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P41562

- IDHC_RAT

UniProt

P41562 - IDHC_RAT

Protein

Isocitrate dehydrogenase [NADP] cytoplasmic

Gene

Idh1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771SubstrateBy similarity
    Binding sitei82 – 821NADPBy similarity
    Binding sitei109 – 1091SubstrateBy similarity
    Binding sitei132 – 1321SubstrateBy similarity
    Sitei139 – 1391Critical for catalysisBy similarity
    Sitei212 – 2121Critical for catalysisBy similarity
    Metal bindingi252 – 2521Magnesium or manganeseBy similarity
    Binding sitei260 – 2601NADPBy similarity
    Metal bindingi275 – 2751Magnesium or manganeseBy similarity
    Binding sitei328 – 3281NADP; via amide nitrogen and carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi75 – 773NADPBy similarity
    Nucleotide bindingi310 – 3156NADPBy similarity

    GO - Molecular functioni

    1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. NAD binding Source: InterPro
    4. NADP binding Source: RGD

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. female gonad development Source: RGD
    3. glutathione metabolic process Source: Ensembl
    4. glyoxylate cycle Source: UniProtKB-KW
    5. isocitrate metabolic process Source: UniProtKB
    6. response to organic cyclic compound Source: RGD
    7. response to oxidative stress Source: Ensembl
    8. response to steroid hormone Source: RGD
    9. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.42. 5301.
    ReactomeiREACT_196228. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NADP] cytoplasmic (EC:1.1.1.42)
    Short name:
    IDH
    Alternative name(s):
    Cytosolic NADP-isocitrate dehydrogenase
    IDP
    NADP(+)-specific ICDH
    Oxalosuccinate decarboxylase
    Gene namesi
    Name:Idh1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 9

    Organism-specific databases

    RGDi2862. Idh1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. mitochondrion Source: Ensembl
    3. peroxisome Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 414413Isocitrate dehydrogenase [NADP] cytoplasmicPRO_0000083580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei81 – 811N6-acetyllysineBy similarity
    Modified residuei126 – 1261N6-succinyllysineBy similarity
    Modified residuei224 – 2241N6-acetyllysineBy similarity
    Modified residuei233 – 2331N6-acetyllysineBy similarity
    Modified residuei243 – 2431N6-acetyllysineBy similarity
    Modified residuei321 – 3211N6-acetyllysineBy similarity
    Modified residuei400 – 4001N6-succinyllysineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.
    Acetylation at Lys-374 dramatically reduces catalytic activity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP41562.
    PRIDEiP41562.

    PTM databases

    PhosphoSiteiP41562.

    Expressioni

    Tissue specificityi

    Ovary, mammary gland and liver.

    Gene expression databases

    GenevestigatoriP41562.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi246640. 1 interaction.
    MINTiMINT-4565540.

    Structurei

    3D structure databases

    ProteinModelPortaliP41562.
    SMRiP41562. Positions 4-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 1007Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0538.
    GeneTreeiENSGT00390000012547.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    KOiK00031.
    OMAiSCGGVAM.
    OrthoDBiEOG7QNVKS.
    PhylomeDBiP41562.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11822. PTHR11822. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000108. IDH_NADP. 1 hit.
    TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P41562-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRKIHGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD    50
    ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR 100
    NILGGTVFRE AIICKNIPRL VTGWVKPIII GRHAYGDQYR ATDFVVPGPG 150
    KVEITYTPKD GSQKVTYLVH DFEEGGGVAM GMYNQDKSIE DFAHSSFQMA 200
    LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSKFE AQKIWYEHRL 250
    IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG 300
    KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT 350
    ELSFFANALE EVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK 400
    LGENLKAKLA QAKL 414
    Length:414
    Mass (Da):46,734
    Last modified:November 1, 1995 - v1
    Checksum:iCF69EE8746DC1AF6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35317 mRNA. Translation: AAA59356.1.
    PIRiA54756.
    RefSeqiNP_113698.1. NM_031510.1.
    XP_006245111.1. XM_006245049.1.
    UniGeneiRn.3561.

    Genome annotation databases

    EnsembliENSRNOT00000020322; ENSRNOP00000020322; ENSRNOG00000015020.
    GeneIDi24479.
    KEGGirno:24479.
    UCSCiRGD:2862. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35317 mRNA. Translation: AAA59356.1 .
    PIRi A54756.
    RefSeqi NP_113698.1. NM_031510.1.
    XP_006245111.1. XM_006245049.1.
    UniGenei Rn.3561.

    3D structure databases

    ProteinModelPortali P41562.
    SMRi P41562. Positions 4-413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246640. 1 interaction.
    MINTi MINT-4565540.

    PTM databases

    PhosphoSitei P41562.

    Proteomic databases

    PaxDbi P41562.
    PRIDEi P41562.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000020322 ; ENSRNOP00000020322 ; ENSRNOG00000015020 .
    GeneIDi 24479.
    KEGGi rno:24479.
    UCSCi RGD:2862. rat.

    Organism-specific databases

    CTDi 3417.
    RGDi 2862. Idh1.

    Phylogenomic databases

    eggNOGi COG0538.
    GeneTreei ENSGT00390000012547.
    HOGENOMi HOG000019858.
    HOVERGENi HBG006119.
    KOi K00031.
    OMAi SCGGVAM.
    OrthoDBi EOG7QNVKS.
    PhylomeDBi P41562.

    Enzyme and pathway databases

    BRENDAi 1.1.1.42. 5301.
    Reactomei REACT_196228. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.

    Miscellaneous databases

    NextBioi 603439.
    PROi P41562.

    Gene expression databases

    Genevestigatori P41562.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view ]
    PANTHERi PTHR11822. PTHR11822. 1 hit.
    Pfami PF00180. Iso_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000108. IDH_NADP. 1 hit.
    TIGRFAMsi TIGR00127. nadp_idh_euk. 1 hit.
    PROSITEi PS00470. IDH_IMDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiIDHC_RAT
    AccessioniPrimary (citable) accession number: P41562
    Secondary accession number(s): P80300
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3