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}.
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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 Genevisible; Q9H4Y5; HS.
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.
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
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