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P41562 (IDHC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP] cytoplasmic

Short name=IDH
EC=1.1.1.42
Alternative name(s):
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:Idh1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length414 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 + NADP+ = 2-oxoglutarate + CO2 + NADPH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Ovary, mammary gland and liver.

Post-translational modification

The N-terminus is blocked.

Acetylation at Lys-374 dramatically reduces catalytic activity By similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

female gonad development

Inferred from expression pattern Ref.1. Source: RGD

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

glyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

isocitrate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to organic cyclic compound

Inferred from direct assay PubMed 8486157. Source: RGD

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from direct assay PubMed 8349575. Source: RGD

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisome

Inferred from direct assay PubMed 14561759. Source: HGNC

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from direct assay PubMed 17447164. Source: RGD

isocitrate dehydrogenase (NADP+) activity

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 414413Isocitrate dehydrogenase [NADP] cytoplasmic
PRO_0000083580

Regions

Nucleotide binding75 – 773NADP By similarity
Nucleotide binding310 – 3156NADP By similarity
Region94 – 1007Substrate binding By similarity

Sites

Metal binding2521Magnesium or manganese By similarity
Metal binding2751Magnesium or manganese By similarity
Binding site771Substrate By similarity
Binding site821NADP By similarity
Binding site1091Substrate By similarity
Binding site1321Substrate By similarity
Binding site2601NADP By similarity
Binding site3281NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1391Critical for catalysis By similarity
Site2121Critical for catalysis By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue1261N6-succinyllysine By similarity
Modified residue2241N6-acetyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue4001N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P41562 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: CF69EE8746DC1AF6

FASTA41446,734
        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 

« Hide

References

[1]"Cytosolic NADP(+)-dependent isocitrate dehydrogenase. Isolation of rat cDNA and study of tissue-specific and developmental expression of mRNA."
Jennings G.T., Sechi S., Stevenson P.M., Tuckey R.C., Parmelee D., McAlister-Henn L.
J. Biol. Chem. 269:23128-23134(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 389-400, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[3]"Structural characterization of cytosolic NADP(+)-dependent isocitrate dehydrogenase from rat ovary."
Sechi S., Parmelee D., Roller P.R., Jennings G.T.
Enzyme Protein 48:27-36(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L35317 mRNA. Translation: AAA59356.1.
PIRA54756.
RefSeqNP_113698.1. NM_031510.1.
XP_006245111.1. XM_006245049.1.
UniGeneRn.3561.

3D structure databases

ProteinModelPortalP41562.
SMRP41562. Positions 4-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246640. 1 interaction.
MINTMINT-4565540.

PTM databases

PhosphoSiteP41562.

Proteomic databases

PaxDbP41562.
PRIDEP41562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020322; ENSRNOP00000020322; ENSRNOG00000015020.
GeneID24479.
KEGGrno:24479.
UCSCRGD:2862. rat.

Organism-specific databases

CTD3417.
RGD2862. Idh1.

Phylogenomic databases

eggNOGCOG0538.
GeneTreeENSGT00390000012547.
HOGENOMHOG000019858.
HOVERGENHBG006119.
KOK00031.
OMAKELSFFA.
OrthoDBEOG7QNVKS.
PhylomeDBP41562.

Enzyme and pathway databases

BRENDA1.1.1.42. 5301.

Gene expression databases

GenevestigatorP41562.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603439.
PROP41562.

Entry information

Entry nameIDHC_RAT
AccessionPrimary (citable) accession number: P41562
Secondary accession number(s): P80300
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 106 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