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Q9D6R2 (IDH3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial

EC=1.1.1.41
Alternative name(s):
Isocitric dehydrogenase subunit alpha
NAD(+)-specific ICDH subunit alpha
Gene names
Name:Idh3a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subunit structure

Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1 By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandMagnesium
Manganese
Metal-binding
NAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

isocitrate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D6R2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9D6R2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 366339Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
PRO_0000014438

Sites

Metal binding2331Magnesium or manganese By similarity
Metal binding2571Magnesium or manganese By similarity
Metal binding2611Magnesium or manganese By similarity
Binding site1151Substrate By similarity
Binding site1251Substrate By similarity
Binding site1461Substrate By similarity
Binding site2331Substrate By similarity
Site1531Critical for catalysis By similarity
Site2001Critical for catalysis By similarity

Amino acid modifications

Modified residue771N6-succinyllysine Ref.4
Modified residue2231N6-acetyllysine Ref.5
Modified residue3431N6-acetyllysine; alternate By similarity
Modified residue3431N6-succinyllysine; alternate Ref.4
Modified residue3501N6-succinyllysine Ref.4

Natural variations

Alternative sequence1 – 7878Missing in isoform 2.
VSP_014517

Experimental info

Sequence conflict3061A → T in BAC33199. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9F1D68C269376955

FASTA36639,639
        10         20         30         40         50         60 
MAGSAWVSKV SRLLGAFHNT KQVTRGFAGG VQTVTLIPGD GIGPEISASV MKIFDAAKAP 

        70         80         90        100        110        120 
IQWEERNVTA IQGPGGKWMI PPEAKESMDK NKMGLKGPLK TPIAAGHPSM NLLLRKTFDL 

       130        140        150        160        170        180 
YANVRPCVSI EGYKTPYTDV NIVTIRENTE GEYSGIEHVI VDGVVQSIKL ITEEASKRIA 

       190        200        210        220        230        240 
EFAFEYARNN HRSNVTAVHK ANIMRMSDGL FLQKCREVAE NCKDIKFNEM YLDTVCLNMV 

       250        260        270        280        290        300 
QDPSQFDVLV MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD 

       310        320        330        340        350        360 
MANPTALLLS AVMMLRHMGL FDHAAKIEAA CFATIKDGKS LTKDLGGNAK CSDFTEEICR 


RVKDLD 

« Hide

Isoform 2 [UniParc].

Checksum: 5A6F91BF1BBD4FC5
Show »

FASTA28831,462

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and DBA/2.
Tissue: Bone marrow, Heart, Tongue, Visual cortex and Wolffian duct.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: FVB/N.
Tissue: Liver.
[3]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 59-85; 101-188; 206-214 AND 300-336, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-343 AND LYS-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003393 mRNA. Translation: BAB22760.1.
AK010065 mRNA. Translation: BAB26679.1.
AK032787 mRNA. Translation: BAC28021.1.
AK047951 mRNA. Translation: BAC33199.1.
AK150618 mRNA. Translation: BAE29708.1.
AK151304 mRNA. Translation: BAE30286.1.
AK152353 mRNA. Translation: BAE31145.1.
AK153459 mRNA. Translation: BAE32011.1.
AK158646 mRNA. Translation: BAE34596.1.
AK159051 mRNA. Translation: BAE34785.1.
AK168049 mRNA. Translation: BAE40031.1.
AK168149 mRNA. Translation: BAE40114.1.
AK169152 mRNA. Translation: BAE40931.1.
BC034273 mRNA. Translation: AAH34273.1.
BC049956 mRNA. Translation: AAH49956.1.
CCDSCCDS23191.1. [Q9D6R2-1]
RefSeqNP_083849.1. NM_029573.2. [Q9D6R2-1]
UniGeneMm.279195.

3D structure databases

ProteinModelPortalQ9D6R2.
SMRQ9D6R2. Positions 30-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D6R2. 8 interactions.
MINTMINT-1861233.

PTM databases

PhosphoSiteQ9D6R2.

2D gel databases

REPRODUCTION-2DPAGEQ9D6R2.
UCD-2DPAGEQ9D6R2.

Proteomic databases

MaxQBQ9D6R2.
PaxDbQ9D6R2.
PRIDEQ9D6R2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000167866; ENSMUSP00000127526; ENSMUSG00000032279. [Q9D6R2-1]
GeneID67834.
KEGGmmu:67834.
UCSCuc009prg.1. mouse. [Q9D6R2-1]

Organism-specific databases

CTD3419.
MGIMGI:1915084. Idh3a.

Phylogenomic databases

eggNOGCOG0473.
GeneTreeENSGT00550000074918.
HOGENOMHOG000021113.
HOVERGENHBG052080.
InParanoidQ9D6R2.
KOK00030.
OMATPIAWEP.
OrthoDBEOG75B85R.
PhylomeDBQ9D6R2.
TreeFamTF105692.

Gene expression databases

BgeeQ9D6R2.
CleanExMM_IDH3A.
GenevestigatorQ9D6R2.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00175. mito_nad_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio325657.
PROQ9D6R2.
SOURCESearch...

Entry information

Entry nameIDH3A_MOUSE
AccessionPrimary (citable) accession number: Q9D6R2
Secondary accession number(s): Q3UAM8, Q8C8A1, Q9D1L1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot