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P22288

- GCH1_RAT

UniProt

P22288 - GCH1_RAT

Protein

GTP cyclohydrolase 1

Gene

Gch1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    May positively regulate nitric oxide synthesis in endothelial cells. May be involved in dopamine synthesis By similarity. May modify pain sensitivity and persistence.By similarity1 Publication

    Catalytic activityi

    GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.

    Enzyme regulationi

    GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity. Zinc is required for catalytic activity. Inhibited by Mg2+.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei87 – 871Involved in pterin ring bindingBy similarity
    Sitei96 – 961Involved in pterin ring bindingBy similarity
    Metal bindingi132 – 1321ZincBy similarity
    Metal bindingi135 – 1351ZincBy similarity
    Metal bindingi203 – 2031ZincBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: RGD
    2. coenzyme binding Source: RGD
    3. GTP binding Source: RGD
    4. GTP cyclohydrolase I activity Source: RGD
    5. GTP-dependent protein binding Source: RGD
    6. protein binding Source: IntAct
    7. zinc ion binding Source: RGD

    GO - Biological processi

    1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. dihydrobiopterin metabolic process Source: RGD
    3. dopamine biosynthetic process Source: Ensembl
    4. GTP catabolic process Source: Ensembl
    5. negative regulation of blood pressure Source: RGD
    6. neuromuscular process controlling posture Source: Ensembl
    7. positive regulation of nitric-oxide synthase activity Source: Ensembl
    8. protein complex assembly Source: RGD
    9. protein heterooligomerization Source: RGD
    10. protein homooligomerization Source: RGD
    11. regulation of lung blood pressure Source: Ensembl
    12. response to interferon-gamma Source: Ensembl
    13. response to lipopolysaccharide Source: Ensembl
    14. response to pain Source: UniProtKB
    15. response to tumor necrosis factor Source: Ensembl
    16. tetrahydrobiopterin biosynthetic process Source: RGD
    17. tetrahydrofolate biosynthetic process Source: InterPro
    18. vasodilation Source: RGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Tetrahydrobiopterin biosynthesis

    Keywords - Ligandi

    GTP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199128. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    UniPathwayiUPA00848; UER00151.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP cyclohydrolase 1 (EC:3.5.4.16)
    Alternative name(s):
    GTP cyclohydrolase I
    Short name:
    GTP-CH-I
    Gene namesi
    Name:Gch1
    Synonyms:Gch
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi61992. Gch1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasmic vesicle Source: Ensembl
    2. cytosol Source: Ensembl
    3. nuclear membrane Source: Ensembl
    4. protein complex Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1111PRO_0000010720Add
    BLAST
    Chaini12 – 241230GTP cyclohydrolase 1PRO_0000010721Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511PhosphoserineBy similarity
    Modified residuei72 – 721PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP22288.

    PTM databases

    PhosphoSiteiP22288.

    Expressioni

    Inductioni

    By cytokines such as insulin, interferon-gamma, and phytohemagglutinin in adrenal gland, macrophages, and T-cell respectively.

    Gene expression databases

    ArrayExpressiP22288.
    GenevestigatoriP22288.

    Interactioni

    Subunit structurei

    Toroid-shaped homodecamer, composed of two pentamers of five dimers. Interacts with AHSA1 and GCHFR/GFRP.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GchfrP705523EBI-1032708,EBI-1032715

    Protein-protein interaction databases

    BioGridi247920. 2 interactions.
    IntActiP22288. 1 interaction.
    STRINGi10116.ENSRNOP00000014821.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi52 – 7322
    Turni80 – 845
    Helixi85 – 9612
    Helixi98 – 1014
    Helixi105 – 1084
    Beta strandi109 – 1113
    Beta strandi112 – 1176
    Beta strandi121 – 13212
    Turni133 – 1353
    Beta strandi138 – 14811
    Beta strandi150 – 1545
    Helixi156 – 16712
    Beta strandi168 – 1714
    Helixi173 – 18816
    Beta strandi191 – 20111
    Helixi202 – 2054
    Beta strandi207 – 2104
    Beta strandi215 – 2239
    Helixi224 – 2274
    Helixi229 – 23911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IS7X-ray2.80A/B/C/D/E/F/G/H/I/J12-241[»]
    1IS8X-ray2.70A/B/C/D/E/F/G/H/I/J12-241[»]
    1WPLX-ray2.80A/B/C/D/E/F/G/H/I/J12-241[»]
    ProteinModelPortaliP22288.
    SMRiP22288. Positions 48-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22288.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTP cyclohydrolase I family.Curated

    Phylogenomic databases

    eggNOGiCOG0302.
    GeneTreeiENSGT00390000013481.
    HOGENOMiHOG000221222.
    HOVERGENiHBG003136.
    InParanoidiP22288.
    KOiK01495.
    OMAiVYSHCEH.
    OrthoDBiEOG77DJ6T.
    PhylomeDBiP22288.

    Family and domain databases

    HAMAPiMF_00223. FolE.
    InterProiIPR001474. GTP_CycHdrlase_I.
    IPR018234. GTP_CycHdrlase_I_CS.
    IPR020602. GTP_CycHdrlase_I_dom.
    [Graphical view]
    PANTHERiPTHR11109. PTHR11109. 1 hit.
    PfamiPF01227. GTP_cyclohydroI. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00063. folE. 1 hit.
    PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P22288-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKPRGVRCT NGFPERELPR PGASRPAEKS RPPEAKGAQP ADAWKAGRPR    50
    SEEDNELNLP NLAAAYSSIL RSLGEDPQRQ GLLKTPWRAA TAMQFFTKGY 100
    QETISDVLND AIFDEDHDEM VIVKDIDMFS MCEHHLVPFV GRVHIGYLPN 150
    KQVLGLSKLA RIVEIYSRRL QVQERLTKQI AVAITEALQP AGVGVVIEAT 200
    HMCMVMRGVQ KMNSKTVTST MLGVFREDPK TREEFLTLIR S 241
    Length:241
    Mass (Da):27,057
    Last modified:August 1, 1991 - v1
    Checksum:i8226E3319816325B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58364 mRNA. Translation: AAA41299.1.
    PIRiA39080.
    RefSeqiNP_077332.1. NM_024356.1.
    UniGeneiRn.28195.

    Genome annotation databases

    EnsembliENSRNOT00000014821; ENSRNOP00000014821; ENSRNOG00000011039.
    GeneIDi29244.
    KEGGirno:29244.
    UCSCiRGD:61992. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58364 mRNA. Translation: AAA41299.1 .
    PIRi A39080.
    RefSeqi NP_077332.1. NM_024356.1.
    UniGenei Rn.28195.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IS7 X-ray 2.80 A/B/C/D/E/F/G/H/I/J 12-241 [» ]
    1IS8 X-ray 2.70 A/B/C/D/E/F/G/H/I/J 12-241 [» ]
    1WPL X-ray 2.80 A/B/C/D/E/F/G/H/I/J 12-241 [» ]
    ProteinModelPortali P22288.
    SMRi P22288. Positions 48-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247920. 2 interactions.
    IntActi P22288. 1 interaction.
    STRINGi 10116.ENSRNOP00000014821.

    PTM databases

    PhosphoSitei P22288.

    Proteomic databases

    PRIDEi P22288.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014821 ; ENSRNOP00000014821 ; ENSRNOG00000011039 .
    GeneIDi 29244.
    KEGGi rno:29244.
    UCSCi RGD:61992. rat.

    Organism-specific databases

    CTDi 2643.
    RGDi 61992. Gch1.

    Phylogenomic databases

    eggNOGi COG0302.
    GeneTreei ENSGT00390000013481.
    HOGENOMi HOG000221222.
    HOVERGENi HBG003136.
    InParanoidi P22288.
    KOi K01495.
    OMAi VYSHCEH.
    OrthoDBi EOG77DJ6T.
    PhylomeDBi P22288.

    Enzyme and pathway databases

    UniPathwayi UPA00848 ; UER00151 .
    Reactomei REACT_199128. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

    Miscellaneous databases

    EvolutionaryTracei P22288.
    NextBioi 608526.
    PROi P22288.

    Gene expression databases

    ArrayExpressi P22288.
    Genevestigatori P22288.

    Family and domain databases

    HAMAPi MF_00223. FolE.
    InterProi IPR001474. GTP_CycHdrlase_I.
    IPR018234. GTP_CycHdrlase_I_CS.
    IPR020602. GTP_CycHdrlase_I_dom.
    [Graphical view ]
    PANTHERi PTHR11109. PTHR11109. 1 hit.
    Pfami PF01227. GTP_cyclohydroI. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00063. folE. 1 hit.
    PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
    PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of cDNA encoding rat GTP cyclohydrolase I. The first enzyme of the tetrahydrobiopterin biosynthetic pathway."
      Hatakeyama K., Inoue Y., Harada T., Kagamiyama H.
      J. Biol. Chem. 266:765-769(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Wistar.
      Tissue: Liver.
    2. "Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells."
      Imazumi K., Sasaki T., Takahashi K., Takai Y.
      Biochem. Biophys. Res. Commun. 205:1409-1416(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 37-46 AND 99-116.
    3. Cited for: FUNCTION.
    4. "Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP."
      Maita N., Okada K., Hatakeyama K., Hakoshima T.
      Proc. Natl. Acad. Sci. U.S.A. 99:1212-1217(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 12-241 IN COMPLEX WITH GFRP, SUBUNIT.

    Entry informationi

    Entry nameiGCH1_RAT
    AccessioniPrimary (citable) accession number: P22288
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 128 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

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3