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 27-MAR-2024, entry version 222. 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 club 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"; 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; 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; 38. DR IntAct; P30711; 13. DR ChEMBL; CHEMBL2141; -. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00958; Carboplatin. DR DrugBank; DB00291; Chlorambucil. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB03619; Deoxycholic acid. 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 PeptideAtlas; P30711; -. DR ProteomicsDB; 54733; -. [P30711-1] DR ProteomicsDB; 66376; -. DR Pumba; P30711; -. 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 MANE-Select; ENST00000612885.4; ENSP00000481741.1; NM_000853.4; NP_000844.2. DR UCSC; uc002zze.4; human. [P30711-1] DR AGR; HGNC:4641; -. 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; 1199296at2759; -. 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 665 CRISPR screens. DR EvolutionaryTrace; P30711; -. DR GeneWiki; GSTT1; -. DR GenomeRNAi; 2952; -. DR Pharos; P30711; Tbio. DR PRO; PR:P30711; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; P30711; Protein. DR Bgee; ENSG00000277656; Expressed in vena cava and 148 other cell types or 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 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; IPR004046; GST_C. DR InterPro; IPR040077; GST_C_Theta. DR InterPro; IPR040075; GST_N_Theta. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR43917; -; 1. DR PANTHER; PTHR43917:SF9; GLUTATHIONE S-TRANSFERASE THETA-1; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF13417; GST_N_3; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01153; Main.4:_Theta-like; 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; 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 //