[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; 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).
[2]	PROTEIN SEQUENCE OF 40-52, AND SUBCELLULAR LOCATION. STRAIN=Wistar; TISSUE=Heart; Li X.-P., Pleissner K.-P., Scheler C., Regitz-Zagrosek V., Salikov J., Jungblut P.R.; Submitted (SEP-1998) to UniProtKB.
[3]	PROTEIN SEQUENCE OF 61-67; 70-89; 113-122; 141-149; 181-188; 244-251; 262-272; 289-299; 341-353 AND 414-426, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus; Lubec G., Chen W.-Q.; Submitted (APR-2007) to UniProtKB.

Comments

FUNCTION: Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex (By similarity).
CATALYTIC ACTIVITY: Isocitrate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.
CATALYTIC ACTIVITY: Oxalosuccinate + NADP⁺ = 2-oxoglutarate + CO₂ + NADPH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion.
MISCELLANEOUS: On the 2D-gel the determined pI of this protein (spot P8) is: 9.0, its MW is: 42 kDa.
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

BC076398; AAH76398.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001014183.1; -.

UniGene

Rn.3490

3D structure databases

SMR

P56574; 40-452.

ModBase

P56574.

Protein-protein interaction databases

IntAct

P56574; -.

Organism-specific databases

RGD

1597139; Idh2.

Gene expression databases

ArrayExpress

P56574; -.

Family and domain databases

InterPro

IPR004790; IsoCit_DHase_NADP-dep_euk.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11822; IDH_NADP_euk; 1.

Pfam

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

PIRSF

PIRSF000108; IDH_NADP; 1.

TIGRFAMs

TIGR00127; nadp_idh_euk; 1.

PROSITE

PS00470; IDH_IMDH; 1.

BLOCKS

P56574.

Genome annotation databases

Ensembl

ENSRNOG00000013949; Rattus norvegicus. [Contig view]

GeneID

361596; -.

KEGG

rno:361596; -.

Phylogenomic databases

HOVERGEN

P56574; -.

Other

ProtoNet

P56574.

UniRef

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

Keywords

Acetylation; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion (By similarity).`
`CHAIN`	`40 452`	`413`	`Isocitrate dehydrogenase [NADP], mitochondrial.`	`PRO_0000083581`
`NP_BIND`	`115 117`	`3`	`NADP (By similarity).`
`NP_BIND`	`349 354`	`6`	`NADP (By similarity).`
`REGION`	`134 140`	`7`	`Substrate binding (By similarity).`
`METAL`	`291 291`		`Magnesium or manganese (By similarity).`
`METAL`	`314 314`		`Magnesium or manganese (By similarity).`
`BINDING`	`117 117`		`Substrate (By similarity).`
`BINDING`	`122 122`		`NADP (By similarity).`
`BINDING`	`149 149`		`Substrate (By similarity).`
`BINDING`	`172 172`		`Substrate (By similarity).`
`BINDING`	`299 299`		`NADP (By similarity).`
`BINDING`	`367 367`		`NADP; via amide nitrogen and carbonyl oxygen (By similarity).`
`SITE`	`179 179`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`251 251`	`1`	`Critical for catalysis (By similarity).`
`MOD_RES`	`106 106`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`272 272`		`N6-acetyllysine (By similarity).`
`CONFLICT`	`49 49`		`P -> K (in Ref. 2; AA sequence).`
`CONFLICT`	`52 52`		`E -> V (in Ref. 2; AA sequence).`

Sequence information

Length: 452 AA [This is the length of the unprocessed precursor]

Molecular weight: 50967 Da [This is the MW of the unprocessed precursor]

CRC64: 2466E1CC2C2CE9D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGYLRAVSS LCRASGSTRT WAPAALNVPS WPEQPRRHYA EKRIKVEKPV VEMDGDEMTR 

        70         80         90        100        110        120 
IIWQFIKEKL ILPHVDVQLK YFDLGLPNRD QTNDQVTIDS ALATQKYSVA VKCATITPDE 

       130        140        150        160        170        180 
ARVEEFKLKK MWKSPNGTIR NILGGTVFRE PIICKNIPRL VPGWTKPITI GRHAHGDQYK 

       190        200        210        220        230        240 
ATDFVVDRAG MFKLVFTPKD GSGAKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYSI 

       250        260        270        280        290        300 
QKKWPLYLST KNTIMKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS 

       310        320        330        340        350        360 
SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT VTRHYREHQK 

       370        380        390        400        410        420 
GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQTLEK VCVQTVESGA MTKDLAGCIH 

       430        440        450 
GLSNVKLNEH FLNTTDFLDT IKSNLDRALG KQ

P56574 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