GUAD_MOUSE
ID GUAD_MOUSE Reviewed; 454 AA.
AC Q9R111;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Guanine deaminase;
DE Short=Guanase;
DE Short=Guanine aminase;
DE EC=3.5.4.3 {ECO:0000305|PubMed:10075721};
DE AltName: Full=Guanine aminohydrolase;
DE Short=GAH;
GN Name=Gda {ECO:0000312|MGI:MGI:95678};
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Paletzki R.F., Gerfen C.R.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=C57BL/6J; TISSUE=Erythrocyte;
RX PubMed=10075721; DOI=10.1074/jbc.274.12.8175;
RA Yuan G., Bin J.C., McKay D.J., Snyder F.F.;
RT "Cloning and characterization of human guanine deaminase. Purification and
RT partial amino acid sequence of the mouse protein.";
RL J. Biol. Chem. 274:8175-8180(1999).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, and
RC Spleen;
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: Catalyzes the hydrolytic deamination of guanine, producing
CC xanthine and ammonia. {ECO:0000269|PubMed:10075721}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanine + H(+) + H2O = NH4(+) + xanthine;
CC Xref=Rhea:RHEA:14665, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16235, ChEBI:CHEBI:17712, ChEBI:CHEBI:28938; EC=3.5.4.3;
CC Evidence={ECO:0000305|PubMed:10075721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14666;
CC Evidence={ECO:0000305|PubMed:10075721};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2T3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y2T3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.7 uM for guanine {ECO:0000269|PubMed:10075721};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1. {ECO:0000269|PubMed:10075721}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2T3}.
CC -!- INTERACTION:
CC Q9R111; Q62108: Dlg4; NbExp=6; IntAct=EBI-2308876, EBI-300895;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
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DR EMBL; AF174583; AAD50297.1; -; mRNA.
DR CCDS; CCDS29698.1; -.
DR RefSeq; NP_034396.1; NM_010266.2.
DR AlphaFoldDB; Q9R111; -.
DR SMR; Q9R111; -.
DR BioGRID; 199872; 19.
DR IntAct; Q9R111; 3.
DR MINT; Q9R111; -.
DR STRING; 10090.ENSMUSP00000084882; -.
DR MEROPS; M38.981; -.
DR iPTMnet; Q9R111; -.
DR PhosphoSitePlus; Q9R111; -.
DR SwissPalm; Q9R111; -.
DR REPRODUCTION-2DPAGE; IPI00469987; -.
DR REPRODUCTION-2DPAGE; Q9R111; -.
DR jPOST; Q9R111; -.
DR MaxQB; Q9R111; -.
DR PaxDb; Q9R111; -.
DR PRIDE; Q9R111; -.
DR ProteomicsDB; 271489; -.
DR Antibodypedia; 12519; 266 antibodies from 24 providers.
DR DNASU; 14544; -.
DR Ensembl; ENSMUST00000087600; ENSMUSP00000084882; ENSMUSG00000058624.
DR GeneID; 14544; -.
DR KEGG; mmu:14544; -.
DR UCSC; uc008gyx.1; mouse.
DR CTD; 9615; -.
DR MGI; MGI:95678; Gda.
DR VEuPathDB; HostDB:ENSMUSG00000058624; -.
DR eggNOG; KOG3968; Eukaryota.
DR GeneTree; ENSGT00390000017130; -.
DR InParanoid; Q9R111; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 612054at2759; -.
DR PhylomeDB; Q9R111; -.
DR TreeFam; TF324539; -.
DR Reactome; R-MMU-74259; Purine catabolism.
DR SABIO-RK; Q9R111; -.
DR UniPathway; UPA00603; UER00660.
DR BioGRID-ORCS; 14544; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Gda; mouse.
DR PRO; PR:Q9R111; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9R111; protein.
DR Bgee; ENSMUSG00000058624; Expressed in epithelium of small intestine and 174 other tissues.
DR ExpressionAtlas; Q9R111; baseline and differential.
DR Genevisible; Q9R111; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0008892; F:guanine deaminase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0000255; P:allantoin metabolic process; IDA:MGI.
DR GO; GO:0006161; P:deoxyguanosine catabolic process; IDA:MGI.
DR GO; GO:0046055; P:dGMP catabolic process; IDA:MGI.
DR GO; GO:0046038; P:GMP catabolic process; IDA:MGI.
DR GO; GO:0006147; P:guanine catabolic process; IDA:MGI.
DR GO; GO:0046098; P:guanine metabolic process; IBA:GO_Central.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR CDD; cd01303; GDEase; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR014311; Guanine_deaminase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11271:SF6; PTHR11271:SF6; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..454
FT /note="Guanine deaminase"
FT /id="PRO_0000122299"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 213..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 240..243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTT6"
SQ SEQUENCE 454 AA; 51013 MW; 7711573C8C93D64E CRC64;
MCAARTPPLA LVFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEESSQ QEKLAKEWCF
KPCEIRELSH HEFFMPGLVD THIHAPQYAF AGSNVDLPLL EWLNKYTFPT EQRFRSTDVA
EEVYTRVVRR TLKNGTTTAC YFGTIHTDSS LILAEITDKF GQRAFVGKVC MDLNDTVPEY
KETTEESVKE TERFVSEMLQ KNYPRVKPIV TPRFTLSCTE TLMSELGNIA KTHDLYIQSH
ISENREEIEA VKSLYPSYKN YTDVYDKNNL LTNKTVMAHG CYLSEEELNI FSERGASIAH
CPNSNLSLSS GLLNVLEVLK HKVKIGLGTD VAGGYSYSML DAIRRAVMVS NVLLINKVNE
KNLTLKEVFR LATLGGSQAL GLDSEIGNFE VGKEFDALLI NPRASDSPID LFYGDFVGDI
SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV
