THTPA_HUMAN
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 03-AUG-2022, entry version 172.
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; 74.
DR IntAct; Q9BU02; 9.
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; Q9BU02; -.
DR PeptideAtlas; Q9BU02; -.
DR PRIDE; Q9BU02; -.
DR ProteomicsDB; 33249; -.
DR ProteomicsDB; 79039; -. [Q9BU02-1]
DR Antibodypedia; 55506; 217 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 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; LMRADHW; -.
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 1082 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 97 other tissues.
DR ExpressionAtlas; Q9BU02; baseline and differential.
DR Genevisible; Q9BU02; HS.
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:thiamin-triphosphatase 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:0042357; P:thiamine diphosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; TAS:UniProtKB.
DR CDD; cd07758; ThTPase; 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; PTHR14586; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF036561; ThTPase; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
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
