GFRP_MOUSE
ID GFRP_MOUSE Reviewed; 84 AA.
AC P99025; Q8BH29;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Liver;
RA Sanchez J.-C., Rouge V., Frutiger S., Hughes G., Yan J.X., Hoogland C.,
RA Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
RL Submitted (AUG-1998) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase
CC 1. This inhibition is reversed by L-phenylalanine (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homopentamer. Forms a complex with GCH1 where a GCH1
CC homodecamer is sandwiched by two GFRP homopentamers. Interacts with
CC GCH1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus membrane
CC {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GFRP family. {ECO:0000305}.
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DR EMBL; AK028116; BAC25756.1; -; mRNA.
DR EMBL; AK028122; BAC25761.1; -; mRNA.
DR CCDS; CCDS38204.1; -.
DR RefSeq; NP_796131.1; NM_177157.4.
DR AlphaFoldDB; P99025; -.
DR SMR; P99025; -.
DR STRING; 10090.ENSMUSP00000060835; -.
DR iPTMnet; P99025; -.
DR PhosphoSitePlus; P99025; -.
DR SwissPalm; P99025; -.
DR SWISS-2DPAGE; P99025; -.
DR jPOST; P99025; -.
DR PaxDb; P99025; -.
DR PeptideAtlas; P99025; -.
DR PRIDE; P99025; -.
DR ProteomicsDB; 263359; -.
DR Antibodypedia; 23158; 233 antibodies from 30 providers.
DR DNASU; 320415; -.
DR Ensembl; ENSMUST00000057454; ENSMUSP00000060835; ENSMUSG00000046814.
DR GeneID; 320415; -.
DR KEGG; mmu:320415; -.
DR UCSC; uc008ltf.1; mouse.
DR CTD; 2644; -.
DR MGI; MGI:2443977; Gchfr.
DR VEuPathDB; HostDB:ENSMUSG00000046814; -.
DR eggNOG; ENOG502S4A0; Eukaryota.
DR GeneTree; ENSGT00440000033849; -.
DR HOGENOM; CLU_195651_0_0_1; -.
DR InParanoid; P99025; -.
DR OMA; GQTCIWT; -.
DR OrthoDB; 1560576at2759; -.
DR PhylomeDB; P99025; -.
DR TreeFam; TF329303; -.
DR Reactome; R-MMU-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR BioGRID-ORCS; 320415; 0 hits in 68 CRISPR screens.
DR ChiTaRS; Gchfr; mouse.
DR PRO; PR:P99025; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P99025; protein.
DR Bgee; ENSMUSG00000046814; Expressed in right kidney and 123 other tissues.
DR ExpressionAtlas; P99025; baseline and differential.
DR Genevisible; P99025; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0042470; C:melanosome; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI.
DR GO; GO:0044549; F:GTP cyclohydrolase binding; ISO:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0009890; P:negative regulation of biosynthetic process; IEA:InterPro.
DR GO; GO:0043105; P:negative regulation of GTP cyclohydrolase I activity; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
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 Cytoplasm; Direct protein sequencing; Membrane; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..84
FT /note="GTP cyclohydrolase 1 feedback regulatory protein"
FT /id="PRO_0000189676"
SQ SEQUENCE 84 AA; 9584 MW; 553BB3B28EC6F6EB CRC64;
MPYLLISTQI RMEVGPTMVG DEHSDPELMQ HLGASKRSVL GNNFYEYYVN DPPRIVLDKL
ECKGFRVLSM TGVGQTLVWC LHKE
