ID IDHP_MOUSE Reviewed; 452 AA. AC P54071; Q8C2R9; Q9EQK1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 3. DT 27-MAR-2024, entry version 173. DE RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial; DE Short=IDH; DE EC=1.1.1.42 {ECO:0000305|PubMed:8867815}; DE AltName: Full=ICD-M; DE AltName: Full=IDP; DE AltName: Full=NADP(+)-specific ICDH; DE AltName: Full=Oxalosuccinate decarboxylase; DE Flags: Precursor; GN Name=Idh2; 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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=BALB/cJ; TISSUE=Heart; RX PubMed=8867815; RX DOI=10.1002/(sici)1097-4644(19960301)60:3<400::aid-jcb11>3.0.co;2-o; RA Yang L., Luo H., Vinay P., Wu J.; RT "Molecular cloning of the cDNA of mouse mitochondrial NADP-dependent RT isocitrate dehydrogenase and the expression of the gene during lymphocyte RT activation."; RL J. Cell. Biochem. 60:400-410(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=11278619; DOI=10.1074/jbc.m010120200; RA Jo S.-H., Son M.-K., Koh H.-J., Lee S.-M., Song I.-H., Kim Y.-O., RA Lee Y.-S., Jeong K.-S., Kim W.B., Park J.-W., Song B.J., Huhe T.-L.; RT "Control of mitochondrial redox balance and cellular defense against RT oxidative damage by mitochondrial NADP+-dependent isocitrate RT dehydrogenase."; RL J. Biol. Chem. 276:16168-16176(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Heart, and Thymus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; 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 [5] RP PROTEIN SEQUENCE OF 44-60 AND 81-89, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263, SUCCINYLATION [LARGE SCALE RP ANALYSIS] AT LYS-80; LYS-106; LYS-166; LYS-180; LYS-193; LYS-256; LYS-282 RP AND LYS-384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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-45; LYS-48; LYS-69; LYS-80; RP LYS-106; LYS-155; LYS-166; LYS-180; LYS-193; LYS-199; LYS-256; LYS-263; RP LYS-272; LYS-280; LYS-282; LYS-384; LYS-400 AND LYS-442, AND IDENTIFICATION RP 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). CC -!- FUNCTION: Plays a role in intermediary metabolism and energy production CC (PubMed:8867815). It may tightly associate or interact with the CC pyruvate dehydrogenase complex (PubMed:8867815). CC {ECO:0000269|PubMed:8867815}. 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:0000305|PubMed:8867815}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P33198}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P33198}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P33198}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P33198}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:8867815}. CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart, liver and kidney CC (PubMed:8867815, PubMed:11278619). Expressed in activated B lymphocytes CC (PubMed:8867815). {ECO:0000269|PubMed:11278619, CC ECO:0000269|PubMed:8867815}. CC -!- DEVELOPMENTAL STAGE: Up-regulated in activated B lymphocytes. CC {ECO:0000269|PubMed:8867815}. CC -!- INDUCTION: By oxidative stress (at protein level). CC {ECO:0000269|PubMed:11278619}. CC -!- PTM: Acetylation at Lys-413 dramatically reduces catalytic activity. CC Deacetylated by SIRT3 (By similarity). {ECO:0000250|UniProtKB:P48735}. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC52473.1; Type=Frameshift; Evidence={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; U51167; AAC52473.1; ALT_FRAME; mRNA. DR EMBL; AF212319; AAG43538.1; -; mRNA. DR EMBL; AK088110; BAC40149.1; -; mRNA. DR EMBL; AK145753; BAE26628.1; -; mRNA. DR EMBL; AK161640; BAE36505.1; -; mRNA. DR EMBL; AK169395; BAE41142.1; -; mRNA. DR EMBL; BC060030; AAH60030.1; -; mRNA. DR CCDS; CCDS39994.1; -. DR RefSeq; NP_766599.2; NM_173011.2. DR PDB; 5H3E; X-ray; 2.21 A; A/B=40-452. DR PDB; 5H3F; X-ray; 3.29 A; A/B=40-452. DR PDBsum; 5H3E; -. DR PDBsum; 5H3F; -. DR AlphaFoldDB; P54071; -. DR SMR; P54071; -. DR BioGRID; 234733; 15. DR IntAct; P54071; 5. DR MINT; P54071; -. DR STRING; 10090.ENSMUSP00000103007; -. DR ChEMBL; CHEMBL2176829; -. DR GlyGen; P54071; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P54071; -. DR MetOSite; P54071; -. DR PhosphoSitePlus; P54071; -. DR SwissPalm; P54071; -. DR EPD; P54071; -. DR jPOST; P54071; -. DR MaxQB; P54071; -. DR PaxDb; 10090-ENSMUSP00000103007; -. DR PeptideAtlas; P54071; -. DR ProteomicsDB; 267192; -. DR Pumba; P54071; -. DR Antibodypedia; 15858; 542 antibodies from 44 providers. DR DNASU; 269951; -. DR Ensembl; ENSMUST00000107384.10; ENSMUSP00000103007.4; ENSMUSG00000030541.17. DR GeneID; 269951; -. DR KEGG; mmu:269951; -. DR UCSC; uc009hzm.2; mouse. DR AGR; MGI:96414; -. DR CTD; 3418; -. DR MGI; MGI:96414; Idh2. DR VEuPathDB; HostDB:ENSMUSG00000030541; -. DR eggNOG; KOG1526; Eukaryota. DR GeneTree; ENSGT00390000012547; -. DR HOGENOM; CLU_023296_1_1_1; -. DR InParanoid; P54071; -. DR OMA; CIKRQQQ; -. DR OrthoDB; 423at2759; -. DR PhylomeDB; P54071; -. DR TreeFam; TF300428; -. DR BRENDA; 1.1.1.42; 3474. DR Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis. DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle). DR BioGRID-ORCS; 269951; 3 hits in 78 CRISPR screens. DR ChiTaRS; Idh2; mouse. DR PRO; PR:P54071; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P54071; Protein. DR Bgee; ENSMUSG00000030541; Expressed in heart right ventricle and 278 other cell types or tissues. DR ExpressionAtlas; P54071; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005777; C:peroxisome; IDA:MGI. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) 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:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB. DR GO; GO:0006741; P:NADP biosynthetic process; ISO:MGI. DR GO; GO:0006739; P:NADP metabolic process; IBA:GO_Central. DR GO; GO:1903976; P:negative regulation of glial cell migration; ISO:MGI. DR GO; GO:0060253; P:negative regulation of glial cell proliferation; ISO:MGI. DR GO; GO:1904465; P:negative regulation of matrix metallopeptidase secretion; ISO:MGI. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00127; nadp_idh_euk; 1. DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1. DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 1. DR SMART; SM01329; Iso_dh; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. DR PROSITE; PS00470; IDH_IMDH; 1. DR Genevisible; P54071; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Glyoxylate bypass; KW Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; KW Reference proteome; Stress response; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1..39 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:P56574" FT CHAIN 40..452 FT /note="Isocitrate dehydrogenase [NADP], mitochondrial" FT /id="PRO_0000014421" FT BINDING 115..117 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 117 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P33198" FT BINDING 122 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 134..140 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P33198" FT BINDING 149 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P33198" FT BINDING 172 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P33198" FT BINDING 291 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P33198" FT BINDING 299 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 314 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P33198" FT BINDING 349..354 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 367 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT SITE 179 FT /note="Critical for catalysis" FT /evidence="ECO:0000250|UniProtKB:P33198" FT SITE 251 FT /note="Critical for catalysis" FT /evidence="ECO:0000250|UniProtKB:P33198" FT MOD_RES 45 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 48 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 67 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P48735" FT MOD_RES 69 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 80 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 80 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 106 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 106 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 155 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 166 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 166 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 180 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 180 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 193 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 193 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 256 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 256 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 263 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753, FT ECO:0007744|PubMed:23806337" FT MOD_RES 272 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 275 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P48735" FT MOD_RES 280 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 282 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 282 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 384 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 384 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 400 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 413 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P48735" FT MOD_RES 442 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT CONFLICT 104 FT /note="T -> A (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="V -> M (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="I -> S (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 200 FT /note="D -> N (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 214 FT /note="A -> G (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 280 FT /note="K -> R (in Ref. 1; AAC52473 and 2; AAG43538)" FT /evidence="ECO:0000305" FT CONFLICT 322..323 FT /note="QG -> SR (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 367..368 FT /note="NP -> KG (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 398 FT /note="L -> R (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT CONFLICT 408 FT /note="Missing (in Ref. 1; AAC52473)" FT /evidence="ECO:0000305" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 57..69 FT /evidence="ECO:0007829|PDB:5H3E" FT TURN 70..74 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 79..83 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 86..91 FT /evidence="ECO:0007829|PDB:5H3E" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 95..107 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 120..126 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 135..143 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 177..180 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 188..201 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 205..214 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 216..224 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 225..242 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 246..250 FT /evidence="ECO:0007829|PDB:5H3E" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 258..273 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 275..280 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 285..289 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 290..299 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 305..308 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 310..324 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 329..335 FT /evidence="ECO:0007829|PDB:5H3E" FT STRAND 342..345 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 352..359 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 369..386 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 389..407 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 413..420 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 422..424 FT /evidence="ECO:0007829|PDB:5H3E" FT TURN 427..429 FT /evidence="ECO:0007829|PDB:5H3E" FT HELIX 434..449 FT /evidence="ECO:0007829|PDB:5H3E" SQ SEQUENCE 452 AA; 50906 MW; 19BB5CF78512ECAB CRC64; MAGYLRAVSS LCRASGSART WAPAALTVPS WPEQPRRHYA EKRIKVEKPV VEMDGDEMTR IIWQFIKEKL ILPHVDVQLK YFDLGLPNRD QTNDQVTIDS ALATQKYSVA VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTVFRE PIICKNIPRL VPGWTKPITI GRHAHGDQYK ATDFVVDRAG TFKLVFTPKD GSSAKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYSI QKKWPLYLST KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT VTRHYREHQK GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQTLEK VCVQTVESGA MTKDLAGCIH GLSNVKLNEH FLNTTDFLDT IKSNLDRALG KQ //