IDH2_ARATH
ID IDH2_ARATH Reviewed; 367 AA.
AC P93032; Q7XJT6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Isocitrate dehydrogenase [NAD] regulatory subunit 2, mitochondrial;
DE AltName: Full=IDH-II;
DE AltName: Full=Isocitric dehydrogenase 2;
DE AltName: Full=NAD(+)-specific ICDH 2;
DE Flags: Precursor;
GN Name=IDH2; OrderedLocusNames=At2g17130; ORFNames=F6P23.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9526501; DOI=10.1023/a:1005923410940;
RA Behal R.H., Oliver D.J.;
RT "NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana.
RT Characterization of two closely related subunits.";
RL Plant Mol. Biol. 36:691-698(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP GENE FAMILY, FUNCTION, AND TISSUE SPECIFICITY.
RX AGRICOLA=IND43633651; DOI=10.1016/j.plantsci.2003.12.012;
RA Lin M., Behal R.H., Oliver D.J.;
RT "Characterization of a mutation in the IDH-II subunit of the NAD(+)-
RT dependent isocitrate dehydrogenase from Arabidopsis thaliana.";
RL Plant Sci. 166:983-988(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16527867; DOI=10.1093/pcp/pcj030;
RA Lemaitre T., Hodges M.;
RT "Expression analysis of Arabidopsis thaliana NAD-dependent isocitrate
RT dehydrogenase genes shows the presence of a functional subunit that is
RT mainly expressed in the pollen and absent from vegetative organs.";
RL Plant Cell Physiol. 47:634-643(2006).
CC -!- FUNCTION: Performs an essential role in the oxidative function of the
CC citric acid cycle. {ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Heterooligomer of catalytic and regulatory subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P93032-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P93032-2; Sequence=VSP_027467;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in roots, stems
CC and leaves. {ECO:0000269|PubMed:16527867, ECO:0000269|Ref.6}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; U81994; AAC49965.1; -; mRNA.
DR EMBL; CP002685; AEC06588.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06589.1; -; Genomic_DNA.
DR EMBL; AK228337; BAF00277.1; -; mRNA.
DR PIR; D84548; D84548.
DR RefSeq; NP_179304.1; NM_127267.3. [P93032-1]
DR RefSeq; NP_849963.1; NM_179632.2. [P93032-2]
DR AlphaFoldDB; P93032; -.
DR SMR; P93032; -.
DR BioGRID; 1575; 3.
DR STRING; 3702.AT2G17130.1; -.
DR PaxDb; P93032; -.
DR PRIDE; P93032; -.
DR ProteomicsDB; 248615; -. [P93032-1]
DR EnsemblPlants; AT2G17130.1; AT2G17130.1; AT2G17130. [P93032-1]
DR EnsemblPlants; AT2G17130.2; AT2G17130.2; AT2G17130. [P93032-2]
DR GeneID; 816218; -.
DR Gramene; AT2G17130.1; AT2G17130.1; AT2G17130. [P93032-1]
DR Gramene; AT2G17130.2; AT2G17130.2; AT2G17130. [P93032-2]
DR KEGG; ath:AT2G17130; -.
DR Araport; AT2G17130; -.
DR TAIR; locus:2827696; AT2G17130.
DR eggNOG; KOG0784; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; P93032; -.
DR OMA; NGDDIGH; -.
DR PhylomeDB; P93032; -.
DR BioCyc; MetaCyc:AT2G17130-MON; -.
DR BRENDA; 1.1.1.41; 399.
DR PRO; PR:P93032; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93032; baseline and differential.
DR Genevisible; P93032; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW NAD; Oxidoreductase; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..367
FT /note="Isocitrate dehydrogenase [NAD] regulatory subunit 2,
FT mitochondrial"
FT /id="PRO_0000271288"
FT VAR_SEQ 171..174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027467"
FT CONFLICT 6
FT /note="F -> S (in Ref. 1; AAC49965)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="G -> R (in Ref. 1; AAC49965)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="T -> S (in Ref. 1; AAC49965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 39590 MW; B5BC1C422AF757F7 CRC64;
MSRQSFSLLK NLRSIASGSK IQTRSVTYMP RPGDGKPRPV TLIPGDGVGP LVTNAVQQVM
EAMHAPVYFE PFEVHGDMKS LPEGLLESIK KNKVCLKGGL KTPVGGGVSS LNVNLRKELD
LFASLVNCFN LPGLASRHEN VDIVVIRENT EGEYAGLEHE VVPGVVESLK VITKFCSERI
AKYAFEYAYL NNRKKVTAVH KANIMKLADG LFLESCQEVA KKYPSIAYNE IIVDNCCMQL
VARPEQFDVM VTPNLYGNLV ANTAAGIAGG TGVMPGGNVG AEYAVFEQGA SAGNVGKDTT
EEQKNANPVA LLLSSAMMLR HLQFPSFADR LETAVKRVIA EGNCRTEDLG GNSTTQEVVD
AVIANLD
