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P22288

- GCH1_RAT

UniProt

P22288 - GCH1_RAT

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Protein

GTP cyclohydrolase 1

Gene

Gch1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

ExpressionAtlasiP22288. baseline and differential.
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 – 7322Combined sources
Turni80 – 845Combined sources
Helixi85 – 9612Combined sources
Helixi98 – 1014Combined sources
Helixi105 – 1084Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi121 – 13212Combined sources
Turni133 – 1353Combined sources
Beta strandi138 – 14811Combined sources
Beta strandi150 – 1545Combined sources
Helixi156 – 16712Combined sources
Beta strandi168 – 1714Combined sources
Helixi173 – 18816Combined sources
Beta strandi191 – 20111Combined sources
Helixi202 – 2054Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi215 – 2239Combined sources
Helixi224 – 2274Combined sources
Helixi229 – 23911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MEKPRGVRCT NGFPERELPR PGASRPAEKS RPPEAKGAQP ADAWKAGRPR
60 70 80 90 100
SEEDNELNLP NLAAAYSSIL RSLGEDPQRQ GLLKTPWRAA TAMQFFTKGY
110 120 130 140 150
QETISDVLND AIFDEDHDEM VIVKDIDMFS MCEHHLVPFV GRVHIGYLPN
160 170 180 190 200
KQVLGLSKLA RIVEIYSRRL QVQERLTKQI AVAITEALQP AGVGVVIEAT
210 220 230 240
HMCMVMRGVQ KMNSKTVTST MLGVFREDPK TREEFLTLIR S
Length:241
Mass (Da):27,057
Last modified:August 1, 1991 - v1
Checksum:i8226E3319816325B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

ExpressionAtlasi P22288. baseline and differential.
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: November 26, 2014
This is version 130 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