA. AC Q9H4Y5; A8K771; B4DJW6; E7ESD6; Q49TW5; Q5GM70; Q5JU15; Q86WP3; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 186. DE RecName: Full=Glutathione S-transferase omega-2; DE Short=GSTO-2; DE EC=2.5.1.18 {ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127}; DE AltName: Full=Glutathione S-transferase omega 2-2; DE Short=GSTO 2-2; DE AltName: Full=Glutathione-dependent dehydroascorbate reductase; DE EC=1.8.5.1 {ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127}; DE AltName: Full=Monomethylarsonic acid reductase; DE Short=MMA(V) reductase; DE EC=1.20.4.2 {ECO:0000269|PubMed:15970797}; GN Name=GSTO2; 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). RA Wang L., Xie Y., Mao Y.; RT "Cloning and characterization of human GSTO-2 gene."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Xu J., Xie Y., Mao Y.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Skeletal muscle, 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 GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Pancreatic carcinoma; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 3-243 (ISOFORM 1), VARIANT ASP-142, AND RP TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=12618591; DOI=10.1097/00008571-200303000-00003; RA Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.; RT "Characterization of the human Omega class glutathione transferase genes RT and associated polymorphisms."; RL Pharmacogenetics 13:131-144(2003). RN [8] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY. RX PubMed=15970797; DOI=10.1097/01.fpc.0000165725.81559.e3; RA Schmuck E.M., Board P.G., Whitbread A.K., Tetlow N., Cavanaugh J.A., RA Blackburn A.C., Masoumi A.; RT "Characterization of the monomethylarsonate reductase and dehydroascorbate RT reductase activities of Omega class glutathione transferase variants: RT implications for arsenic metabolism and the age-at-onset of Alzheimer's and RT Parkinson's diseases."; RL Pharmacogenet. Genomics 15:493-501(2005). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-239 ALONE AND IN COMPLEX WITH RP GLUTATHIONE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-34. RX PubMed=22522127; DOI=10.1016/j.jmb.2012.04.014; RA Zhou H., Brock J., Liu D., Board P.G., Oakley A.J.; RT "Structural insights into the dehydroascorbate reductase activity of human RT omega-class glutathione transferases."; RL J. Mol. Biol. 420:190-203(2012). CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity. CC Has high dehydroascorbate reductase activity and may contribute to the CC recycling of ascorbic acid. Participates in the biotransformation of CC inorganic arsenic and reduces monomethylarsonic acid (MMA). CC {ECO:0000269|PubMed:15970797}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glutathione + RX = a halide anion + an S-substituted CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:90779; EC=2.5.1.18; CC Evidence={ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide + CC L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1; CC Evidence={ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide CC + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2; CC Evidence={ECO:0000269|PubMed:15970797}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:15970797}; CC -!- INTERACTION: CC Q9H4Y5; P28676: GCA; NbExp=3; IntAct=EBI-10194609, EBI-947242; CC Q9H4Y5; Q9H4Y5: GSTO2; NbExp=8; IntAct=EBI-10194609, EBI-10194609; CC Q9H4Y5; P31273: HOXC8; NbExp=3; IntAct=EBI-10194609, EBI-1752118; CC Q9H4Y5; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10194609, EBI-6509505; CC Q9H4Y5; Q6JEL2: KLHL10; NbExp=3; IntAct=EBI-10194609, EBI-6426253; CC Q9H4Y5; Q9H6H2: MUM1; NbExp=3; IntAct=EBI-10194609, EBI-10307610; CC Q9H4Y5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10194609, EBI-741158; CC Q9H4Y5; Q99471: PFDN5; NbExp=3; IntAct=EBI-10194609, EBI-357275; CC Q9H4Y5; O15160: POLR1C; NbExp=3; IntAct=EBI-10194609, EBI-1055079; CC Q9H4Y5; Q92922: SMARCC1; NbExp=3; IntAct=EBI-10194609, EBI-355653; CC Q9H4Y5; P05549: TFAP2A; NbExp=4; IntAct=EBI-10194609, EBI-347351; CC Q9H4Y5; P05549-5: TFAP2A; NbExp=6; IntAct=EBI-10194609, EBI-12194905; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H4Y5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H4Y5-2; Sequence=VSP_042567; CC Name=3; CC IsoId=Q9H4Y5-3; Sequence=VSP_045267; CC -!- TISSUE SPECIFICITY: Expressed in a range of tissues, including the CC liver, kidney, skeletal muscle and prostate. Strongest expression in CC the testis. {ECO:0000269|PubMed:12618591}. CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family. CC {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; AY350731; AAR02452.1; -; mRNA. DR EMBL; AY209189; AAP47743.1; -; mRNA. DR EMBL; AK291886; BAF84575.1; -; mRNA. DR EMBL; AK296266; BAG58978.1; -; mRNA. DR EMBL; AL139341; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL162742; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49600.1; -; Genomic_DNA. DR EMBL; BC046194; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC056918; AAH56918.1; -; mRNA. DR EMBL; AY191318; AAO23573.1; -; mRNA. DR CCDS; CCDS53574.1; -. [Q9H4Y5-2] DR CCDS; CCDS53575.1; -. [Q9H4Y5-3] DR CCDS; CCDS7556.1; -. [Q9H4Y5-1] DR RefSeq; NP_001177942.1; NM_001191013.1. [Q9H4Y5-2] DR RefSeq; NP_001177943.1; NM_001191014.1. [Q9H4Y5-3] DR RefSeq; NP_001177944.1; NM_001191015.1. DR RefSeq; NP_899062.1; NM_183239.1. [Q9H4Y5-1] DR RefSeq; XP_011537572.1; XM_011539270.2. DR PDB; 3Q18; X-ray; 1.70 A; A/B=1-239. DR PDB; 3Q19; X-ray; 1.90 A; A/B=1-239. DR PDB; 3QAG; X-ray; 2.00 A; A=1-239. DR PDBsum; 3Q18; -. DR PDBsum; 3Q19; -. DR PDBsum; 3QAG; -. DR AlphaFoldDB; Q9H4Y5; -. DR SMR; Q9H4Y5; -. DR BioGRID; 125638; 27. DR IntAct; Q9H4Y5; 15. DR STRING; 9606.ENSP00000345023; -. DR ChEMBL; CHEMBL2161; -. DR DrugBank; DB00143; Glutathione. DR iPTMnet; Q9H4Y5; -. DR PhosphoSitePlus; Q9H4Y5; -. DR BioMuta; GSTO2; -. DR DMDM; 34922124; -. DR MassIVE; Q9H4Y5; -. DR PaxDb; 9606-ENSP00000345023; -. DR PeptideAtlas; Q9H4Y5; -. DR ProteomicsDB; 63249; -. DR ProteomicsDB; 80881; -. [Q9H4Y5-1] DR ProteomicsDB; 80882; -. [Q9H4Y5-2] DR Antibodypedia; 31611; 357 antibodies from 29 providers. DR DNASU; 119391; -. DR Ensembl; ENST00000338595.7; ENSP00000345023.1; ENSG00000065621.15. [Q9H4Y5-1] DR Ensembl; ENST00000369707.2; ENSP00000358721.1; ENSG00000065621.15. [Q9H4Y5-3] DR Ensembl; ENST00000450629.6; ENSP00000390986.2; ENSG00000065621.15. [Q9H4Y5-2] DR GeneID; 119391; -. DR KEGG; hsa:119391; -. DR MANE-Select; ENST00000338595.7; ENSP00000345023.1; NM_183239.2; NP_899062.1. DR UCSC; uc001kyb.4; human. [Q9H4Y5-1] DR AGR; HGNC:23064; -. DR CTD; 119391; -. DR DisGeNET; 119391; -. DR GeneCards; GSTO2; -. DR HGNC; HGNC:23064; GSTO2. DR HPA; ENSG00000065621; Tissue enhanced (testis). DR MIM; 612314; gene. DR neXtProt; NX_Q9H4Y5; -. DR OpenTargets; ENSG00000065621; -. DR PharmGKB; PA133787053; -. DR VEuPathDB; HostDB:ENSG00000065621; -. DR eggNOG; KOG0406; Eukaryota. DR GeneTree; ENSGT00940000162030; -. DR HOGENOM; CLU_011226_9_2_1; -. DR InParanoid; Q9H4Y5; -. DR OMA; PDADIHP; -. DR OrthoDB; 103277at2759; -. DR PhylomeDB; Q9H4Y5; -. DR TreeFam; TF105325; -. DR BRENDA; 1.8.5.1; 2681. DR BRENDA; 2.5.1.18; 2681. DR PathwayCommons; Q9H4Y5; -. DR Reactome; R-HSA-156590; Glutathione conjugation. DR Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism. DR SignaLink; Q9H4Y5; -. DR BioGRID-ORCS; 119391; 12 hits in 1154 CRISPR screens. DR ChiTaRS; GSTO2; human. DR GeneWiki; GSTO2; -. DR GenomeRNAi; 119391; -. DR Pharos; Q9H4Y5; Tbio. DR PRO; PR:Q9H4Y5; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9H4Y5; Protein. DR Bgee; ENSG00000065621; Expressed in body of pancreas and 149 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB. DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central. DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB. DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB. DR CDD; cd03184; GST_C_Omega; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR005442; GST_omega. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR43968; -; 1. DR PANTHER; PTHR43968:SF4; GLUTATHIONE S-TRANSFERASE OMEGA-2; 1. DR Pfam; PF13417; GST_N_3; 1. DR PRINTS; PR01625; GSTRNSFRASEO. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG00358; Main_(cytGST); 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. DR Genevisible; Q9H4Y5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Oxidoreductase; Reference proteome; KW Transferase. FT CHAIN 1..243 FT /note="Glutathione S-transferase omega-2" FT /id="PRO_0000185888" FT DOMAIN 22..101 FT /note="GST N-terminal" FT DOMAIN 106..231 FT /note="GST C-terminal" FT ACT_SITE 32 FT /note="Nucleophile" FT BINDING 59 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:22522127" FT BINDING 72 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:22522127" FT BINDING 85..86 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:22522127" FT VAR_SEQ 1..28 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045267" FT VAR_SEQ 123..156 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042567" FT VARIANT 130 FT /note="C -> Y (in dbSNP:rs45582439)" FT /id="VAR_049492" FT VARIANT 142 FT /note="N -> D (in dbSNP:rs156697)" FT /evidence="ECO:0000269|PubMed:12618591" FT /id="VAR_016812" FT MUTAGEN 34 FT /note="Y->A: Abolishes DHAR activity." FT /evidence="ECO:0000269|PubMed:22522127" FT CONFLICT 215 FT /note="A -> V (in Ref. 2; AAP47743)" FT /evidence="ECO:0000305" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 33..44 FT /evidence="ECO:0007829|PDB:3Q18" FT STRAND 49..54 FT /evidence="ECO:0007829|PDB:3Q18" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 61..65 FT /evidence="ECO:0007829|PDB:3Q18" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:3Q18" FT STRAND 82..85 FT /evidence="ECO:0007829|PDB:3QAG" FT HELIX 86..96 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 107..119 FT /evidence="ECO:0007829|PDB:3Q18" FT TURN 120..122 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 123..136 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 141..161 FT /evidence="ECO:0007829|PDB:3Q18" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 173..183 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 185..188 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 198..208 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 211..216 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 220..231 FT /evidence="ECO:0007829|PDB:3Q18" FT HELIX 235..238 FT /evidence="ECO:0007829|PDB:3Q18" SQ SEQUENCE 243 AA; 28254 MW; 45A959432BCF490A CRC64; MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE VVNINLRNKP EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR KLFPYDPYER ARQKMLLELF CKVPHLTKEC LVALRCGREC TNLKAALRQE FSNLEEILEY QNTTFFGGTC ISMIDYLLWP WFERLDVYGI LDCVSHTPAL RLWISAMKWD PTVCALLMDK SIFQGFLNLY FQNNPNAFDF GLC //