GTP cyclohydrolase 1 precursor - Rattus norvegicus (Rat)

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P22288 (GCH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 108. History...

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

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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 protein level

General annotation (Comments)

Function	May positively regulate nitric oxide synthesis in endothelial cells. May be involved in dopamine synthesis By similarity. May modify pain sensitivity and persistence. Ref.3
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. Ref.4
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Induction	By cytokines such as insulin, interferon-gamma, and phytohemagglutinin in adrenal gland, macrophages, and T-cell respectively.
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	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	dihydrobiopterin metabolic process Inferred from direct assay. Source: RGD induction of apoptosis Inferred from expression pattern. Source: RGD negative regulation of blood pressure Inferred from mutant phenotype. Source: RGD protein heterooligomerization Inferred from direct assay Ref.4. Source: RGD protein homooligomerization Inferred from direct assay. Source: RGD response to pain Inferred from direct assay Ref.3. Source: UniProtKB tetrahydrobiopterin biosynthetic process Traceable author statement. Source: RGD tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: InterPro vasodilation Inferred from mutant phenotype. Source: RGD
Cellular component	protein complex Inferred from direct assay Ref.4. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	GTP binding Inferred from direct assay. Source: RGD GTP cyclohydrolase I activity Inferred from direct assay. Source: RGD GTP-dependent protein binding Inferred from physical interaction. Source: RGD calcium ion binding Inferred from direct assay. Source: RGD coenzyme binding Inferred from direct assay. Source: RGD zinc ion binding Inferred from direct assay Ref.4. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Gchfr	P70552	3	EBI-1032708,EBI-1032715

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 11

PRO_0000010720

Chain

12 – 241

230

GTP cyclohydrolase 1

PRO_0000010721

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

Secondary structure

241

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P22288 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 8226E3319816325B
Show »

FASTA

241

27,057

        10         20         30         40         50         60 
MEKPRGVRCT NGFPERELPR PGASRPAEKS RPPEAKGAQP ADAWKAGRPR SEEDNELNLP 

        70         80         90        100        110        120 
NLAAAYSSIL RSLGEDPQRQ GLLKTPWRAA TAMQFFTKGY 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

[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: 1985963] [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: 7802677] [Abstract] Cited for: PROTEIN SEQUENCE OF 37-46 AND 99-116.
[3]	"GTP cyclohydrolase and tetrahydrobiopterin regulate pain sensitivity and persistence." Tegeder I., Costigan M., Griffin R.S., Abele A., Belfer I., Schmidt H., Ehnert C., Nejim J., Marian C., Scholz J., Wu T., Allchorne A., Diatchenko L., Binshtok A.M., Goldman D., Adolph J., Sama S., Atlas S.J. Woolf C.J. Nat. Med. 12:1269-1277(2006) [PubMed: 17057711] [Abstract] 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: 11818540] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 12-241 IN COMPLEX WITH GFRP, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M58364 mRNA. Translation: AAA41299.1.

IPI

IPI00205214.

PIR

A39080.

RefSeq

NP_077332.1. NM_024356.1.

UniGene

Rn.28195.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P22288.

SMR

P22288. Positions 48-241.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22288. 1 interaction.

STRING

P22288.

PTM databases

PhosphoSite

P22288.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

29244.

KEGG

rno:29244.

Organism-specific databases

CTD

2643.

RGD

61992. Gch1.

Phylogenomic databases

eggNOG

roNOG16997.

GeneTree

ENSGT00390000013481.

HOVERGEN

HBG003136.

InParanoid

P22288.

OrthoDB

EOG4FR0SK.

PhylomeDB

P22288.

Gene expression databases

ArrayExpress

P22288.

Genevestigator

P22288.

GermOnline

ENSRNOG00000011039. Rattus norvegicus.

Family and domain databases

InterPro

IPR001474. GTP_CycHdrlase_I.
IPR020602. GTP_CycHdrlase_I/CN_OxRdtase.
IPR018234. GTP_CycHdrlase_I_CS.
[Graphical view]

K01495.

PANTHER

PTHR11109. GTP_cyclohydro_I. 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

608526.

Entry information

Entry name

GCH1_RAT

Accession

Primary (citable) accession number: P22288

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	November 16, 2011
This is version 108 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents