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GTP cyclohydrolase 1 (EC 3.5.4.16) (GTP cyclohydrolase I) (GTP-CH-I)

 GCH1_HUMAN              Reviewed;         250 AA.
P30793; Q6FHY7; Q9Y4I8;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
27-SEP-2017, entry version 188.
RecName: Full=GTP cyclohydrolase 1;
EC=3.5.4.16 {ECO:0000269|PubMed:16778797, ECO:0000269|PubMed:2463916, ECO:0000269|PubMed:3753653};
AltName: Full=GTP cyclohydrolase I;
Short=GTP-CH-I;
Name=GCH1; Synonyms=DYT5, GCH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GCH-1; GCH-2 AND GCH-3).
TISSUE=Liver;
PubMed=1520321; DOI=10.1016/S0006-291X(05)81501-3;
Togari A., Ichinose H., Matsumoto S., Fujita K., Nagatsu T.;
"Multiple mRNA forms of human GTP cyclohydrolase I.";
Biochem. Biophys. Res. Commun. 187:359-365(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GCH-1 AND GCH-2), AND FUNCTION.
TISSUE=Liver;
PubMed=8068008; DOI=10.1042/bj3020215;
Guetlich M., Jaeger E., Rucknaegel K.P., Werner T., Roedl W.,
Ziegler I., Bacher A.;
"Human GTP cyclohydrolase I: only one out of three cDNA isoforms gives
rise to the active enzyme.";
Biochem. J. 302:215-221(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pheochromocytoma;
PubMed=8695054; DOI=10.1007/BF01271561;
Nomura T., Ohtsuki M., Matsui S., Sumi-Ichinose C., Nomura H.,
Hagino Y., Iwase K., Ichinose H., Fujita K., Nagatsu T.;
"Isolation of a full-length cDNA clone for human GTP cyclohydrolase I
type 1 from pheochromocytoma.";
J. Neural Transm. 101:237-242(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GCH-1 AND GCH-4).
TISSUE=Myelomonocyte;
PubMed=11284739; DOI=10.1042/0264-6021:3550499;
Golderer G., Werner E.R., Heufler C., Strohmaier W., Grobner P.,
Werner-Felmayer G.;
"GTP cyclohydrolase I mRNA: novel splice variants in the slime mould
Physarum polycephalum and in human monocytes (THP-1) indicate
conservation of mRNA processing.";
Biochem. J. 355:499-507(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GCH-1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GCH-1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
TISSUE=Granulocyte;
PubMed=8666288; DOI=10.1016/0378-1119(95)00886-1;
Witter K., Werner T., Blusch J.H., Schneider E.-M., Riess O.,
Ziegler I., Roedl W., Bacher A., Guetlich M.;
"Cloning, sequencing and functional studies of the gene encoding human
GTP cyclohydrolase I.";
Gene 171:285-290(1996).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 60-242.
PubMed=1482676;
Guetlich M., Schott K., Werner T., Bacher A., Ziegler I.;
"Species and tissue specificity of mammalian GTP cyclohydrolase I
messenger RNA.";
Biochim. Biophys. Acta 1171:133-140(1992).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-209.
PubMed=7730309; DOI=10.1074/jbc.270.17.10062;
Ichinose H., Ohye T., Matsuda Y., Hori T.A., Blau N., Burlina A.,
Rouse B., Matalon R., Fujita K., Nagatsu T.;
"Characterization of mouse and human GTP cyclohydrolase I genes.
Mutations in patients with GTP cyclohydrolase I deficiency.";
J. Biol. Chem. 270:10062-10071(1995).
[11]
ENZYME ACTIVITY, AND ENZYME REGULATION.
PubMed=3753653; DOI=10.1016/0304-4165(86)90115-7;
Blau N., Niederwieser A.;
"The application of 8-aminoguanosine triphosphate, a new inhibitor of
GTP cyclohydrolase I, to the purification of the enzyme from human
liver.";
Biochim. Biophys. Acta 880:26-31(1986).
[12]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=2500984; DOI=10.1016/0300-9084(89)90006-0;
Shen R.-S., Alam A., Zhang Y.X.;
"Human liver GTP cyclohydrolase I: purification and some properties.";
Biochimie 71:343-349(1989).
[13]
ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=2463916; DOI=10.1111/j.1432-1033.1989.tb14491.x;
Schoedon G., Redweik U., Curtius H.-C.;
"Purification of GTP cyclohydrolase I from human liver and production
of specific monoclonal antibodies.";
Eur. J. Biochem. 178:627-634(1989).
[14]
INDUCTION.
PubMed=7678411;
Werner-Felmayer G., Werner E.R., Fuchs D., Hausen A., Reibnegger G.,
Schmidt K., Weiss G., Wachter H.;
"Pteridine biosynthesis in human endothelial cells. Impact on nitric
oxide-mediated formation of cyclic GMP.";
J. Biol. Chem. 268:1842-1846(1993).
[15]
REVIEW ON VARIANTS.
PubMed=9222755;
DOI=10.1002/(SICI)1098-1004(1997)10:1<11::AID-HUMU2>3.0.CO;2-P;
Thoeny B., Blau N.;
"Mutations in the GTP cyclohydrolase I and 6-pyruvoyl-tetrahydropterin
synthase genes.";
Hum. Mutat. 10:11-20(1997).
[16]
FUNCTION, AND INDUCTION.
PubMed=9445252; DOI=10.1161/01.ATV.18.1.27;
Katusic Z.S., Stelter A., Milstien S.;
"Cytokines stimulate GTP cyclohydrolase I gene expression in cultured
human umbilical vein endothelial cells.";
Arterioscler. Thromb. Vasc. Biol. 18:27-32(1998).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12176133; DOI=10.1016/S0008-6363(02)00460-1;
Cai S., Alp N.J., McDonald D., Smith I., Kay J., Canevari L.,
Heales S., Channon K.M.;
"GTP cyclohydrolase I gene transfer augments intracellular
tetrahydrobiopterin in human endothelial cells: effects on nitric
oxide synthase activity, protein levels and dimerisation.";
Cardiovasc. Res. 55:838-849(2002).
[18]
INDUCTION.
PubMed=12002810; DOI=10.1016/S0024-3205(02)01503-5;
Ohtsuki M., Shiraishi H., Kato T., Kuroda R., Tazawa M.,
Sumi-Ichinose C., Tada S., Udagawa Y., Itoh M., Hishida H.,
Ichinose H., Nagatsu T., Hagino Y., Nomura T.;
"cAMP inhibits cytokine-induced biosynthesis of tetrahydrobiopterin in
human umbilical vein endothelial cells.";
Life Sci. 70:2187-2198(2002).
[19]
INDUCTION.
PubMed=12607127; DOI=10.1007/s00395-003-0394-y;
Gesierich A., Niroomand F., Tiefenbacher C.P.;
"Role of human GTP cyclohydrolase I and its regulatory protein in
tetrahydrobiopterin metabolism.";
Basic Res. Cardiol. 98:69-75(2003).
[20]
INDUCTION.
PubMed=14646243; DOI=10.1254/jphs.93.265;
Shiraishi H., Kato T., Atsuta K., Sumi-Ichinose C., Ohtsuki M.,
Itoh M., Hishida H., Tada S., Udagawa Y., Nagatsu T., Hagino Y.,
Ichinose H., Nomura T.;
"cGMP inhibits GTP cyclohydrolase I activity and biosynthesis of
tetrahydrobiopterin in human umbilical vein endothelial cells.";
J. Pharmacol. Sci. 93:265-271(2003).
[21]
ENZYME REGULATION.
PubMed=14717702; DOI=10.1046/j.1432-1033.2003.03933.x;
Suzuki T., Kurita H., Ichinose H.;
"GTP cyclohydrolase I utilizes metal-free GTP as its substrate.";
Eur. J. Biochem. 271:349-355(2004).
[22]
FUNCTION.
PubMed=16338639; DOI=10.1016/j.brainresprot.2005.10.005;
Duan C.-L., Su Y., Zhao C.-L., Lu L.-L., Xu Q.-Y., Yang H.;
"The assays of activities and function of TH, AADC, and GCH1 and their
potential use in ex vivo gene therapy of PD.";
Brain Res. Brain Res. Protoc. 16:37-43(2005).
[23]
INDUCTION.
PubMed=15604419; DOI=10.1161/01.RES.0000153669.24827.DF;
Huang A., Zhang Y.-Y., Chen K., Hatakeyama K., Keaney J.F. Jr.;
"Cytokine-stimulated GTP cyclohydrolase I expression in endothelial
cells requires coordinated activation of nuclear factor-kappaB and
Stat1/Stat3.";
Circ. Res. 96:164-171(2005).
[24]
INDUCTION.
PubMed=15649650; DOI=10.1016/j.freeradbiomed.2004.11.004;
Kalivendi S., Hatakeyama K., Whitsett J., Konorev E., Kalyanaraman B.,
Vasquez-Vivar J.;
"Changes in tetrahydrobiopterin levels in endothelial cells and adult
cardiomyocytes induced by LPS and hydrogen peroxide -- a role for
GFRP?";
Free Radic. Biol. Med. 38:481-491(2005).
[25]
SUBUNIT.
PubMed=16848765; DOI=10.1042/BJ20060765;
Pandya M.J., Golderer G., Werner E.R., Werner-Felmayer G.;
"Interaction of human GTP cyclohydrolase I with its splice variants.";
Biochem. J. 400:75-80(2006).
[26]
ENZYME ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=16778797; DOI=10.1038/sj.jid.5700425;
Chavan B., Gillbro J.M., Rokos H., Schallreuter K.U.;
"GTP cyclohydrolase feedback regulatory protein controls cofactor 6-
tetrahydrobiopterin synthesis in the cytosol and in the nucleus of
epidermal keratinocytes and melanocytes.";
J. Invest. Dermatol. 126:2481-2489(2006).
[27]
INTERACTION WITH AHSA1 AND GCHFR.
PubMed=16696853; DOI=10.1111/j.1471-4159.2006.03836.x;
Swick L., Kapatos G.;
"A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein
interactions.";
J. Neurochem. 97:1447-1455(2006).
[28]
FUNCTION.
PubMed=17057711; DOI=10.1038/nm1490;
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., Carlezon W.A., Parsegian A., Loetsch J.,
Fillingim R.B., Maixner W., Geisslinger G., Max M.B., Woolf C.J.;
"GTP cyclohydrolase and tetrahydrobiopterin regulate pain sensitivity
and persistence.";
Nat. Med. 12:1269-1277(2006).
[29]
PHOSPHORYLATION AT SER-81.
PubMed=17704208; DOI=10.1161/CIRCRESAHA.107.153809;
Widder J.D., Chen W., Li L., Dikalov S., Thony B., Hatakeyama K.,
Harrison D.G.;
"Regulation of tetrahydrobiopterin biosynthesis by shear stress.";
Circ. Res. 101:830-838(2007).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[31]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 55-250, SUBUNIT, AND
ZINC-BINDING SITES.
PubMed=11087827; DOI=10.1073/pnas.240463497;
Auerbach G., Herrmann A., Bracher A., Bader G., Gutlich M.,
Fischer M., Neukamm M., Garrido-Franco M., Richardson J., Nar H.,
Huber R., Bacher A.;
"Zinc plays a key role in human and bacterial GTP cyclohydrolase I.";
Proc. Natl. Acad. Sci. U.S.A. 97:13567-13572(2000).
[32]
VARIANTS DRD TRP-88; VAL-134 AND GLU-201.
PubMed=7874165; DOI=10.1038/ng1194-236;
Ichinose H., Ohye T., Takahashi E., Seki N., Hori T., Segawa M.,
Nomura Y., Endo K., Tanaka H., Tsuji S., Fujita K., Nagatsu T.;
"Hereditary progressive dystonia with marked diurnal fluctuation
caused by mutations in the GTP cyclohydrolase I gene.";
Nat. Genet. 8:236-242(1994).
[33]
VARIANT DRD PRO-79, AND VARIANTS HPABH4B HIS-184 AND ILE-211.
PubMed=7501255; DOI=10.1016/0304-3940(95)11820-M;
Ichinose H., Ohye T., Segawa M., Nomura Y., Endo K., Tanaka H.,
Tsuji S., Fujita K., Nagatsu T.;
"GTP cyclohydrolase I gene in hereditary progressive dystonia with
marked diurnal fluctuation.";
Neurosci. Lett. 196:5-8(1995).
[34]
VARIANT DRD PRO-144.
PubMed=8957022; DOI=10.1002/ana.410400517;
Hirano M., Tamaru Y., Ito H., Matsumoto S., Imai T., Ueno S.;
"Mutant GTP cyclohydrolase I mRNA levels contribute to dopa-responsive
dystonia onset.";
Ann. Neurol. 40:796-798(1996).
[35]
VARIANTS DRD PRO-88; PRO-153; ARG-203; ARG-224 AND SER-234.
PubMed=8852666; DOI=10.1093/hmg/5.3.403;
Bandmann O., Nygaard T.G., Surtess R., Mardsen C.D., Wood N.W.,
Harding A.E.;
"Dopa-responsive dystonia in British patients: new mutations of the
GTP-cyclohydrolase I gene and evidence for genetic heterogeneity.";
Hum. Mol. Genet. 5:403-406(1996).
[36]
VARIANT DRD SER-178.
PubMed=9120469; DOI=10.1136/jnnp.62.4.420;
Beyer K., Lao-Villadoniga J.I., Vecino-Bilbao B., Cacabelos R.,
de la Fuent-Fernandez R.;
"A novel point mutation in the GTP cyclohydrolase I gene in a Spanish
family with hereditary progressive and dopa responsive dystonia.";
J. Neurol. Neurosurg. Psych. 62:420-421(1997).
[37]
VARIANTS DRD LEU-23 AND ASN-115.
PubMed=9328244; DOI=10.1136/jnnp.63.3.304;
Jarman P.R., Bandmann O., Marsden C.D., Wood N.W.;
"GTP cyclohydrolase I mutations in patients with dystonia responsive
to anticholinergic drugs.";
J. Neurol. Neurosurg. Psych. 63:304-308(1997).
[38]
VARIANTS HPABH4B ASP-108; THR-221 AND ARG-224.
PubMed=9667588; DOI=10.1002/ana.410440107;
Furukawa Y., Kish S.J., Bebin E.M., Jacobson R.D., Fryburg J.S.,
Wilson W.G., Shimadzu M., Hyland K., Trugman J.M.;
"Dystonia with motor delay in compound heterozygotes for GTP-
cyclohydrolase I gene mutations.";
Ann. Neurol. 44:10-16(1998).
[39]
VARIANTS DRD GLN-71; VAL-74; ALA-83; ILE-191; VAL-211 AND TRP-241.
PubMed=9778264; DOI=10.1002/ana.410440411;
Bandmann O., Valente E.M., Holmans P., Surtees R.A., Walters J.H.,
Wevers R.A., Marsden C.D., Wood N.W.;
"Dopa-responsive dystonia: a clinical and molecular genetic study.";
Ann. Neurol. 44:649-656(1998).
[40]
VARIANT DRD SER-249.
PubMed=10987649; DOI=10.1007/s004390051093;
Hwu W.-L., Wang P.-J., Hsiao K.-J., Wang T.-R., Chiou Y.-W.,
Lee Y.-M.;
"Dopa-responsive dystonia induced by a recessive GTP cyclohydrolase I
mutation.";
Hum. Genet. 105:226-230(1999).
[41]
VARIANTS DRD ARG-102; LYS-102; ARG-141; TRP-141; THR-176; SER-178 AND
LYS-186.
PubMed=10582612; DOI=10.1046/j.1471-4159.1999.0732510.x;
Suzuki T., Ohye T., Inagaki H., Nagatsu T., Ichinose H.;
"Characterization of wild-type and mutants of recombinant human GTP
cyclohydrolase I: relationship to etiology of dopa-responsive
dystonia.";
J. Neurochem. 73:2510-2516(1999).
[42]
VARIANT DRD LYS-135.
PubMed=10208576; DOI=10.1097/00001756-199902250-00008;
Brique S., Destee A., Lambert J.-C., Mouroux V., Delacourte A.,
Amouyel P., Chartier-Harlin M.-C.;
"A new GTP-cyclohydrolase I mutation in an unusual dopa-responsive
dystonia, familial form.";
NeuroReport 10:487-491(1999).
[43]
VARIANT DRD VAL-90.
PubMed=10076897; DOI=10.1016/S0304-3940(98)00984-7;
Hirano M., Komure O., Ueno S.;
"A novel missense mutant inactivates GTP cyclohydrolase I in dopa-
responsive dystonia.";
Neurosci. Lett. 260:181-184(1999).
[44]
VARIANTS DRD ALA-83; 88-ARG-GLN-89 DEL; SER-178; ARG-180; LEU-199 AND
GLU-201.
PubMed=10825351; DOI=10.1093/brain/123.6.1112;
Tassin J., Duerr A., Bonnet A.-M., Gil R., Vidailhet M.,
Luecking C.B., Goas J.-Y., Durif F., Abada M., Echenne B., Motte J.,
Lagueny A., Lacomblez L., Jedynak P., Bartholome B., Agid Y.,
Brice A.;
"Levodopa-responsive dystonia. GTP cyclohydrolase I or parkin
mutations?";
Brain 123:1112-1121(2000).
[45]
VARIANTS DRD ARG-163 AND VAL-213.
PubMed=11113234; DOI=10.1212/WNL.55.11.1735;
Steinberger D., Korinthenberg R., Topka H., Berghaeuser M., Wedde R.,
Mueller U.;
"Dopa-responsive dystonia: mutation analysis of GCH1 and analysis of
therapeutic doses of L-dopa. German Dystonia Study Group.";
Neurology 55:1735-1737(2000).
[46]
VARIANT DRD ARG-224.
PubMed=12391354; DOI=10.1212/WNL.59.8.1241;
Leuzzi V., Carducci C., Carducci C., Cardona F., Artiola C.,
Antonozzi I.;
"Autosomal dominant GTP-CH deficiency presenting as a dopa-responsive
myoclonus-dystonia syndrome.";
Neurology 59:1241-1243(2002).
[47]
VARIANT DRD ILE-106.
PubMed=17101830; DOI=10.1001/archneur.63.11.1605;
Ohta E., Funayama M., Ichinose H., Toyoshima I., Urano F., Matsuo M.,
Tomoko N., Yukihiko K., Yoshino S., Yokoyama H., Shimazu H., Maeda K.,
Hasegawa K., Obata F.;
"Novel mutations in the guanosine triphosphate cyclohydrolase 1 gene
associated with DYT5 dystonia.";
Arch. Neurol. 63:1605-1610(2006).
[48]
VARIANTS CYS-75; VAL-98 AND THR-135.
PubMed=23762320; DOI=10.1371/journal.pone.0065215;
Cai C., Shi W., Zeng Z., Zhang M., Ling C., Chen L., Cai C., Zhang B.,
Li W.D.;
"GTP cyclohydrolase I and tyrosine hydroxylase gene mutations in
familial and sporadic dopa-responsive dystonia patients.";
PLoS ONE 8:E65215-E65215(2013).
-!- FUNCTION: Positively regulates nitric oxide synthesis in umbilical
vein endothelial cells (HUVECs). May be involved in dopamine
synthesis. May modify pain sensitivity and persistence. Isoform
GCH-1 is the functional enzyme, the potential function of the
enzymatically inactive isoforms remains unknown.
{ECO:0000269|PubMed:12176133, ECO:0000269|PubMed:16338639,
ECO:0000269|PubMed:17057711, ECO:0000269|PubMed:8068008,
ECO:0000269|PubMed:9445252}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6-
(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
{ECO:0000269|PubMed:16778797, ECO:0000269|PubMed:2463916,
ECO:0000269|PubMed:3753653}.
-!- ENZYME REGULATION: GTP shows a positive allosteric effect, and
tetrahydrobiopterin inhibits the enzyme activity. Zinc is required
for catalytic activity. Inhibited by Mg(2+).
{ECO:0000269|PubMed:14717702, ECO:0000269|PubMed:16778797,
ECO:0000269|PubMed:3753653}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=116 uM for GTP {ECO:0000269|PubMed:2500984};
pH dependence:
Optimum pH is 7.7 in phosphate buffer.
{ECO:0000269|PubMed:2500984};
Temperature dependence:
Relatively stable at high temperatures. Retains 50% of its
activity after incubation at 70 degrees Celsius for 15 minutes.
{ECO:0000269|PubMed:2500984};
-!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step
1/1. {ECO:0000305|PubMed:16778797, ECO:0000305|PubMed:2463916,
ECO:0000305|PubMed:3753653}.
-!- SUBUNIT: Toroid-shaped homodecamer, composed of a dimer of
pentamers. The inactive isoforms also form decamers and may
possibly be incorporated into GCH1 heterodecamers, decreasing
enzyme stability and activity. Interacts with AHSA1 and
GCHFR/GFRP. {ECO:0000269|PubMed:11087827,
ECO:0000269|PubMed:16696853, ECO:0000269|PubMed:16848765}.
-!- INTERACTION:
O95433:AHSA1; NbExp=3; IntAct=EBI-958183, EBI-448610;
P63104:YWHAZ; NbExp=4; IntAct=EBI-958183, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12176133,
ECO:0000269|PubMed:16778797, ECO:0000269|PubMed:2463916}. Nucleus
{ECO:0000269|PubMed:16778797}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=GCH-1;
IsoId=P30793-1; Sequence=Displayed;
Name=GCH-2;
IsoId=P30793-2; Sequence=VSP_001612, VSP_001613;
Name=GCH-3;
IsoId=P30793-3; Sequence=VSP_001610;
Name=GCH-4;
IsoId=P30793-4; Sequence=VSP_001611, VSP_001614;
-!- TISSUE SPECIFICITY: In epidermis, expressed predominantly in basal
undifferentiated keratinocytes and in some but not all melanocytes
(at protein level). {ECO:0000269|PubMed:16778797}.
-!- INDUCTION: Up-regulated by IFNG/IFN-gamma, TNF, IL1B/interleukin-1
beta, bacterial lipopolysaccharides (LPS) and phenylalanine, and
down-regulated by dibutyryl-cAMP, iloprost and 8-bromo-cGMP in
HUVEC cells. Up-regulation of GCH1 expression, in turn, stimulates
production of tetrahydrobiopterin, with subsequent elevation of
endothelial nitric oxide synthase activity. Cytokine-induced GCH1
up-regulation in HUVECs in response to TNF and IFNG/IFN-gamma
involves cooperative activation of both the NF-kappa-B and
JAK2/STAT pathways. Also up-regulated by hydrogen peroxide in
human aorta endothelial cells (HAECs).
{ECO:0000269|PubMed:12002810, ECO:0000269|PubMed:12607127,
ECO:0000269|PubMed:14646243, ECO:0000269|PubMed:15604419,
ECO:0000269|PubMed:15649650, ECO:0000269|PubMed:7678411,
ECO:0000269|PubMed:9445252}.
-!- PTM: Phosphorylated by casein kinase II at Ser-81 in HAECs during
oscillatory shear stress; phosphorylation at Ser-81 results in
increased enzyme activity. {ECO:0000269|PubMed:17704208}.
-!- DISEASE: Hyperphenylalaninemia, BH4-deficient, B (HPABH4B)
[MIM:233910]: A disease characterized by malignant
hyperphenylalaninemia due to tetrahydrobiopterin deficiency, and
defective neurotransmission due to depletion of the
neurotransmitters dopamine and serotonin. The principal symptoms
include: psychomotor retardation, tonicity disorders, convulsions,
drowsiness, irritability, abnormal movements, hyperthermia,
hypersalivation, and difficulty swallowing. Some patients may
present a phenotype of intermediate severity between severe
hyperphenylalaninemia and mild dystonia. In this intermediate
phenotype, there is marked motor delay, but no mental retardation
and only minimal, if any, hyperphenylalaninemia.
{ECO:0000269|PubMed:7501255, ECO:0000269|PubMed:9667588}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Dystonia, dopa-responsive (DRD) [MIM:128230]: A form of
dystonia that responds to L-DOPA treatment without side effects.
Dystonia is defined by the presence of sustained involuntary
muscle contractions, often leading to abnormal postures. DRD
typically presents in childhood with walking problems due to
dystonia of the lower limbs and worsening of the dystonia towards
the evening. It is characterized by postural and motor
disturbances showing marked diurnal fluctuation. Torsion of the
trunk is unusual. Symptoms are alleviated after sleep and
aggravated by fatigue and exercise. {ECO:0000269|PubMed:10076897,
ECO:0000269|PubMed:10208576, ECO:0000269|PubMed:10582612,
ECO:0000269|PubMed:10825351, ECO:0000269|PubMed:10987649,
ECO:0000269|PubMed:11113234, ECO:0000269|PubMed:12391354,
ECO:0000269|PubMed:17101830, ECO:0000269|PubMed:7501255,
ECO:0000269|PubMed:7874165, ECO:0000269|PubMed:8852666,
ECO:0000269|PubMed:8957022, ECO:0000269|PubMed:9120469,
ECO:0000269|PubMed:9328244, ECO:0000269|PubMed:9778264}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S44049; AAB23164.1; -; mRNA.
EMBL; S44053; AAB23165.1; -; mRNA.
EMBL; S43856; AAB23166.1; -; mRNA.
EMBL; Z29433; CAB77391.1; -; mRNA.
EMBL; Z29434; CAB77392.1; -; mRNA.
EMBL; U19523; AAB16861.1; -; mRNA.
EMBL; U66095; AAD38866.1; -; mRNA.
EMBL; U66097; AAD38868.1; -; mRNA.
EMBL; CR536551; CAG38788.1; -; mRNA.
EMBL; CH471061; EAW80647.1; -; Genomic_DNA.
EMBL; BC025415; AAH25415.1; -; mRNA.
EMBL; L29478; AAB42186.1; -; Genomic_DNA.
EMBL; Z30952; CAA83213.1; -; Genomic_DNA.
EMBL; Z16418; CAA78908.1; -; mRNA.
EMBL; U19259; AAB60633.1; -; Genomic_DNA.
EMBL; U19256; AAB60633.1; JOINED; Genomic_DNA.
EMBL; U19257; AAB60633.1; JOINED; Genomic_DNA.
EMBL; U19258; AAB60633.1; JOINED; Genomic_DNA.
CCDS; CCDS41954.1; -. [P30793-4]
CCDS; CCDS45110.1; -. [P30793-2]
CCDS; CCDS9720.1; -. [P30793-1]
PIR; G01630; PC1117.
PIR; JC1225; JC1225.
RefSeq; NP_000152.1; NM_000161.2. [P30793-1]
RefSeq; NP_001019195.1; NM_001024024.1. [P30793-1]
RefSeq; NP_001019241.1; NM_001024070.1. [P30793-4]
RefSeq; NP_001019242.1; NM_001024071.1. [P30793-2]
UniGene; Hs.86724; -.
PDB; 1FB1; X-ray; 3.10 A; A/B/C/D/E=55-250.
PDBsum; 1FB1; -.
ProteinModelPortal; P30793; -.
SMR; P30793; -.
BioGrid; 108913; 31.
IntAct; P30793; 14.
MINT; MINT-3011998; -.
STRING; 9606.ENSP00000378890; -.
DrugBank; DB02377; Guanine.
DrugBank; DB02325; Isopropyl Alcohol.
iPTMnet; P30793; -.
PhosphoSitePlus; P30793; -.
BioMuta; GCH1; -.
DMDM; 399536; -.
EPD; P30793; -.
MaxQB; P30793; -.
PaxDb; P30793; -.
PeptideAtlas; P30793; -.
PRIDE; P30793; -.
DNASU; 2643; -.
Ensembl; ENST00000395514; ENSP00000378890; ENSG00000131979. [P30793-1]
Ensembl; ENST00000491895; ENSP00000419045; ENSG00000131979. [P30793-1]
Ensembl; ENST00000536224; ENSP00000445246; ENSG00000131979. [P30793-2]
Ensembl; ENST00000543643; ENSP00000444011; ENSG00000131979. [P30793-4]
Ensembl; ENST00000622544; ENSP00000477796; ENSG00000131979. [P30793-1]
GeneID; 2643; -.
KEGG; hsa:2643; -.
UCSC; uc001xbh.2; human. [P30793-1]
CTD; 2643; -.
DisGeNET; 2643; -.
EuPathDB; HostDB:ENSG00000131979.18; -.
GeneCards; GCH1; -.
GeneReviews; GCH1; -.
HGNC; HGNC:4193; GCH1.
HPA; HPA028612; -.
MalaCards; GCH1; -.
MIM; 128230; phenotype.
MIM; 233910; phenotype.
MIM; 600225; gene.
neXtProt; NX_P30793; -.
OpenTargets; ENSG00000131979; -.
Orphanet; 98808; Autosomal dominant dopa-responsive dystonia.
Orphanet; 2102; GTP cyclohydrolase I deficiency.
PharmGKB; PA28608; -.
eggNOG; KOG2698; Eukaryota.
eggNOG; COG0302; LUCA.
GeneTree; ENSGT00390000013481; -.
HOGENOM; HOG000221222; -.
HOVERGEN; HBG003136; -.
InParanoid; P30793; -.
KO; K01495; -.
OMA; PFMGKVH; -.
OrthoDB; EOG091G0PCE; -.
PhylomeDB; P30793; -.
TreeFam; TF105616; -.
BioCyc; MetaCyc:HS05586-MONOMER; -.
BRENDA; 3.5.4.16; 2681.
Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
SABIO-RK; P30793; -.
SIGNOR; P30793; -.
UniPathway; UPA00848; UER00151.
ChiTaRS; GCH1; human.
EvolutionaryTrace; P30793; -.
GeneWiki; GTP_cyclohydrolase_I; -.
GenomeRNAi; 2643; -.
PRO; PR:P30793; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000131979; -.
CleanEx; HS_GCH1; -.
ExpressionAtlas; P30793; baseline and differential.
Genevisible; P30793; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0044306; C:neuron projection terminus; TAS:ParkinsonsUK-UCL.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
GO; GO:0050662; F:coenzyme binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003934; F:GTP cyclohydrolase I activity; IDA:UniProtKB.
GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042416; P:dopamine biosynthetic process; IDA:UniProtKB.
GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
GO; GO:0006809; P:nitric oxide biosynthetic process; NAS:UniProtKB.
GO; GO:0010460; P:positive regulation of heart rate; IEA:Ensembl.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0042559; P:pteridine-containing compound biosynthetic process; IDA:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
GO; GO:0014916; P:regulation of lung blood pressure; IEA:Ensembl.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
GO; GO:2000121; P:regulation of removal of superoxide radicals; IMP:BHF-UCL.
GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0048265; P:response to pain; ISS:UniProtKB.
GO; GO:0034612; P:response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IDA:UniProtKB.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
HAMAP; MF_00223; FolE; 1.
InterPro; IPR001474; GTP_CycHdrlase_I.
InterPro; IPR018234; GTP_CycHdrlase_I_CS.
InterPro; IPR020602; GTP_CycHdrlase_I_dom.
PANTHER; PTHR11109; PTHR11109; 1.
Pfam; PF01227; GTP_cyclohydroI; 1.
TIGRFAMs; TIGR00063; folE; 1.
PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing;
Complete proteome; Cytoplasm; Disease mutation; Dystonia; GTP-binding;
Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Parkinsonism;
Phenylketonuria; Phosphoprotein; Polymorphism; Reference proteome;
Tetrahydrobiopterin biosynthesis; Zinc.
CHAIN 1 250 GTP cyclohydrolase 1.
/FTId=PRO_0000119478.
METAL 141 141 Zinc. {ECO:0000269|PubMed:11087827}.
METAL 144 144 Zinc. {ECO:0000269|PubMed:11087827}.
METAL 212 212 Zinc. {ECO:0000269|PubMed:11087827}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000269|PubMed:17704208}.
VAR_SEQ 210 250 Missing (in isoform GCH-3).
{ECO:0000303|PubMed:1520321}.
/FTId=VSP_001610.
VAR_SEQ 210 233 HMCMVMRGVQKMNSKTVTSTMLGV -> KSNKYNKGLSPLL
SSCHLFVAILK (in isoform GCH-4).
{ECO:0000303|PubMed:11284739}.
/FTId=VSP_001611.
VAR_SEQ 210 213 HMCM -> SAEP (in isoform GCH-2).
{ECO:0000303|PubMed:1520321,
ECO:0000303|PubMed:8068008}.
/FTId=VSP_001612.
VAR_SEQ 214 250 Missing (in isoform GCH-2).
{ECO:0000303|PubMed:1520321,
ECO:0000303|PubMed:8068008}.
/FTId=VSP_001613.
VAR_SEQ 234 250 Missing (in isoform GCH-4).
{ECO:0000303|PubMed:11284739}.
/FTId=VSP_001614.
VARIANT 15 15 G -> D (in HGCH-3).
/FTId=VAR_002632.
VARIANT 23 23 P -> L (in DRD; dbSNP:rs41298432).
{ECO:0000269|PubMed:9328244}.
/FTId=VAR_002633.
VARIANT 71 71 L -> Q (in DRD).
{ECO:0000269|PubMed:9778264}.
/FTId=VAR_016888.
VARIANT 74 74 A -> V (in DRD).
{ECO:0000269|PubMed:9778264}.
/FTId=VAR_016889.
VARIANT 75 75 Y -> C (found in patients with DRD;
unknown pathological significance).
/FTId=VAR_072733.
VARIANT 79 79 L -> P (in DRD).
{ECO:0000269|PubMed:7501255}.
/FTId=VAR_002634.
VARIANT 83 83 G -> A (in DRD).
{ECO:0000269|PubMed:10825351,
ECO:0000269|PubMed:9778264}.
/FTId=VAR_016890.
VARIANT 88 89 Missing (in DRD).
{ECO:0000269|PubMed:10825351}.
/FTId=VAR_016891.
VARIANT 88 88 R -> P (in DRD).
{ECO:0000269|PubMed:8852666}.
/FTId=VAR_002635.
VARIANT 88 88 R -> W (in DRD; dbSNP:rs104894433).
{ECO:0000269|PubMed:7874165}.
/FTId=VAR_002636.
VARIANT 90 90 G -> V (in DRD).
{ECO:0000269|PubMed:10076897}.
/FTId=VAR_016892.
VARIANT 98 98 A -> V.
/FTId=VAR_072734.
VARIANT 102 102 M -> K (in DRD).
{ECO:0000269|PubMed:10582612}.
/FTId=VAR_002637.
VARIANT 102 102 M -> R (in DRD).
{ECO:0000269|PubMed:10582612}.
/FTId=VAR_016893.
VARIANT 106 106 T -> I (in DRD).
{ECO:0000269|PubMed:17101830}.
/FTId=VAR_054112.
VARIANT 108 108 G -> D (in HPABH4B; intermediate
phenotype presenting with dystonia and
motor delay; dbSNP:rs104894435).
{ECO:0000269|PubMed:9667588}.
/FTId=VAR_016894.
VARIANT 115 115 D -> N (in DRD).
{ECO:0000269|PubMed:9328244}.
/FTId=VAR_016895.
VARIANT 134 134 D -> V (in DRD; dbSNP:rs104894437).
{ECO:0000269|PubMed:7874165}.
/FTId=VAR_002638.
VARIANT 135 135 I -> K (in DRD; dbSNP:rs104894441).
{ECO:0000269|PubMed:10208576}.
/FTId=VAR_016896.
VARIANT 135 135 I -> T.
/FTId=VAR_072735.
VARIANT 141 141 C -> R (in DRD).
{ECO:0000269|PubMed:10582612}.
/FTId=VAR_016897.
VARIANT 141 141 C -> W (in DRD).
{ECO:0000269|PubMed:10582612}.
/FTId=VAR_002639.
VARIANT 144 144 H -> P (in DRD; dbSNP:rs104894440).
{ECO:0000269|PubMed:8957022}.
/FTId=VAR_002640.
VARIANT 153 153 H -> P (in DRD).
{ECO:0000269|PubMed:8852666}.
/FTId=VAR_002641.
VARIANT 163 163 L -> R (in DRD).
{ECO:0000269|PubMed:11113234}.
/FTId=VAR_016898.
VARIANT 176 176 S -> T (in DRD).
{ECO:0000269|PubMed:10582612}.
/FTId=VAR_016899.
VARIANT 178 178 R -> S (in DRD).
{ECO:0000269|PubMed:10582612,
ECO:0000269|PubMed:10825351,
ECO:0000269|PubMed:9120469}.
/FTId=VAR_002642.
VARIANT 180 180 Q -> R (in DRD).
{ECO:0000269|PubMed:10825351}.
/FTId=VAR_016900.
VARIANT 184 184 R -> H (in HPABH4B; severe
hyperphenylalaninemia;
dbSNP:rs104894445).
{ECO:0000269|PubMed:7501255}.
/FTId=VAR_002643.
VARIANT 186 186 T -> K (in DRD).
{ECO:0000269|PubMed:10582612}.
/FTId=VAR_002644.
VARIANT 191 191 V -> I (in DRD; dbSNP:rs762208304).
{ECO:0000269|PubMed:9778264}.
/FTId=VAR_016901.
VARIANT 199 199 P -> L (in DRD).
{ECO:0000269|PubMed:10825351}.
/FTId=VAR_016902.
VARIANT 201 201 G -> E (in DRD; dbSNP:rs104894438).
{ECO:0000269|PubMed:10825351,
ECO:0000269|PubMed:7874165}.
/FTId=VAR_002645.
VARIANT 203 203 G -> R (in DRD).
{ECO:0000269|PubMed:8852666}.
/FTId=VAR_002646.
VARIANT 211 211 M -> I (in HPABH4B; severe
hyperphenylalaninemia;
dbSNP:rs104894443).
{ECO:0000269|PubMed:7501255}.
/FTId=VAR_002647.
VARIANT 211 211 M -> V (in DRD).
{ECO:0000269|PubMed:9778264}.
/FTId=VAR_016903.
VARIANT 213 213 M -> V (in DRD).
{ECO:0000269|PubMed:11113234}.
/FTId=VAR_016904.
VARIANT 221 221 M -> T (in HPABH4B; intermediate
phenotype presenting with dystonia and
motor delay; compound heterozygote for an
additional deletion; dbSNP:rs104894434).
{ECO:0000269|PubMed:9667588}.
/FTId=VAR_016905.
VARIANT 224 224 K -> R (in HPABH4B and DRD; phenotype
presenting with dystonia and myoclonus;
dbSNP:rs41298442).
{ECO:0000269|PubMed:12391354,
ECO:0000269|PubMed:8852666,
ECO:0000269|PubMed:9667588}.
/FTId=VAR_002648.
VARIANT 234 234 F -> S (in DRD).
{ECO:0000269|PubMed:8852666}.
/FTId=VAR_002649.
VARIANT 241 241 R -> W (in DRD).
{ECO:0000269|PubMed:9778264}.
/FTId=VAR_016906.
VARIANT 249 249 R -> S (in DRD; dbSNP:rs104894442).
{ECO:0000269|PubMed:10987649}.
/FTId=VAR_016907.
CONFLICT 11 11 E -> G (in Ref. 4; AAD38866).
{ECO:0000305}.
CONFLICT 206 206 V -> I (in Ref. 9; CAA78908).
{ECO:0000305}.
HELIX 61 81 {ECO:0000244|PDB:1FB1}.
HELIX 91 93 {ECO:0000244|PDB:1FB1}.
HELIX 94 102 {ECO:0000244|PDB:1FB1}.
TURN 103 106 {ECO:0000244|PDB:1FB1}.
HELIX 108 110 {ECO:0000244|PDB:1FB1}.
TURN 113 115 {ECO:0000244|PDB:1FB1}.
STRAND 130 141 {ECO:0000244|PDB:1FB1}.
TURN 142 144 {ECO:0000244|PDB:1FB1}.
STRAND 147 156 {ECO:0000244|PDB:1FB1}.
HELIX 165 176 {ECO:0000244|PDB:1FB1}.
STRAND 177 180 {ECO:0000244|PDB:1FB1}.
HELIX 182 197 {ECO:0000244|PDB:1FB1}.
STRAND 202 210 {ECO:0000244|PDB:1FB1}.
HELIX 211 214 {ECO:0000244|PDB:1FB1}.
TURN 215 217 {ECO:0000244|PDB:1FB1}.
STRAND 224 230 {ECO:0000244|PDB:1FB1}.
HELIX 233 236 {ECO:0000244|PDB:1FB1}.
HELIX 238 248 {ECO:0000244|PDB:1FB1}.
SEQUENCE 250 AA; 27903 MW; B8A0CB344C598B9A CRC64;
MEKGPVRAPA EKPRGARCSN GFPERDPPRP GPSRPAEKPP RPEAKSAQPA DGWKGERPRS
EEDNELNLPN LAAAYSSILS SLGENPQRQG LLKTPWRAAS AMQFFTKGYQ ETISDVLNDA
IFDEDHDEMV IVKDIDMFSM CEHHLVPFVG KVHIGYLPNK QVLGLSKLAR IVEIYSRRLQ
VQERLTKQIA VAITEALRPA GVGVVVEATH MCMVMRGVQK MNSKTVTSTM LGVFREDPKT
REEFLTLIRS


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