MIOX_HUMAN
ID MIOX_HUMAN Reviewed; 285 AA.
AC Q9UGB7; Q05DJ6; Q5S8C9; Q9BZZ1; Q9UHB8;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Inositol oxygenase;
DE EC=1.13.99.1;
DE AltName: Full=Aldehyde reductase-like 6;
DE AltName: Full=Kidney-specific protein 32;
DE AltName: Full=Myo-inositol oxygenase;
DE Short=MI oxygenase;
DE AltName: Full=Renal-specific oxidoreductase;
GN Name=MIOX; Synonyms=ALDRL6, KSP32, RSOR;
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).
RA Parthasarathy L., Seelan R., Parthasarathy R.;
RT "Cloning and expression of human myo-inositol oxygenase (MIOX).";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Hu E., Chen Z., Fredrickson T., Gellai M., Jugus M., Contino L., Spurr N.,
RA Sims M., Halsey W., Van Horn S., Mao J., Sathe G., Brooks D.;
RT "Identification of a novel kidney specific gene, KSP32, that is down
RT regulated in acute ischemic renal failure.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=10944187; DOI=10.1073/pnas.160266197;
RA Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K.,
RA Kanwar Y.S.;
RT "Identification of a renal-specific oxido-reductase in newborn diabetic
RT mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15504367; DOI=10.1016/j.bbrc.2004.09.209;
RA Arner R.J., Prabhu K.S., Reddy C.C.;
RT "Molecular cloning, expression, and characterization of myo-inositol
RT oxygenase from mouse, rat, and human kidney.";
RL Biochem. Biophys. Res. Commun. 324:1386-1392(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [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 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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Kidney;
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-285 IN COMPLEX WITH IRON AND
RP MYO-INOSOSE-1, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF LYS-127.
RX PubMed=18364358; DOI=10.1074/jbc.m800348200;
RA Thorsell A.G., Persson C., Voevodskaya N., Busam R.D., Hammarstrom M.,
RA Graslund S., Graslund A., Hallberg B.M.;
RT "Structural and biophysical characterization of human myo-inositol
RT oxygenase.";
RL J. Biol. Chem. 283:15209-15216(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=myo-inositol + O2 = D-glucuronate + H(+) + H2O;
CC Xref=Rhea:RHEA:23696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17268, ChEBI:CHEBI:58720;
CC EC=1.13.99.1; Evidence={ECO:0000269|PubMed:18364358};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:18364358};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:18364358};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC glucuronate; D-glucuronate from myo-inositol: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGB7-2; Sequence=VSP_041667, VSP_041668;
CC -!- TISSUE SPECIFICITY: Kidney specific.
CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC {ECO:0000305}.
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DR EMBL; AY064416; AAL47192.1; -; mRNA.
DR EMBL; AF230095; AAK00766.1; -; mRNA.
DR EMBL; AF197129; AAF25204.1; -; mRNA.
DR EMBL; AY738258; AAV65816.1; -; mRNA.
DR EMBL; AK000576; BAA91266.1; -; mRNA.
DR EMBL; CR456478; CAG30364.1; -; mRNA.
DR EMBL; AL096767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73547.1; -; Genomic_DNA.
DR EMBL; BC012025; AAH12025.1; -; mRNA.
DR EMBL; BC073848; AAH73848.1; -; mRNA.
DR CCDS; CCDS14092.1; -. [Q9UGB7-1]
DR RefSeq; NP_060054.4; NM_017584.5. [Q9UGB7-1]
DR PDB; 2IBN; X-ray; 1.50 A; A/B=38-285.
DR PDBsum; 2IBN; -.
DR AlphaFoldDB; Q9UGB7; -.
DR SMR; Q9UGB7; -.
DR BioGRID; 120733; 18.
DR STRING; 9606.ENSP00000216075; -.
DR iPTMnet; Q9UGB7; -.
DR PhosphoSitePlus; Q9UGB7; -.
DR BioMuta; MIOX; -.
DR jPOST; Q9UGB7; -.
DR MassIVE; Q9UGB7; -.
DR PaxDb; Q9UGB7; -.
DR PeptideAtlas; Q9UGB7; -.
DR PRIDE; Q9UGB7; -.
DR ProteomicsDB; 84204; -. [Q9UGB7-1]
DR ProteomicsDB; 84205; -. [Q9UGB7-2]
DR TopDownProteomics; Q9UGB7-1; -. [Q9UGB7-1]
DR Antibodypedia; 53923; 312 antibodies from 21 providers.
DR DNASU; 55586; -.
DR Ensembl; ENST00000216075.11; ENSP00000216075.6; ENSG00000100253.13. [Q9UGB7-1]
DR Ensembl; ENST00000395733.7; ENSP00000379082.3; ENSG00000100253.13. [Q9UGB7-2]
DR GeneID; 55586; -.
DR KEGG; hsa:55586; -.
DR MANE-Select; ENST00000216075.11; ENSP00000216075.6; NM_017584.6; NP_060054.4.
DR UCSC; uc003bll.2; human. [Q9UGB7-1]
DR CTD; 55586; -.
DR DisGeNET; 55586; -.
DR GeneCards; MIOX; -.
DR HGNC; HGNC:14522; MIOX.
DR HPA; ENSG00000100253; Tissue enriched (kidney).
DR MIM; 606774; gene.
DR neXtProt; NX_Q9UGB7; -.
DR OpenTargets; ENSG00000100253; -.
DR PharmGKB; PA24716; -.
DR VEuPathDB; HostDB:ENSG00000100253; -.
DR eggNOG; KOG1573; Eukaryota.
DR GeneTree; ENSGT00390000016211; -.
DR HOGENOM; CLU_1351676_0_0_1; -.
DR InParanoid; Q9UGB7; -.
DR OMA; RYNTKYG; -.
DR OrthoDB; 1436589at2759; -.
DR PhylomeDB; Q9UGB7; -.
DR TreeFam; TF300089; -.
DR BRENDA; 1.13.99.1; 2681.
DR PathwayCommons; Q9UGB7; -.
DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; Q9UGB7; -.
DR UniPathway; UPA00111; UER00527.
DR BioGRID-ORCS; 55586; 10 hits in 1066 CRISPR screens.
DR ChiTaRS; MIOX; human.
DR EvolutionaryTrace; Q9UGB7; -.
DR GenomeRNAi; 55586; -.
DR Pharos; Q9UGB7; Tbio.
DR PRO; PR:Q9UGB7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UGB7; protein.
DR Bgee; ENSG00000100253; Expressed in kidney epithelium and 74 other tissues.
DR ExpressionAtlas; Q9UGB7; baseline and differential.
DR Genevisible; Q9UGB7; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016234; C:inclusion body; ISS:UniProtKB.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR GO; GO:0050113; F:inositol oxygenase activity; IDA:UniProtKB.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:Ensembl.
DR GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; ISS:UniProtKB.
DR GO; GO:0019310; P:inositol catabolic process; IDA:UniProtKB.
DR InterPro; IPR007828; Inositol_oxygenase.
DR PANTHER; PTHR12588; PTHR12588; 1.
DR Pfam; PF05153; MIOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Iron; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..285
FT /note="Inositol oxygenase"
FT /id="PRO_0000079148"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85..87
FT /ligand="substrate"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18364358"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18364358"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18364358"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18364358"
FT BINDING 127
FT /ligand="substrate"
FT BINDING 141..142
FT /ligand="substrate"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18364358"
FT BINDING 220..221
FT /ligand="substrate"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18364358"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18364358"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXN4"
FT VAR_SEQ 114..231
FT /note="DWFHLVGLLHDLGKVLALFGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNP
FT DLQDPRYSTELGMYQPHCGLDRVLMSWGHDEYMYQVMKFNKFSLPPEAFYMIRFHSFYP
FT WHTGRDY -> VPNLPCPSPSQTGSTSSGSCTTWGRSWPCSGSPSGLSSATPSPSDAVR
FT RPPWFSATPPSRTTLTSRILDTAQSSGCISPTVGSTGSSCPGAMMQVRPLHQVPGPAGR
FT GQAAALLPGAH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041667"
FT VAR_SEQ 232..285
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041668"
FT MUTAGEN 127
FT /note="K->S: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:18364358"
FT CONFLICT 4
FT /note="T -> D (in Ref. 3; AAF25204)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="Y -> F (in Ref. 2; AAK00766)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..221
FT /note="FHS -> VHF (in Ref. 2; AAK00766)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> T (in Ref. 3; AAF25204)"
FT /evidence="ECO:0000305"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:2IBN"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2IBN"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2IBN"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2IBN"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:2IBN"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 237..253
FT /evidence="ECO:0007829|PDB:2IBN"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:2IBN"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2IBN"
SQ SEQUENCE 285 AA; 33010 MW; ED70B197FF267B2B CRC64;
MKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH
AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG
LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ
PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL
AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW
