GTP cyclohydrolase 1 precursor - Mus musculus (Mouse)

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Q05915 (GCH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Catalytic activity	GTP + H₂O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
Enzyme regulation	GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity. Zinc is required for catalytic activity. Inhibited by Mg²⁺.
Pathway	Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
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.
Post-translational modification	Phosphorylated By similarity.
Sequence similarities	Belongs to the GTP cyclohydrolase I family.

Ontologies

Keywords
Biological process	Tetrahydrobiopterin biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7,8-dihydroneopterin 3'-triphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway GTP catabolic process Inferred from electronic annotation. Source: Compara dopamine biosynthetic process Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from electronic annotation. Source: Compara negative regulation of blood pressure Inferred from electronic annotation. Source: Compara neuromuscular process controlling posture Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase activity Inferred from electronic annotation. Source: Compara protein heterooligomerization Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara regulation of lung blood pressure Inferred from mutant phenotype PubMed 15824199. Source: MGI response to interferon-gamma Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to pain Inferred from sequence or structural similarity. Source: UniProtKB response to tumor necrosis factor Inferred from electronic annotation. Source: Compara 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: Compara
Cellular_component	cytoplasmic vesicle Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara nuclear membrane Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	GTP 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: Compara coenzyme binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 11

By similarity

PRO_0000010718

Chain

12 – 241

230

GTP cyclohydrolase 1

PRO_0000010719

Sites

Metal binding

132

Zinc By similarity

Metal binding

135

Zinc By similarity

Metal binding

203

Zinc By similarity

Site

Involved in pterin ring binding By similarity

Site

Involved in pterin ring binding By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Experimental info

Sequence conflict

E → D in AAC60677. Ref.3

Sequence conflict

Q → E in AAC60677. Ref.3

Sequence conflict

235

F → S in AAC60677. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q05915 [UniParc].

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

FASTA

241

27,014

        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' referencesShow '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.
+	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.
IPI	IPI00114691.
PIR	JQ1934.
RefSeq	NP_032128.1. NM_008102.3.
UniGene	Mm.10651.
3D structure databases
ProteinModelPortal	Q05915.
SMR	Q05915. Positions 48-241.
ModBase	Search...
PTM databases
PhosphoSite	Q05915.
Proteomic databases
PaxDb	Q05915.
PRIDE	Q05915.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000089959; ENSMUSP00000087405; ENSMUSG00000037580.
GeneID	14528.
KEGG	mmu:14528.
Organism-specific databases
CTD	2643.
MGI	MGI:95675. Gch1.
Phylogenomic databases
eggNOG	COG0302.
HOGENOM	HOG000221222.
HOVERGEN	HBG003136.
InParanoid	Q05915.
KO	K01495.
OMA	LYSVCEH.
OrthoDB	EOG4FR0SK.
Enzyme and pathway databases
BRENDA	3.5.4.16. 3474.
UniPathway	UPA00848; UER00151.
Gene expression databases
ArrayExpress	Q05915.
Bgee	Q05915.
CleanEx	MM_GCH1.
Genevestigator	Q05915.
GermOnline	ENSMUSG00000037580. Mus musculus.
Family and domain databases
InterPro	IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view]
PANTHER	PTHR11109. PTHR11109. 1 hit.
Pfam	PF01227. GTP_cyclohydroI. 1 hit. [Graphical view]
TIGRFAMs	TIGR00063. folE. 1 hit.
PROSITE	PS00859. GTP_CYCLOHYDROL_1_1. 1 hit. PS00860. GTP_CYCLOHYDROL_1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	286176.
SOURCE	Search...

Entry information

Entry name

GCH1_MOUSE

Accession

Primary (citable) accession number: Q05915

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents