ID   GSTA3_HUMAN             Reviewed;         222 AA.
AC   Q16772; O43468; Q068V6; Q8WWA8; Q9H415;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 3.
DT   24-JAN-2024, entry version 197.
DE   RecName: Full=Glutathione S-transferase A3 {ECO:0000305};
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha member 3;
DE   AltName: Full=Glutathione S-transferase A3-3;
GN   Name=GSTA3 {ECO:0000312|HGNC:HGNC:4628};
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 [GENOMIC DNA].
RX   PubMed=8307579; DOI=10.1016/s0888-7543(05)80373-8;
RA   Suzuki T., Johnston P.N., Board P.G.;
RT   "Structure and organization of the human alpha class glutathione S-
RT   transferase genes and related pseudogenes.";
RL   Genomics 18:680-686(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, CATALYTIC ACTIVITY, FUNCTION,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11418619; DOI=10.1074/jbc.m104539200;
RA   Johansson A.-S., Mannervik B.;
RT   "Human glutathione transferase A3-3, a highly efficient catalyst of double-
RT   bond isomerization in the biosynthetic pathway of steroid hormones.";
RL   J. Biol. Chem. 276:33061-33065(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-36; LEU-71; ASP-73;
RP   GLN-113 AND THR-208.
RG   NIEHS SNPs program;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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 30-222, AND VARIANT LEU-71.
RX   PubMed=9480897; DOI=10.1042/bj3300827;
RA   Board P.G.;
RT   "Identification of cDNAs encoding two human alpha class glutathione
RT   transferases (GSTA3 and GSTA4) and the heterologous expression of
RT   GSTA4-4.";
RL   Biochem. J. 330:827-831(1998).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX   PubMed=15595823; DOI=10.1021/bi048757g;
RA   Gu Y., Guo J., Pal A., Pan S.S., Zimniak P., Singh S.V., Ji X.;
RT   "Crystal structure of human glutathione S-transferase A3-3 and mechanistic
RT   implications for its high steroid isomerase activity.";
RL   Biochemistry 43:15673-15679(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
RP   DELTA5-ANDROSTENE-3-17-DIONE, FUNCTION, AND SUBUNIT.
RX   PubMed=20083122; DOI=10.1016/j.jmb.2010.01.023;
RA   Tars K., Olin B., Mannervik B.;
RT   "Structural basis for featuring of steroid isomerase activity in alpha
RT   class glutathione transferases.";
RL   J. Mol. Biol. 397:332-340(2010).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. Catalyzes
CC       isomerization reactions that contribute to the biosynthesis of steroid
CC       hormones. Efficiently catalyze obligatory double-bond isomerizations of
CC       delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione,
CC       precursors to testosterone and progesterone, respectively. Has
CC       substantial activity toward aflatoxin B1-8,9-epoxide (By similarity).
CC       {ECO:0000250|UniProtKB:P30115, ECO:0000269|PubMed:11418619,
CC       ECO:0000269|PubMed:15595823, ECO:0000269|PubMed:20083122}.
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:0000305|PubMed:11418619};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000305|PubMed:11418619};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC         Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC         Evidence={ECO:0000269|PubMed:11418619};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC         Evidence={ECO:0000305|PubMed:11418619};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pregn-5-ene-3,20-dione = progesterone; Xref=Rhea:RHEA:43928,
CC         ChEBI:CHEBI:17026, ChEBI:CHEBI:63837;
CC         Evidence={ECO:0000269|PubMed:11418619};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43929;
CC         Evidence={ECO:0000305|PubMed:11418619};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=23 uM for androst-5-ene-3,17-dione {ECO:0000269|PubMed:15595823};
CC         KM=24 uM for androst-5-ene-3,17-dione (at pH 8.0 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:11418619};
CC         KM=24 uM for androst-5-ene-3,17-dione (at pH 7.4 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:11418619};
CC         KM=17 uM for pregn-5-ene-3,20-dione (at pH 8.0 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:11418619};
CC         KM=17 uM for pregn-5-ene-3,20-dione (at pH 7.4 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:11418619};
CC         Vmax=99 umol/min/mg enzyme for delta(5)-androstene-3,17-dione
CC         isomerization {ECO:0000269|PubMed:15595823};
CC         Note=kcats are 102 sec(-1) and 27 sec(-1) for
CC         androst-5-ene-3,17-dione and pregn-5-ene-3,20-dione as substrates,
CC         respectively (at pH 8.0 and 30 degrees Celsius).
CC         {ECO:0000269|PubMed:11418619};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15595823,
CC       ECO:0000269|PubMed:20083122}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA74634.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAD04712.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/gsta3/";
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DR   EMBL; L13275; AAA74634.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L13270; AAA74634.1; JOINED; Genomic_DNA.
DR   EMBL; L13271; AAA74634.1; JOINED; Genomic_DNA.
DR   EMBL; L13272; AAA74634.1; JOINED; Genomic_DNA.
DR   EMBL; L13273; AAA74634.1; JOINED; Genomic_DNA.
DR   EMBL; L13274; AAA74634.1; JOINED; Genomic_DNA.
DR   EMBL; AF508266; AAM33360.1; -; mRNA.
DR   EMBL; DQ993361; ABI75350.1; -; Genomic_DNA.
DR   EMBL; AL121969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX04391.1; -; Genomic_DNA.
DR   EMBL; BC020619; AAH20619.1; -; mRNA.
DR   EMBL; AF020919; AAD04712.1; ALT_INIT; mRNA.
DR   CCDS; CCDS4947.1; -.
DR   PIR; A49365; A49365.
DR   RefSeq; NP_000838.3; NM_000847.4.
DR   PDB; 1TDI; X-ray; 2.40 A; A/B=1-222.
DR   PDB; 2VCV; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-222.
DR   PDBsum; 1TDI; -.
DR   PDBsum; 2VCV; -.
DR   AlphaFoldDB; Q16772; -.
DR   SMR; Q16772; -.
DR   BioGRID; 109195; 4.
DR   IntAct; Q16772; 1.
DR   STRING; 9606.ENSP00000211122; -.
DR   ChEMBL; CHEMBL4866; -.
DR   DrugBank; DB04521; 4-S-Glutathionyl-5-pentyl-tetrahydro-furan-2-ol.
DR   DrugBank; DB00143; Glutathione.
DR   SwissLipids; SLP:000001612; -.
DR   iPTMnet; Q16772; -.
DR   PhosphoSitePlus; Q16772; -.
DR   BioMuta; GSTA3; -.
DR   DMDM; 21264437; -.
DR   jPOST; Q16772; -.
DR   MassIVE; Q16772; -.
DR   MaxQB; Q16772; -.
DR   PaxDb; 9606-ENSP00000211122; -.
DR   PeptideAtlas; Q16772; -.
DR   ProteomicsDB; 61058; -.
DR   Antibodypedia; 30950; 336 antibodies from 29 providers.
DR   DNASU; 2940; -.
DR   Ensembl; ENST00000211122.4; ENSP00000211122.3; ENSG00000174156.15.
DR   GeneID; 2940; -.
DR   KEGG; hsa:2940; -.
DR   MANE-Select; ENST00000211122.4; ENSP00000211122.3; NM_000847.5; NP_000838.3.
DR   UCSC; uc003pbb.4; human.
DR   AGR; HGNC:4628; -.
DR   CTD; 2940; -.
DR   DisGeNET; 2940; -.
DR   GeneCards; GSTA3; -.
DR   HGNC; HGNC:4628; GSTA3.
DR   HPA; ENSG00000174156; Group enriched (adrenal gland, fallopian tube, placenta, skin).
DR   MIM; 605449; gene.
DR   neXtProt; NX_Q16772; -.
DR   OpenTargets; ENSG00000174156; -.
DR   PharmGKB; PA29018; -.
DR   VEuPathDB; HostDB:ENSG00000174156; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000164319; -.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   InParanoid; Q16772; -.
DR   OMA; FTEMIMN; -.
DR   OrthoDB; 3412208at2759; -.
DR   PhylomeDB; Q16772; -.
DR   TreeFam; TF105321; -.
DR   BRENDA; 2.5.1.18; 2681.
DR   BRENDA; 5.3.3.1; 2681.
DR   PathwayCommons; Q16772; -.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   Reactome; R-HSA-9818027; NFE2L2 regulating anti-oxidant/detoxification enzymes.
DR   SABIO-RK; Q16772; -.
DR   SignaLink; Q16772; -.
DR   BioGRID-ORCS; 2940; 10 hits in 1084 CRISPR screens.
DR   EvolutionaryTrace; Q16772; -.
DR   GeneWiki; GSTA3; -.
DR   GenomeRNAi; 2940; -.
DR   Pharos; Q16772; Tbio.
DR   PRO; PR:Q16772; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q16772; Protein.
DR   Bgee; ENSG00000174156; Expressed in right uterine tube and 103 other cell types or tissues.
DR   ExpressionAtlas; Q16772; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd03208; GST_C_Alpha; 1.
DR   CDD; cd03077; GST_N_Alpha; 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; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF257; GLUTATHIONE S-TRANSFERASE A3; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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; Q16772; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Lipid metabolism; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   CHAIN           2..222
FT                   /note="Glutathione S-transferase A3"
FT                   /id="PRO_0000185785"
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..207
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:15595823,
FT                   ECO:0000269|PubMed:20083122"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:15595823,
FT                   ECO:0000269|PubMed:20083122"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:15595823,
FT                   ECO:0000269|PubMed:20083122"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:15595823,
FT                   ECO:0000269|PubMed:20083122"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   MOD_RES         4
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   VARIANT         36
FT                   /note="G -> E (in dbSNP:rs45504096)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_062276"
FT   VARIANT         71
FT                   /note="I -> L (in dbSNP:rs1052661)"
FT                   /evidence="ECO:0000269|PubMed:9480897, ECO:0000269|Ref.3"
FT                   /id="VAR_049484"
FT   VARIANT         73
FT                   /note="N -> D (in dbSNP:rs41273858)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_049485"
FT   VARIANT         113
FT                   /note="R -> Q (in dbSNP:rs45602042)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_062277"
FT   VARIANT         208
FT                   /note="A -> T (in dbSNP:rs45620832)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_062278"
FT   CONFLICT        63
FT                   /note="M -> I (in Ref. 6; AAH20619)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113..114
FT                   /note="RP -> PA (in Ref. 1; AAA74634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="T -> I (in Ref. 1; AAA74634)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           17..25
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           86..108
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           114..130
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           132..143
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           155..170
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   TURN            172..177
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           179..190
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           192..197
FT                   /evidence="ECO:0007829|PDB:2VCV"
FT   HELIX           210..220
FT                   /evidence="ECO:0007829|PDB:2VCV"
SQ   SEQUENCE   222 AA;  25302 MW;  904AA17519B5343C CRC64;
     MAGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL MFQQVPMVEI
     DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA DLNEMILLLP LCRPEEKDAK
     IALIKEKTKS RYFPAFEKVL QSHGQDYLVG NKLSRADISL VELLYYVEEL DSSLISNFPL
     LKALKTRISN LPTVKKFLQP GSPRKPPADA KALEEARKIF RF
//