GFRP_RAT
ID GFRP_RAT Reviewed; 84 AA.
AC P70552;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=GTP cyclohydrolase 1 feedback regulatory protein;
DE Short=GFRP;
DE AltName: Full=GTP cyclohydrolase I feedback regulatory protein;
DE AltName: Full=p35;
GN Name=Gchfr; Synonyms=Gfrp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 12-25; 55-62 AND 67-78.
RC TISSUE=Liver;
RX PubMed=8702680; DOI=10.1074/jbc.271.33.19743;
RA Milstien S., Jaffe H., Kowlessur D., Bonner T.I.;
RT "Purification and cloning of the GTP cyclohydrolase I feedback regulatory
RT protein, GFRP.";
RL J. Biol. Chem. 271:19743-19751(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC STRAIN=Wistar;
RX PubMed=9092499; DOI=10.1074/jbc.272.15.9690;
RA Yoneyama T., Brewer J.M., Hatakeyama K.;
RT "GTP cyclohydrolase I feedback regulatory protein is a pentamer of
RT identical subunits. Purification, cDNA cloning, and bacterial expression.";
RL J. Biol. Chem. 272:9690-9696(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=11580249; DOI=10.1006/jmbi.2001.5011;
RA Bader G., Schiffmann S., Herrmann A., Fischer M., Gutlich M., Auerbach G.,
RA Ploom T., Bacher A., Huber R., Lemm T.;
RT "Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein,
RT GFRP.";
RL J. Mol. Biol. 312:1051-1057(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GCH1.
RX PubMed=11818540; DOI=10.1073/pnas.022646999;
RA Maita N., Okada K., Hatakeyama K., Hakoshima T.;
RT "Crystal structure of the stimulatory complex of GTP cyclohydrolase I and
RT its feedback regulatory protein GFRP.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1212-1217(2002).
CC -!- FUNCTION: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase
CC 1. This inhibition is reversed by L-phenylalanine.
CC -!- SUBUNIT: Homopentamer. Forms a complex with GCH1 where a GCH1
CC homodecamer is sandwiched by two GFRP homopentamers. Interacts with
CC GCH1. {ECO:0000269|PubMed:11818540, ECO:0000269|PubMed:9092499}.
CC -!- INTERACTION:
CC P70552; P22288: Gch1; NbExp=3; IntAct=EBI-1032715, EBI-1032708;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus membrane
CC {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Liver and kidney. Somewhat lower level in testis,
CC heart, brain and lung.
CC -!- SIMILARITY: Belongs to the GFRP family. {ECO:0000305}.
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DR EMBL; U53710; AAC52776.1; -; mRNA.
DR EMBL; U85512; AAD09241.1; -; mRNA.
DR EMBL; BC086944; AAH86944.1; -; mRNA.
DR RefSeq; NP_598279.1; NM_133595.2.
DR PDB; 1IS7; X-ray; 2.80 A; K/L/M/N/O/P/Q/R/S/T=1-84.
DR PDB; 1IS8; X-ray; 2.70 A; K/L/M/N/O/P/Q/R/S/T=1-84.
DR PDB; 1JG5; X-ray; 2.60 A; A/B/C/D/E=2-84.
DR PDB; 1WPL; X-ray; 2.80 A; K/L/M/N/O/P/Q/R/S/T=1-84.
DR PDBsum; 1IS7; -.
DR PDBsum; 1IS8; -.
DR PDBsum; 1JG5; -.
DR PDBsum; 1WPL; -.
DR AlphaFoldDB; P70552; -.
DR SMR; P70552; -.
DR BioGRID; 251135; 2.
DR CORUM; P70552; -.
DR IntAct; P70552; 1.
DR STRING; 10116.ENSRNOP00000016458; -.
DR iPTMnet; P70552; -.
DR PhosphoSitePlus; P70552; -.
DR PaxDb; P70552; -.
DR PRIDE; P70552; -.
DR GeneID; 171128; -.
DR KEGG; rno:171128; -.
DR UCSC; RGD:621746; rat.
DR CTD; 2644; -.
DR RGD; 621746; Gchfr.
DR VEuPathDB; HostDB:ENSRNOG00000012290; -.
DR eggNOG; ENOG502S4A0; Eukaryota.
DR HOGENOM; CLU_195651_0_0_1; -.
DR InParanoid; P70552; -.
DR OMA; GQTCIWT; -.
DR OrthoDB; 1560576at2759; -.
DR PhylomeDB; P70552; -.
DR TreeFam; TF329303; -.
DR Reactome; R-RNO-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR EvolutionaryTrace; P70552; -.
DR PRO; PR:P70552; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012290; Expressed in liver and 19 other tissues.
DR Genevisible; P70552; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0042470; C:melanosome; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:RGD.
DR GO; GO:0044549; F:GTP cyclohydrolase binding; IDA:RGD.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0009890; P:negative regulation of biosynthetic process; IEA:InterPro.
DR GO; GO:0043105; P:negative regulation of GTP cyclohydrolase I activity; IDA:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; NAS:RGD.
DR Gene3D; 3.30.1410.10; -; 1.
DR InterPro; IPR036717; GFRP_sf.
DR InterPro; IPR009112; GTP_CycHdrlase_I_reg.
DR PANTHER; PTHR16852; PTHR16852; 1.
DR Pfam; PF06399; GFRP; 1.
DR SUPFAM; SSF69761; SSF69761; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Membrane; Nucleus;
KW Reference proteome.
FT CHAIN 1..84
FT /note="GTP cyclohydrolase 1 feedback regulatory protein"
FT /id="PRO_0000189677"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1JG5"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1IS8"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1JG5"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1JG5"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1JG5"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1JG5"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1JG5"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1JG5"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1JG5"
SQ SEQUENCE 84 AA; 9672 MW; 874EC3B28EC7DDFC CRC64;
MPYLLISTQI RMEVGPTMVG DEHSDPELMQ QLGASKRRVL GNNFYEYYVN DPPRIVLDKL
ECRGFRVLSM TGVGQTLVWC LHKE
