IDHC_MOUSE
ID IDHC_MOUSE Reviewed; 414 AA.
AC O88844; Q3UAV7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Isocitrate dehydrogenase [NADP] cytoplasmic;
DE Short=IDH {ECO:0000303|PubMed:29923039};
DE Short=IDH1;
DE EC=1.1.1.42 {ECO:0000269|PubMed:12031902, ECO:0000269|PubMed:29923039};
DE AltName: Full=Cytosolic NADP-isocitrate dehydrogenase;
DE AltName: Full=IDPc;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
GN Name=Idh1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9866202; DOI=10.1093/oxfordjournals.molbev.a025894;
RA Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.;
RT "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and
RT phylogenetic analysis of the enzyme family.";
RL Mol. Biol. Evol. 15:1674-1684(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 30-49.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12031902; DOI=10.1016/s0891-5849(02)00815-8;
RA Lee S.M., Koh H.J., Park D.C., Song B.J., Huh T.L., Park J.W.;
RT "Cytosolic NADP(+)-dependent isocitrate dehydrogenase status modulates
RT oxidative damage to cells.";
RL Free Radic. Biol. Med. 32:1185-1196(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-126 AND LYS-400, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-224; LYS-233 AND LYS-243,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 4-413 IN COMPLEX WITH NADP
RP CITRATE AND CADMIUM, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, AND MUTAGENESIS OF CYS-245 AND CYS-379.
RX PubMed=29923039; DOI=10.1007/s00775-018-1581-5;
RA Cho H.J., Cho H.Y., Park J.W., Kwon O.S., Lee H.S., Huh T.L., Kang B.S.;
RT "NADP(+)-dependent cytosolic isocitrate dehydrogenase provides NADPH in the
RT presence of cadmium due to the moderate chelating effect of glutathione.";
RL J. Biol. Inorg. Chem. 23:849-860(2018).
CC -!- FUNCTION: Catalyzes the NADP(+)-dependent oxidative decarboxylation of
CC isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate),
CC which is required by other enzymes such as the phytanoyl-CoA
CC dioxygenase (PubMed:12031902, PubMed:29923039). Plays a critical role
CC in the generation of NADPH, an important cofactor in many biosynthesis
CC pathways (PubMed:12031902). May act as a corneal epithelial crystallin
CC and may be involved in maintaining corneal epithelial transparency (By
CC similarity). {ECO:0000250|UniProtKB:Q9XSG3,
CC ECO:0000269|PubMed:12031902, ECO:0000269|PubMed:29923039,
CC ECO:0000303|PubMed:12031902}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC Evidence={ECO:0000269|PubMed:12031902, ECO:0000269|PubMed:29923039};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19630;
CC Evidence={ECO:0000305|PubMed:12031902, ECO:0000305|PubMed:29923039};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29923039};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:29923039};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000305|PubMed:29923039};
CC -!- ACTIVITY REGULATION: Irreversibly inhibited by Cd(2+) concentrations
CC above 50 uM. {ECO:0000269|PubMed:29923039}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29923039}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12031902}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver followed by kidney,
CC lower expression in spleen, brain and lung.
CC {ECO:0000269|PubMed:12031902}.
CC -!- PTM: Acetylation at Lys-374 dramatically reduces catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; AF020039; AAD02919.1; -; mRNA.
DR EMBL; AK149019; BAE28720.1; -; mRNA.
DR EMBL; AK151212; BAE30207.1; -; mRNA.
DR EMBL; AK159173; BAE34873.1; -; mRNA.
DR EMBL; AK160896; BAE36075.1; -; mRNA.
DR EMBL; AK167158; BAE39299.1; -; mRNA.
DR EMBL; CH466548; EDL00223.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00225.1; -; Genomic_DNA.
DR CCDS; CCDS15016.1; -.
DR RefSeq; NP_001104790.1; NM_001111320.1.
DR RefSeq; NP_034627.3; NM_010497.3.
DR PDB; 5YZH; X-ray; 1.99 A; A/B=1-414.
DR PDB; 5YZI; X-ray; 2.52 A; A/B=1-414.
DR PDBsum; 5YZH; -.
DR PDBsum; 5YZI; -.
DR AlphaFoldDB; O88844; -.
DR SMR; O88844; -.
DR BioGRID; 200510; 15.
DR IntAct; O88844; 3.
DR MINT; O88844; -.
DR STRING; 10090.ENSMUSP00000095316; -.
DR CarbonylDB; O88844; -.
DR iPTMnet; O88844; -.
DR PhosphoSitePlus; O88844; -.
DR SwissPalm; O88844; -.
DR COMPLUYEAST-2DPAGE; O88844; -.
DR REPRODUCTION-2DPAGE; O88844; -.
DR SWISS-2DPAGE; O88844; -.
DR CPTAC; non-CPTAC-3715; -.
DR EPD; O88844; -.
DR jPOST; O88844; -.
DR MaxQB; O88844; -.
DR PaxDb; O88844; -.
DR PeptideAtlas; O88844; -.
DR PRIDE; O88844; -.
DR ProteomicsDB; 269529; -.
DR Antibodypedia; 34198; 988 antibodies from 47 providers.
DR DNASU; 15926; -.
DR Ensembl; ENSMUST00000097709; ENSMUSP00000095316; ENSMUSG00000025950.
DR Ensembl; ENSMUST00000169032; ENSMUSP00000127307; ENSMUSG00000025950.
DR GeneID; 15926; -.
DR KEGG; mmu:15926; -.
DR UCSC; uc007bhn.2; mouse.
DR CTD; 3417; -.
DR MGI; MGI:96413; Idh1.
DR VEuPathDB; HostDB:ENSMUSG00000025950; -.
DR eggNOG; KOG1526; Eukaryota.
DR GeneTree; ENSGT00390000012547; -.
DR HOGENOM; CLU_023296_1_1_1; -.
DR InParanoid; O88844; -.
DR OMA; HGTVQRH; -.
DR OrthoDB; 769322at2759; -.
DR PhylomeDB; O88844; -.
DR TreeFam; TF300428; -.
DR BRENDA; 1.1.1.42; 3474.
DR Reactome; R-MMU-389542; NADPH regeneration.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 15926; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Idh1; mouse.
DR EvolutionaryTrace; O88844; -.
DR PRO; PR:O88844; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O88844; protein.
DR Bgee; ENSMUSG00000025950; Expressed in metanephric proximal tubule and 287 other tissues.
DR ExpressionAtlas; O88844; baseline and differential.
DR Genevisible; O88844; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IDA:MGI.
DR GO; GO:0004448; F:isocitrate dehydrogenase activity; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; IBA:GO_Central.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IMP:MGI.
DR GO; GO:0060696; P:regulation of phospholipid catabolic process; IMP:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR GO; GO:0048545; P:response to steroid hormone; ISO:MGI.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR11822; PTHR11822; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT CHAIN 2..414
FT /note="Isocitrate dehydrogenase [NADP] cytoplasmic"
FT /id="PRO_0000083578"
FT BINDING 75..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZH, ECO:0007744|PDB:5YZI"
FT BINDING 77
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZI"
FT BINDING 82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZH, ECO:0007744|PDB:5YZI"
FT BINDING 94..100
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZI"
FT BINDING 109
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZI"
FT BINDING 132
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZI"
FT BINDING 212
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZI"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000305|PubMed:29923039"
FT BINDING 260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZH, ECO:0007744|PDB:5YZI"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:29923039"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:29923039"
FT BINDING 310..315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZH, ECO:0007744|PDB:5YZI"
FT BINDING 328
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29923039,
FT ECO:0007744|PDB:5YZH, ECO:0007744|PDB:5YZI"
FT SITE 139
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 212
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT MOD_RES 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 126
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 224
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 400
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 245
FT /note="C->S: No effect on inhibition by cadmium ions."
FT /evidence="ECO:0000269|PubMed:29923039"
FT MUTAGEN 379
FT /note="C->S: Decreased inhibition by cadmium ions."
FT /evidence="ECO:0000269|PubMed:29923039"
FT CONFLICT 243
FT /note="K -> N (in Ref. 1; AAD02919)"
FT /evidence="ECO:0000305"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:5YZH"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:5YZH"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:5YZH"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:5YZH"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 330..347
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 350..368
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:5YZH"
FT HELIX 394..413
FT /evidence="ECO:0007829|PDB:5YZH"
SQ SEQUENCE 414 AA; 46674 MW; C7FEF315D042C44C CRC64;
MSRKIQGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA
AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL
VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GTQKVTYMVH DFEEGGGVAM
GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKKYKSQFE
AQKICYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFAKALE
DVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL
