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Q05915 (GCH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
GTP cyclohydrolase 1

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I
Gene names
Name:Gch1
Synonyms:Gch
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May positively regulate nitric oxide synthesis in endothelial cells. May be involved in dopamine synthesis. May modify pain sensitivity and persistence By similarity. HAMAP-Rule MF_00223

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_00223

Enzyme regulation

GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity. Zinc is required for catalytic activity. Inhibited by Mg2+. HAMAP-Rule MF_00223

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_00223

Subunit structure

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

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_00223.

Post-translational modification

Phosphorylated By similarity. HAMAP-Rule MF_00223

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Ontologies

Keywords
   Biological processTetrahydrobiopterin biosynthesis
   Cellular componentCytoplasm
Nucleus
   LigandGTP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7,8-dihydroneopterin 3'-triphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

GTP catabolic process

Inferred from electronic annotation. Source: Ensembl

dopamine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling posture

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from mutant phenotype PubMed 15824199. Source: MGI

regulation of lung blood pressure

Inferred from mutant phenotype PubMed 15824199. Source: MGI

response to interferon-gamma

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to pain

Inferred from sequence or structural similarity. Source: UniProtKB

response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

tetrahydrobiopterin biosynthetic process

Inferred by curator PubMed 7524491. Source: MGI

tetrahydrofolate biosynthetic process

Inferred from electronic annotation. Source: InterPro

vasodilation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP cyclohydrolase I activity

Inferred from direct assay PubMed 7524491. Source: MGI

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

coenzyme binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1111 By similarity
PRO_0000010718
Chain12 – 241230GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000010719

Sites

Metal binding1321Zinc By similarity
Metal binding1351Zinc By similarity
Metal binding2031Zinc By similarity
Site871Involved in pterin ring binding By similarity
Site961Involved in pterin ring binding By similarity

Amino acid modifications

Modified residue511Phosphoserine Ref.4
Modified residue721Phosphoserine By similarity

Experimental info

Sequence conflict541E → D in AAC60677. Ref.3
Sequence conflict561Q → E in AAC60677. Ref.3
Sequence conflict2351F → S in AAC60677. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q05915 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: B4366F102B4A6FE6

FASTA24127,014
        10         20         30         40         50         60 
MEKPRGVRCT NGFSERELPR PGASPPAEKS RPPEAKGAQP ADAWKAGRHR SEEENQVNLP 

        70         80         90        100        110        120 
KLAAAYSSIL LSLGEDPQRQ GLLKTPWRAA TAMQYFTKGY QETISDVLND AIFDEDHDEM 

       130        140        150        160        170        180 
VIVKDIDMFS MCEHHLVPFV GRVHIGYLPN KQVLGLSKLA RIVEIYSRRL QVQERLTKQI 

       190        200        210        220        230        240 
AVAITEALQP AGVGVVIEAT HMCMVMRGVQ KMNSKTVTST MLGVFREDPK TREEFLTLIR 


S 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of cDNA encoding mouse GTP cyclohydrolase I."
Nomura T., Ichinose H., Sumi-Ichinose C., Nomura H., Hagino Y., Fujita K., Nagatsu T.
Biochem. Biophys. Res. Commun. 191:523-527(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon and Mammary gland.
[3]"Detection and quantification of GTP cyclohydrolase I mRNA."
Gutlich M., Schott K., Werner T., Bacher A., Ziegler I.
Adv. Exp. Med. Biol. 338:167-170(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-241.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09737 mRNA. Translation: AAA37757.1.
BC005643 mRNA. Translation: AAH05643.1.
BC069921 mRNA. Translation: AAH69921.1.
S71373 mRNA. Translation: AAC60677.2.
CCDSCCDS26984.1.
PIRJQ1934.
RefSeqNP_032128.1. NM_008102.3.
UniGeneMm.10651.

3D structure databases

ProteinModelPortalQ05915.
SMRQ05915. Positions 48-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199864. 1 interaction.

PTM databases

PhosphoSiteQ05915.

Proteomic databases

MaxQBQ05915.
PaxDbQ05915.
PRIDEQ05915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089959; ENSMUSP00000087405; ENSMUSG00000037580.
GeneID14528.
KEGGmmu:14528.
UCSCuc007tht.1. mouse.

Organism-specific databases

CTD2643.
MGIMGI:95675. Gch1.

Phylogenomic databases

eggNOGCOG0302.
HOGENOMHOG000221222.
HOVERGENHBG003136.
InParanoidQ05915.
KOK01495.
OMAKRTYDEE.
OrthoDBEOG77DJ6T.
PhylomeDBQ05915.
TreeFamTF105616.

Enzyme and pathway databases

BRENDA3.5.4.16. 3474.
UniPathwayUPA00848; UER00151.

Gene expression databases

BgeeQ05915.
CleanExMM_GCH1.
GenevestigatorQ05915.

Family and domain databases

HAMAPMF_00223. FolE.
InterProIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERPTHR11109. PTHR11109. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsTIGR00063. folE. 1 hit.
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286176.
PROQ05915.
SOURCESearch...

Entry information

Entry nameGCH1_MOUSE
AccessionPrimary (citable) accession number: Q05915
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 128 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot