IDHP_MOUSE
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 03-AUG-2022, entry version 164.
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, 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 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; 12.
DR IntAct; P54071; 5.
DR MINT; P54071; -.
DR STRING; 10090.ENSMUSP00000103007; -.
DR ChEMBL; CHEMBL2176829; -.
DR iPTMnet; P54071; -.
DR PhosphoSitePlus; P54071; -.
DR SwissPalm; P54071; -.
DR EPD; P54071; -.
DR jPOST; P54071; -.
DR MaxQB; P54071; -.
DR PaxDb; P54071; -.
DR PeptideAtlas; P54071; -.
DR PRIDE; P54071; -.
DR ProteomicsDB; 267192; -.
DR Antibodypedia; 15858; 476 antibodies from 44 providers.
DR DNASU; 269951; -.
DR Ensembl; ENSMUST00000107384; ENSMUSP00000103007; ENSMUSG00000030541.
DR GeneID; 269951; -.
DR KEGG; mmu:269951; -.
DR UCSC; uc009hzm.2; mouse.
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; IQKRWPL; -.
DR OrthoDB; 769322at2759; -.
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 73 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 274 other tissues.
DR ExpressionAtlas; P54071; baseline and differential.
DR Genevisible; P54071; MM.
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: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: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 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; 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
