ID THTPA_HUMAN Reviewed; 230 AA. AC Q9BU02; D3DS50; G3V4J3; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 181. DE RecName: Full=Thiamine-triphosphatase; DE Short=ThTPase; DE EC=3.6.1.28; GN Name=THTPA; 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), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=11827967; DOI=10.1074/jbc.m111241200; RA Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B., RA De Pauw E., Wins P., Grisar T., Bettendorff L.; RT "Molecular characterization of a specific thiamine triphosphatase widely RT expressed in mammalian tissues."; RL J. Biol. Chem. 277:13771-13777(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Trachea; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Placenta; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH TRIPHOSPHATE, RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBUNIT, AND MUTAGENESIS OF LYS-11; ASP-37; TYR-39; TRP-53; LYS-65; TYR-79; RP GLU-81; ASP-147 AND LYS-193. RX PubMed=23707715; DOI=10.1016/j.bbagen.2013.05.014; RA Delvaux D., Kerff F., Murty M.R., Lakaye B., Czerniecki J., Kohn G., RA Wins P., Herman R., Gabelica V., Heuze F., Tordoir X., Maree R., RA Matagne A., Charlier P., De Pauw E., Bettendorff L.; RT "Structural determinants of specificity and catalytic mechanism in RT mammalian 25-kDa thiamine triphosphatase."; RL Biochim. Biophys. Acta 1830:4513-4523(2013). CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP). CC {ECO:0000269|PubMed:11827967, ECO:0000269|PubMed:23707715}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + thiamine triphosphate = H(+) + phosphate + thiamine CC diphosphate; Xref=Rhea:RHEA:11744, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58937, CC ChEBI:CHEBI:58938; EC=3.6.1.28; CC Evidence={ECO:0000269|PubMed:23707715}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:23707715}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:23707715}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8 uM for thiamine triphosphate {ECO:0000269|PubMed:23707715}; CC Vmax=59 umol/min/mg enzyme {ECO:0000269|PubMed:23707715}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23707715}. CC -!- INTERACTION: CC Q9BU02; O43711: TLX3; NbExp=3; IntAct=EBI-2820864, EBI-3939165; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11827967}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BU02-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BU02-2; Sequence=VSP_047213, VSP_047214; CC -!- TISSUE SPECIFICITY: Widely expressed but at a low level. CC {ECO:0000269|PubMed:11827967}. CC -!- SIMILARITY: Belongs to the ThTPase family. {ECO:0000305}. 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; AF432862; AAM22403.1; -; mRNA. DR EMBL; AK057691; BAB71546.1; -; mRNA. DR EMBL; BX161435; CAD61907.1; -; mRNA. DR EMBL; BX378775; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL135999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471078; EAW66140.1; -; Genomic_DNA. DR EMBL; CH471078; EAW66141.1; -; Genomic_DNA. DR EMBL; BC002984; AAH02984.1; -; mRNA. DR CCDS; CCDS32053.1; -. [Q9BU02-1] DR CCDS; CCDS58307.1; -. [Q9BU02-2] DR RefSeq; NP_001119811.1; NM_001126339.3. [Q9BU02-1] DR RefSeq; NP_001242991.1; NM_001256062.2. [Q9BU02-2] DR RefSeq; NP_001243250.1; NM_001256321.2. [Q9BU02-2] DR RefSeq; NP_001243251.1; NM_001256322.2. DR RefSeq; NP_001243252.1; NM_001256323.2. DR RefSeq; NP_077304.1; NM_024328.5. [Q9BU02-1] DR PDB; 3BHD; X-ray; 1.50 A; A/B=1-215. DR PDB; 3TVL; X-ray; 2.30 A; A/B=1-230. DR PDBsum; 3BHD; -. DR PDBsum; 3TVL; -. DR AlphaFoldDB; Q9BU02; -. DR SMR; Q9BU02; -. DR BioGRID; 122595; 78. DR IntAct; Q9BU02; 8. DR STRING; 9606.ENSP00000288014; -. DR DrugBank; DB00152; Thiamine. DR DrugCentral; Q9BU02; -. DR iPTMnet; Q9BU02; -. DR MetOSite; Q9BU02; -. DR PhosphoSitePlus; Q9BU02; -. DR BioMuta; THTPA; -. DR DMDM; 37538018; -. DR EPD; Q9BU02; -. DR jPOST; Q9BU02; -. DR MassIVE; Q9BU02; -. DR MaxQB; Q9BU02; -. DR PaxDb; 9606-ENSP00000288014; -. DR PeptideAtlas; Q9BU02; -. DR ProteomicsDB; 33249; -. DR ProteomicsDB; 79039; -. [Q9BU02-1] DR Pumba; Q9BU02; -. DR Antibodypedia; 55506; 254 antibodies from 23 providers. DR DNASU; 79178; -. DR Ensembl; ENST00000288014.7; ENSP00000288014.6; ENSG00000259431.6. [Q9BU02-1] DR Ensembl; ENST00000404535.3; ENSP00000384580.3; ENSG00000259431.6. [Q9BU02-1] DR Ensembl; ENST00000554789.1; ENSP00000450459.1; ENSG00000259431.6. [Q9BU02-2] DR Ensembl; ENST00000556015.5; ENSP00000451835.1; ENSG00000259431.6. [Q9BU02-2] DR GeneID; 79178; -. DR KEGG; hsa:79178; -. DR MANE-Select; ENST00000288014.7; ENSP00000288014.6; NM_024328.6; NP_077304.1. DR UCSC; uc001wkg.7; human. [Q9BU02-1] DR AGR; HGNC:18987; -. DR CTD; 79178; -. DR DisGeNET; 79178; -. DR GeneCards; THTPA; -. DR HGNC; HGNC:18987; THTPA. DR HPA; ENSG00000259431; Low tissue specificity. DR MalaCards; THTPA; -. DR MIM; 611612; gene. DR neXtProt; NX_Q9BU02; -. DR OpenTargets; ENSG00000259431; -. DR PharmGKB; PA38774; -. DR VEuPathDB; HostDB:ENSG00000259431; -. DR eggNOG; ENOG502S5G9; Eukaryota. DR GeneTree; ENSGT00390000005996; -. DR HOGENOM; CLU_105907_0_0_1; -. DR InParanoid; Q9BU02; -. DR OMA; HWLRHRE; -. DR PhylomeDB; Q9BU02; -. DR TreeFam; TF333398; -. DR BRENDA; 3.6.1.28; 2681. DR PathwayCommons; Q9BU02; -. DR Reactome; R-HSA-196819; Vitamin B1 (thiamin) metabolism. DR SignaLink; Q9BU02; -. DR BioGRID-ORCS; 79178; 12 hits in 1160 CRISPR screens. DR ChiTaRS; THTPA; human. DR EvolutionaryTrace; Q9BU02; -. DR GenomeRNAi; 79178; -. DR Pharos; Q9BU02; Tbio. DR PRO; PR:Q9BU02; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9BU02; Protein. DR Bgee; ENSG00000259431; Expressed in prefrontal cortex and 99 other cell types or tissues. DR ExpressionAtlas; Q9BU02; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016787; F:hydrolase activity; TAS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0050333; F:thiamine triphosphate phosphatase activity; IDA:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB. DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:UniProtKB. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:Ensembl. DR GO; GO:0042357; P:thiamine diphosphate metabolic process; ISS:UniProtKB. DR GO; GO:0006772; P:thiamine metabolic process; TAS:UniProtKB. DR CDD; cd07758; ThTPase; 1. DR Gene3D; 2.40.320.10; Hypothetical Protein Pfu-838710-001; 1. DR InterPro; IPR033469; CYTH-like_dom_sf. DR InterPro; IPR023577; CYTH_domain. DR InterPro; IPR039582; THTPA. DR InterPro; IPR012177; ThTPase_euk. DR PANTHER; PTHR14586; THIAMINE-TRIPHOSPHATASE; 1. DR PANTHER; PTHR14586:SF1; THIAMINE-TRIPHOSPHATASE; 1. DR Pfam; PF01928; CYTH; 1. DR PIRSF; PIRSF036561; ThTPase; 1. DR SMART; SM01118; CYTH; 1. DR SUPFAM; SSF55154; CYTH-like phosphatases; 1. DR PROSITE; PS51707; CYTH; 1. DR Genevisible; Q9BU02; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Hydrolase; KW Magnesium; Metal-binding; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..230 FT /note="Thiamine-triphosphatase" FT /id="PRO_0000221490" FT DOMAIN 5..201 FT /note="CYTH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 11 FT /ligand="substrate" FT BINDING 55 FT /ligand="substrate" FT BINDING 57 FT /ligand="substrate" FT BINDING 65 FT /ligand="substrate" FT BINDING 125 FT /ligand="substrate" FT BINDING 145 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 157 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 157 FT /ligand="substrate" FT BINDING 159 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 193 FT /ligand="substrate" FT /evidence="ECO:0000305" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT VAR_SEQ 96..105 FT /note="LRADGLGAGD -> CLHRRQHQPS (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_047213" FT VAR_SEQ 106..230 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_047214" FT VARIANT 176 FT /note="H -> R (in dbSNP:rs34015250)" FT /id="VAR_062152" FT MUTAGEN 11 FT /note="K->A: Mildly decreases enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 37 FT /note="D->A: Strongly decreases affinity for thiamine FT triphosphate and enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 39 FT /note="Y->A: Strongly decreases affinity for thiamine FT triphosphate and enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 53 FT /note="W->A: Strongly decreases affinity for thiamine FT triphosphate and enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 65 FT /note="K->A: Strongly decreases enzyme activity. No effect FT on affinity for thiamine triphosphate." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 79 FT /note="Y->A: Decreases enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 81 FT /note="E->A: Mildly decreases enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 147 FT /note="D->A: Strongly decreases affinity for thiamine FT triphosphate and enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT MUTAGEN 193 FT /note="K->A: Strongly decreases affinity for thiamine FT triphosphate and enzyme activity." FT /evidence="ECO:0000269|PubMed:23707715" FT STRAND 5..12 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 18..24 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 28..41 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 46..49 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:3BHD" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 61..70 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 85..96 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 106..113 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 116..131 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 132..135 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 141..149 FT /evidence="ECO:0007829|PDB:3BHD" FT STRAND 154..164 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 168..181 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 193..201 FT /evidence="ECO:0007829|PDB:3BHD" FT HELIX 203..213 FT /evidence="ECO:0007829|PDB:3BHD" SQ SEQUENCE 230 AA; 25566 MW; 49B79C6C1D19D91D CRC64; MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG //