[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Heart; PubMed=7755589 [NCBI, ExPASy, EBI, Israel, Japan] Kim Y.O., Oh I.U., Park H.S., Jeng J., Song B.J., Huh T.L.; "Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species."; Biochem. J. 308:63-68(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Brain cortex; The German cDNA consortium; Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Lymph; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PROTEIN SEQUENCE OF 135-146 AND 179-188, AND MASS SPECTROMETRY. TISSUE=Brain, and Cajal-Retzius cell; Lubec G., Vishwanath V.; Submitted (MAR-2007) to UniProtKB.

Comments

CATALYTIC ACTIVITY: Isocitrate + NAD⁺ = 2-oxoglutarate + CO₂ + NADH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1 (By similarity).
SUBCELLULAR LOCATION: Mitochondrion.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P50213-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P50213-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_014516.

SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U07681; AAA85639.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL442090; CAC09449.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021967; AAH21967.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S55282; S55282.

NP_005521.1; -.

3D structure databases

HSSP

P08200; 1ISO. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P50213.

Protein-protein interaction databases

IntAct

P50213; -.

Enzyme and pathway databases

Reactome

REACT_1046; Pyruvate metabolism and TCA cycle.

2D gel databases

OGP

P50213; -.

REPRODUCTION-2DPAGE

IPI00030702; -.

Organism-specific databases

HGNC:5384; IDH3A.

601149; gene. [NCBI / EBI]

PharmGKB

PA29632; -.

GeneCards

P50213.

Gene expression databases

ArrayExpress

P50213; -.

CleanEx

HS_IDH3A; -.

GermOnline

ENSG00000166411; Homo sapiens.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from experiment from Reactome).
GO:0005975;	Biological process: carbohydrate metabolic process (non-traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00175; mito_nad_idh; 1.

PROSITE

PS00470; IDH_IMDH; 1.

BLOCKS

P50213.

Genome annotation databases

Ensembl

ENSG00000166411; Homo sapiens. [Contig view]

GeneID

3419; -.

KEGG

hsa:3419; -.

NMPDR

fig|9606.3.peg.11057; -.

Phylogenomic databases

HOGENOM

P50213; -.

HOVERGEN

P50213; -.

Other

DB00157; NADH.

IDH3A; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Direct protein sequencing; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 27`	`27`	`Mitochondrion (By similarity).`
`CHAIN`	`28 366`	`339`	`Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial.`	`PRO_0000014436`
`METAL`	`233 233`		`Magnesium or manganese (By similarity).`
`METAL`	`257 257`		`Magnesium or manganese (By similarity).`
`METAL`	`261 261`		`Magnesium or manganese (By similarity).`
`BINDING`	`115 115`		`Substrate (By similarity).`
`BINDING`	`125 125`		`Substrate (By similarity).`
`BINDING`	`146 146`		`Substrate (By similarity).`
`BINDING`	`233 233`		`Substrate (By similarity).`
`SITE`	`153 153`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`200 200`	`1`	`Critical for catalysis (By similarity).`
`VAR_SEQ`	`1 78`		`Missing (in isoform 2).`	`VSP_014516`

Sequence information

Length: 366 AA [This is the length of the unprocessed precursor]

Molecular weight: 39592 Da [This is the MW of the unprocessed precursor]

CRC64: 695F6A34F97430CF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGPAWISKV SRLLGAFHNP KQVTRGFTGG VQTVTLIPGD GIGPEISAAV MKIFDAAKAP 

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

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

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

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

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


RVKDLD

P50213 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools