[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; PubMed=8083215 [NCBI, ExPASy, EBI, Israel, Japan] Jennings G.T., Sechi S., Stevenson P.M., Tuckey R.C., Parmelee D., McAlister-Henn L.; "Cytosolic NADP(+)-dependent isocitrate dehydrogenase. Isolation of rat cDNA and study of tissue-specific and developmental expression of mRNA."; J. Biol. Chem. 269:23128-23134(1994).
[2]	PROTEIN SEQUENCE OF 389-400, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.
[3]	PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. TISSUE=Ovary; PubMed=7787968 [NCBI, ExPASy, EBI, Israel, Japan] Sechi S., Parmelee D., Roller P.R., Jennings G.T.; "Structural characterization of cytosolic NADP(+)-dependent isocitrate dehydrogenase from rat ovary."; Enzyme Protein 48:27-36(1995).

Comments

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.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Ovary, mammary gland and liver.
PTM: The N-terminus is blocked.
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

L35317; AAA59356.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A54756; A54756.

NP_113698.1; -.

3D structure databases

HSSP

P33198; 1LWD. [HSSP ENTRY / PDB]

SMR

P41562; 1-414.

ModBase

P41562.

Organism-specific databases

RGD

2862; Idh1.

Gene expression databases

ArrayExpress

P41562; -.

GermOnline

ENSRNOG00000015020; Rattus norvegicus.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from direct assay from HGNC).
GO:0004450;	Molecular function: isocitrate dehydrogenase (NADP+) activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006097;	Biological process: glyoxylate cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006102;	Biological process: isocitrate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProtoNet

P41562.

Genome annotation databases

Ensembl

ENSRNOG00000015020; Rattus norvegicus. [Contig view]

GeneID

24479; -.

KEGG

rno:24479; -.

Phylogenomic databases

HOVERGEN

P41562; -.

Other

NextBio

603439; -.

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 414`	`414`	`Isocitrate dehydrogenase [NADP] cytoplasmic.`	`PRO_0000083580`
`NP_BIND`	`75 77`	`3`	`NADP (By similarity).`
`NP_BIND`	`310 315`	`6`	`NADP (By similarity).`
`REGION`	`94 100`	`7`	`Substrate binding (By similarity).`
`METAL`	`252 252`		`Magnesium or manganese (By similarity).`
`METAL`	`275 275`		`Magnesium or manganese (By similarity).`
`BINDING`	`77 77`		`Substrate (By similarity).`
`BINDING`	`82 82`		`NADP (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`132 132`		`Substrate (By similarity).`
`BINDING`	`260 260`		`NADP (By similarity).`
`BINDING`	`328 328`		`NADP; via amide nitrogen and carbonyl oxygen (By similarity).`
`SITE`	`139 139`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`212 212`	`1`	`Critical for catalysis (By similarity).`

Sequence information

Length: 414 AA [This is the length of the unprocessed precursor]

Molecular weight: 46734 Da [This is the MW of the unprocessed precursor]

CRC64: CF69EE8746DC1AF6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRKIHGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA 

        70         80         90        100        110        120 
AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL 

       130        140        150        160        170        180 
VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GSQKVTYLVH DFEEGGGVAM 

       190        200        210        220        230        240 
GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSKFE 

       250        260        270        280        290        300 
AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG 

       310        320        330        340        350        360 
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFANALE 

       370        380        390        400        410 
EVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL

P41562 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