MUTYH_RAT
ID MUTYH_RAT Reviewed; 516 AA.
AC Q8R5G2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Adenine DNA glycosylase;
DE EC=3.2.2.31 {ECO:0000250|UniProtKB:Q99P21};
DE AltName: Full=MutY homolog;
DE Short=rMYH;
GN Name=Mutyh; Synonyms=Myh;
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 TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
RX PubMed=11948257; DOI=10.1046/j.0022-3042.2002.00774.x;
RA Lee H.-M., Wang C., Hu Z., Greeley G.H. Jr., Makalowski W., Hellmich H.L.,
RA Englander E.W.;
RT "Hypoxia induces mitochondrial DNA damage and stimulates expression of a
RT DNA repair enzyme, the Escherichia coli MutY DNA glycosylase homolog (MYH),
RT in vivo, in the rat brain.";
RL J. Neurochem. 80:928-937(2002).
CC -!- FUNCTION: Involved in oxidative DNA damage repair. Initiates repair of
CC A*oxoG to C*G by removing the inappropriately paired adenine base from
CC the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase
CC activities. {ECO:0000250|UniProtKB:Q9UIF7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-
CC oxoguanine:adenine mismatched double-stranded DNA, leaving an
CC apurinic site.; EC=3.2.2.31; Evidence={ECO:0000250|UniProtKB:Q9UIF7};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a
CC role in catalysis, but is probably involved in the proper positioning
CC of the enzyme along the DNA strand. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UIF7}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q99P21}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, spleen, heart, liver and
CC kidney. {ECO:0000269|PubMed:11948257}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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DR EMBL; AF478683; AAL79551.1; -; mRNA.
DR RefSeq; NP_579850.1; NM_133316.1.
DR AlphaFoldDB; Q8R5G2; -.
DR SMR; Q8R5G2; -.
DR STRING; 10116.ENSRNOP00000024375; -.
DR PhosphoSitePlus; Q8R5G2; -.
DR PaxDb; Q8R5G2; -.
DR PRIDE; Q8R5G2; -.
DR GeneID; 170841; -.
DR KEGG; rno:170841; -.
DR UCSC; RGD:620045; rat.
DR CTD; 4595; -.
DR RGD; 620045; Mutyh.
DR eggNOG; KOG2457; Eukaryota.
DR InParanoid; Q8R5G2; -.
DR OrthoDB; 616758at2759; -.
DR PhylomeDB; Q8R5G2; -.
DR BRENDA; 3.2.2.31; 5301.
DR Reactome; R-RNO-110331; Cleavage of the damaged purine.
DR Reactome; R-RNO-110357; Displacement of DNA glycosylase by APEX1.
DR PRO; PR:Q8R5G2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0035485; F:adenine/guanine mispair binding; IBA:GO_Central.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032407; F:MutSalpha complex binding; ISO:RGD.
DR GO; GO:0032357; F:oxidized purine DNA binding; IBA:GO_Central.
DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0060546; P:negative regulation of necroptotic process; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR CDD; cd03431; DNA_Glycosylase_C; 1.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR InterPro; IPR005760; A/G_AdeGlyc_MutY.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR42944; PTHR42944; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR01084; mutY; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..516
FT /note="Adenine DNA glycosylase"
FT /id="PRO_0000102241"
FT DOMAIN 335..467
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 376..398
FT /note="Nudix box"
FT COMPBIAS 1..20
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT SITE 207
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P83847"
SQ SEQUENCE 516 AA; 57919 MW; E42FD4AC86BE3467 CRC64;
MKKLRASVRS HKKQPANHKR RGKCALSSSQ AKPSGLDGLA KQKREELLKT PVSPYHLFSD
IADVTAFRRN LLSWYDQEKR DLPWRKRVKE ETNLDRRAYA VWVSEVMLQQ TQVATVIDYY
TRWMQKWPTL QDLASASLEE VNQLWSGLGY YSRGRRLQEG ARKVVEELGG HVPRTAETLQ
QLLPGVGRYT AGAIASIAFD QVTGVVDGNV IRVLCRVRAI GADPTSSFVS HHLWDLAQQL
VDPARPGDFN QAAMELGATV CTPQRPLCNH CPVQSLCRAH QRVGQGRLSA LPGSPDIEEC
ALNTRQCQLC LPSTNPWDPN MGVVNFPRKA SRRPPREEYS ATCVVEQPGA TGGPLILLVQ
RPNSGLLAGL WEFPSVTLEP SGQHQHKALL QELQHWSAPL PTTPLQHLGE VIHVFSHIKL
TYQVYSLALE GQTPASTTLP GARWLTWEEF RNAAVSTAMK KVFRVYEEHR RGTCKGSKRP
QVCTPSSRKK PSRGQQVLDR FFQRHIPTHK PNSTTQ
