GenomeNet

Database: UniProt/SWISS-PROT
Entry: GSTO2_HUMAN
LinkDB: GSTO2_HUMAN
Original site: GSTO2_HUMAN 
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   31-JUL-2019, entry version 160.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
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 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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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.,
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 (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
RT   project: 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
RT   genes 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
RT   dehydroascorbate reductase activities of Omega class glutathione
RT   transferase variants: implications for arsenic metabolism and the age-
RT   at-onset of Alzheimer's and 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
RP   WITH 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
RT   human omega-class glutathione transferases.";
RL   J. Mol. Biol. 420:190-203(2012).
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase
CC       activity. Has high dehydroascorbate reductase activity and may
CC       contribute to the recycling of ascorbic acid. Participates in the
CC       biotransformation of inorganic arsenic and reduces
CC       monomethylarsonic acid (MMA). {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,
CC         ECO:0000269|PubMed:22522127};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione
CC         disulfide + L-ascorbate; Xref=Rhea:RHEA:24424,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000269|PubMed:15970797,
CC         ECO:0000269|PubMed:22522127};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione
CC         disulfide + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826,
CC         ChEBI:CHEBI:33409, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297;
CC         EC=1.20.4.2; Evidence={ECO:0000269|PubMed:15970797};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:15970797};
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-10194609, EBI-10194609;
CC       Q9H6H2:MUM1; NbExp=3; IntAct=EBI-10194609, EBI-10307610;
CC       P05549:TFAP2A; NbExp=3; IntAct=EBI-10194609, EBI-347351;
CC       P05549-5:TFAP2A; NbExp=5; 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         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q9H4Y5-3; Sequence=VSP_045267;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in a range of tissues, including the
CC       liver, kidney, skeletal muscle and prostate. Strongest expression
CC       in the testis. {ECO:0000269|PubMed:12618591}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
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. [Q9H4Y5-1]
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   SMR; Q9H4Y5; -.
DR   BioGrid; 125638; 16.
DR   IntAct; Q9H4Y5; 11.
DR   STRING; 9606.ENSP00000345023; -.
DR   ChEMBL; CHEMBL2161; -.
DR   DrugBank; DB00143; Glutathione.
DR   iPTMnet; Q9H4Y5; -.
DR   PhosphoSitePlus; Q9H4Y5; -.
DR   BioMuta; GSTO2; -.
DR   DMDM; 34922124; -.
DR   jPOST; Q9H4Y5; -.
DR   PaxDb; Q9H4Y5; -.
DR   PeptideAtlas; Q9H4Y5; -.
DR   PRIDE; Q9H4Y5; -.
DR   ProteomicsDB; 63249; -.
DR   ProteomicsDB; 80881; -. [Q9H4Y5-1]
DR   ProteomicsDB; 80882; -. [Q9H4Y5-2]
DR   DNASU; 119391; -.
DR   Ensembl; ENST00000338595; ENSP00000345023; ENSG00000065621. [Q9H4Y5-1]
DR   Ensembl; ENST00000369707; ENSP00000358721; ENSG00000065621. [Q9H4Y5-3]
DR   Ensembl; ENST00000450629; ENSP00000390986; ENSG00000065621. [Q9H4Y5-2]
DR   GeneID; 119391; -.
DR   KEGG; hsa:119391; -.
DR   UCSC; uc001kyb.4; human. [Q9H4Y5-1]
DR   CTD; 119391; -.
DR   DisGeNET; 119391; -.
DR   GeneCards; GSTO2; -.
DR   HGNC; HGNC:23064; GSTO2.
DR   HPA; HPA048141; -.
DR   MIM; 612314; gene.
DR   neXtProt; NX_Q9H4Y5; -.
DR   OpenTargets; ENSG00000065621; -.
DR   PharmGKB; PA133787053; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   eggNOG; ENOG410XSIX; LUCA.
DR   GeneTree; ENSGT00940000162030; -.
DR   HOGENOM; HOG000006560; -.
DR   InParanoid; Q9H4Y5; -.
DR   KO; K00799; -.
DR   OMA; IDYLFWP; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q9H4Y5; -.
DR   TreeFam; TF105325; -.
DR   BRENDA; 1.8.5.1; 2681.
DR   BRENDA; 2.5.1.18; 2681.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR   ChiTaRS; GSTO2; human.
DR   GeneWiki; GSTO2; -.
DR   GenomeRNAi; 119391; -.
DR   PRO; PR:Q9H4Y5; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000065621; Expressed in 157 organ(s), highest expression level in right testis.
DR   Genevisible; Q9H4Y5; HS.
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; IEA:UniProtKB-EC.
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:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
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   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Oxidoreductase;
KW   Polymorphism; Reference proteome; Transferase.
FT   CHAIN         1    243       Glutathione S-transferase omega-2.
FT                                /FTId=PRO_0000185888.
FT   DOMAIN       22    101       GST N-terminal.
FT   DOMAIN      106    231       GST C-terminal.
FT   REGION       85     86       Glutathione binding.
FT                                {ECO:0000269|PubMed:22522127}.
FT   ACT_SITE     32     32       Nucleophile.
FT   BINDING      59     59       Glutathione.
FT                                {ECO:0000269|PubMed:22522127}.
FT   BINDING      72     72       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000269|PubMed:22522127}.
FT   VAR_SEQ       1     28       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_045267.
FT   VAR_SEQ     123    156       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_042567.
FT   VARIANT     130    130       C -> Y (in dbSNP:rs45582439).
FT                                /FTId=VAR_049492.
FT   VARIANT     142    142       N -> D (in dbSNP:rs156697).
FT                                {ECO:0000269|PubMed:12618591}.
FT                                /FTId=VAR_016812.
FT   MUTAGEN      34     34       Y->A: Abolishes DHAR activity.
FT                                {ECO:0000269|PubMed:22522127}.
FT   CONFLICT    215    215       A -> V (in Ref. 2; AAP47743).
FT                                {ECO:0000305}.
FT   STRAND       24     28       {ECO:0000244|PDB:3Q18}.
FT   HELIX        33     44       {ECO:0000244|PDB:3Q18}.
FT   STRAND       49     54       {ECO:0000244|PDB:3Q18}.
FT   STRAND       56     58       {ECO:0000244|PDB:3Q18}.
FT   HELIX        61     65       {ECO:0000244|PDB:3Q18}.
FT   STRAND       74     76       {ECO:0000244|PDB:3Q18}.
FT   STRAND       82     85       {ECO:0000244|PDB:3QAG}.
FT   HELIX        86     96       {ECO:0000244|PDB:3Q18}.
FT   HELIX       107    119       {ECO:0000244|PDB:3Q18}.
FT   TURN        120    122       {ECO:0000244|PDB:3Q18}.
FT   HELIX       123    136       {ECO:0000244|PDB:3Q18}.
FT   HELIX       141    161       {ECO:0000244|PDB:3Q18}.
FT   STRAND      168    170       {ECO:0000244|PDB:3Q18}.
FT   HELIX       173    183       {ECO:0000244|PDB:3Q18}.
FT   HELIX       185    188       {ECO:0000244|PDB:3Q18}.
FT   HELIX       191    194       {ECO:0000244|PDB:3Q18}.
FT   HELIX       198    208       {ECO:0000244|PDB:3Q18}.
FT   HELIX       211    216       {ECO:0000244|PDB:3Q18}.
FT   HELIX       220    231       {ECO:0000244|PDB:3Q18}.
FT   HELIX       235    238       {ECO:0000244|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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