GSTT1_HUMAN
ID GSTT1_HUMAN Reviewed; 240 AA.
AC P30711; O00226; Q5TZY2; Q6IC69; Q969K8; Q96IY3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Glutathione S-transferase theta-1;
DE EC=2.5.1.18 {ECO:0000269|PubMed:16298388, ECO:0000269|PubMed:20097269};
DE AltName: Full=GST class-theta-1;
DE AltName: Full=Glutathione transferase T1-1;
GN Name=GSTT1;
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=8198545; DOI=10.1042/bj3000271;
RA Pemble S., Schroeder K.R., Spencer S.R., Meyer D.J., Hallier E., Bolt H.M.,
RA Ketterer B., Taylor J.B.;
RT "Human glutathione S-transferase theta (GSTT1): cDNA cloning and the
RT characterization of a genetic polymorphism.";
RL Biochem. J. 300:271-276(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RX PubMed=9434735; DOI=10.1006/abbi.1997.0357;
RA Jemth P., Mannervik B.;
RT "Kinetic characterization of recombinant human glutathione transferase T1-
RT 1, a polymorphic detoxication enzyme.";
RL Arch. Biochem. Biophys. 348:247-254(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10975610; DOI=10.1097/00008571-200008000-00009;
RA Sprenger R., Schlagenhaufer R., Kerb R., Bruhn C., Brockmoeller J.,
RA Roots I., Brinkmann U.;
RT "Characterization of the glutathione S-transferase GSTT1 deletion:
RT discrimination of all genotypes by polymerase chain reaction indicates a
RT trimodular genotype-phenotype correlation.";
RL Pharmacogenetics 10:557-565(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Thymus;
RA Iida A., Kondo K., Kitamura Y., Mishima C., Osawa S., Kitamoto T.,
RA Harigae C., Nakamura Y.;
RT "Complete genomic structure of human glutathione S-transferase TT1.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-169.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [9]
RP PROTEIN SEQUENCE OF 2-47.
RC TISSUE=Liver;
RX PubMed=1848757; DOI=10.1042/bj2740409;
RA Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B.;
RT "Theta, a new class of glutathione transferases purified from rat and
RT man.";
RL Biochem. J. 274:409-414(1991).
RN [10]
RP TISSUE SPECIFICITY.
RC TISSUE=Liver, and Lung;
RX PubMed=8761485; DOI=10.1042/bj3180297;
RA Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T.;
RT "The distribution of theta-class glutathione S-transferases in the liver
RT and lung of mouse, rat and human.";
RL Biochem. J. 318:297-303(1996).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20097269; DOI=10.1016/j.bbagen.2010.01.003;
RA Shokeer A., Mannervik B.;
RT "Residue 234 is a master switch of the alternative-substrate activity
RT profile of human and rodent theta class glutathione transferase T1-1.";
RL Biochim. Biophys. Acta 1800:466-473(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-234 IN
RP COMPLEX WITH HEXYLGLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF HIS-176 AND TRP-234.
RX PubMed=16298388; DOI=10.1016/j.jmb.2005.10.049;
RA Tars K., Larsson A.K., Shokeer A., Olin B., Mannervik B., Kleywegt G.J.;
RT "Structural basis of the suppressed catalytic activity of wild-type human
RT glutathione transferase T1-1 compared to its W234R mutant.";
RL J. Mol. Biol. 355:96-105(2006).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Acts on 1,2-epoxy-
CC 3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl
CC chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase
CC activity with cumene hydroperoxide. {ECO:0000269|PubMed:16298388,
CC ECO:0000269|PubMed:20097269}.
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:16298388, ECO:0000269|PubMed:20097269};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16298388}.
CC -!- INTERACTION:
CC P30711; P35609: ACTN2; NbExp=3; IntAct=EBI-8770084, EBI-77797;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30711-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30711-2; Sequence=VSP_056474;
CC -!- TISSUE SPECIFICITY: Found in erythrocyte. Expressed at low levels in
CC liver. In lung, expressed at low levels in Clara cells and ciliated
CC cells at the alveolar/bronchiolar junction. Absent from epithelial
CC cells of larger bronchioles. {ECO:0000269|PubMed:8761485}.
CC -!- POLYMORPHISM: The GSTT1 gene is absent from 38% of the population. The
CC presence or absence of the GSTT1 gene is coincident with the conjugator
CC (GSST1+) and non-conjugator (GSTT1-) phenotypes respectively. The
CC GSTT1+ phenotype can catalyze the glutathione conjugation of
CC dichloromethane. {ECO:0000269|PubMed:8198545}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=C&genename=GSTT1";
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DR EMBL; X79389; CAA55935.1; -; mRNA.
DR EMBL; AF435971; AAL31549.1; -; mRNA.
DR EMBL; AF240786; AAG02374.1; -; Genomic_DNA.
DR EMBL; AB057594; BAB39498.1; -; Genomic_DNA.
DR EMBL; CR456499; CAG30385.1; -; mRNA.
DR EMBL; BT019951; AAV38754.1; -; mRNA.
DR EMBL; AP000351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z84718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007065; AAH07065.1; -; mRNA.
DR PIR; S44358; S44358.
DR RefSeq; NP_000844.2; NM_000853.3. [P30711-1]
DR RefSeq; NP_001280736.1; NM_001293807.1.
DR RefSeq; NP_001280737.1; NM_001293808.1. [P30711-2]
DR RefSeq; NP_001280738.1; NM_001293809.1. [P30711-2]
DR RefSeq; NP_001280739.1; NM_001293810.1. [P30711-2]
DR RefSeq; NP_001280740.1; NM_001293811.1. [P30711-2]
DR RefSeq; NP_001280741.1; NM_001293812.1. [P30711-2]
DR PDB; 2C3N; X-ray; 1.50 A; A/B/C/D=2-240.
DR PDB; 2C3Q; X-ray; 1.85 A; A/B/C/D=2-240.
DR PDB; 2C3T; X-ray; 2.40 A; A/B/C/D=2-240.
DR PDBsum; 2C3N; -.
DR PDBsum; 2C3Q; -.
DR PDBsum; 2C3T; -.
DR AlphaFoldDB; P30711; -.
DR SMR; P30711; -.
DR BioGRID; 109207; 35.
DR IntAct; P30711; 13.
DR ChEMBL; CHEMBL2141; -.
DR DrugBank; DB00958; Carboplatin.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB00773; Etoposide.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR DrugBank; DB00526; Oxaliplatin.
DR DrugBank; DB09221; Polaprezinc.
DR GlyGen; P30711; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30711; -.
DR PhosphoSitePlus; P30711; -.
DR BioMuta; GSTT1; -.
DR DMDM; 21264427; -.
DR EPD; P30711; -.
DR jPOST; P30711; -.
DR MassIVE; P30711; -.
DR MaxQB; P30711; -.
DR PaxDb; P30711; -.
DR PeptideAtlas; P30711; -.
DR PRIDE; P30711; -.
DR ProteomicsDB; 54733; -. [P30711-1]
DR ProteomicsDB; 66376; -.
DR TopDownProteomics; P30711-1; -. [P30711-1]
DR DNASU; 2952; -.
DR Ensembl; ENST00000612885.3; ENSP00000481741.1; ENSG00000277656.3. [P30711-1]
DR GeneID; 2952; -.
DR KEGG; hsa:2952; -.
DR UCSC; uc002zze.4; human. [P30711-1]
DR CTD; 2952; -.
DR DisGeNET; 2952; -.
DR GeneCards; GSTT1; -.
DR HGNC; HGNC:4641; GSTT1.
DR MIM; 600436; gene.
DR neXtProt; NX_P30711; -.
DR OpenTargets; ENSG00000277656; -.
DR PharmGKB; PA183; -.
DR InParanoid; P30711; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; P30711; -.
DR TreeFam; TF325759; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; P30711; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SABIO-RK; P30711; -.
DR SignaLink; P30711; -.
DR BioGRID-ORCS; 2952; 10 hits in 630 CRISPR screens.
DR EvolutionaryTrace; P30711; -.
DR GeneWiki; GSTT1; -.
DR GenomeRNAi; 2952; -.
DR Pharos; P30711; Tbio.
DR PRO; PR:P30711; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P30711; protein.
DR Bgee; ENSG00000277656; Expressed in vena cava and 148 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR CDD; cd03183; GST_C_Theta; 1.
DR CDD; cd03050; GST_N_Theta; 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; IPR004046; GST_C.
DR InterPro; IPR040077; GST_C_Theta.
DR InterPro; IPR040075; GST_N_Theta.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
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; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1848757"
FT CHAIN 2..240
FT /note="Glutathione S-transferase theta-1"
FT /id="PRO_0000185938"
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT DOMAIN 88..220
FT /note="GST C-terminal"
FT BINDING 40
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:16298388"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:16298388"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:16298388"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15461802"
FT /id="VSP_056474"
FT VARIANT 21
FT /note="A -> T (in dbSNP:rs1601976480)"
FT /id="VAR_014501"
FT VARIANT 141
FT /note="D -> N (in dbSNP:rs1601989145)"
FT /id="VAR_014502"
FT VARIANT 169
FT /note="V -> I (in dbSNP:rs2266637)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_014503"
FT VARIANT 173
FT /note="E -> K (in dbSNP:rs1601989046)"
FT /id="VAR_014504"
FT MUTAGEN 176
FT /note="H->Q: Increases activity towards alkylhalogenides,
FT but not hydroperoxides."
FT /evidence="ECO:0000269|PubMed:16298388"
FT MUTAGEN 234
FT /note="W->R: Facilitates binding of substrates and
FT increases catalytic activity."
FT /evidence="ECO:0000269|PubMed:16298388"
FT CONFLICT 43..44
FT /note="DA -> SD (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="F -> C (in Ref. 8; AAH07065)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="E -> G (in Ref. 1; CAA55935)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:2C3N"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:2C3N"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2C3N"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 130..150
FT /evidence="ECO:0007829|PDB:2C3N"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:2C3N"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2C3N"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:2C3N"
SQ SEQUENCE 240 AA; 27335 MW; BD19F2BFDEF9F619 CRC64;
MGLELYLDLL SQPCRAVYIF AKKNDIPFEL RIVDLIKGQH LSDAFAQVNP LKKVPALKDG
DFTLTESVAI LLYLTRKYKV PDYWYPQDLQ ARARVDEYLA WQHTTLRRSC LRALWHKVMF
PVFLGEPVSP QTLAATLAEL DVTLQLLEDK FLQNKAFLTG PHISLADLVA ITELMHPVGA
GCQVFEGRPK LATWRQRVEA AVGEDLFQEA HEVILKAKDF PPADPTIKQK LMPWVLAMIR
