MACD2_XENLA
ID MACD2_XENLA Reviewed; 418 AA.
AC Q6PAV8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=ADP-ribose glycohydrolase MACROD2 {ECO:0000305};
DE AltName: Full=MACRO domain-containing protein 2;
DE AltName: Full=O-acetyl-ADP-ribose deacetylase MACROD2 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:A1Z1Q3};
DE AltName: Full=[Protein ADP-ribosylaspartate] hydrolase MACROD2 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:A1Z1Q3};
DE AltName: Full=[Protein ADP-ribosylglutamate] hydrolase MACROD2 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:A1Z1Q3};
GN Name=macrod2 {ECO:0000250|UniProtKB:A1Z1Q3};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes ADP-ribose from aspartate and glutamate residues in
CC proteins bearing a single ADP-ribose moiety. Inactive towards proteins
CC bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling
CC molecule generated by the deacetylation of acetylated lysine residues
CC in histones and other proteins. {ECO:0000250|UniProtKB:A1Z1Q3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose +
CC H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:83767;
CC Evidence={ECO:0000250|UniProtKB:A1Z1Q3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose
CC + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:A1Z1Q3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose
CC + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:142540; Evidence={ECO:0000250|UniProtKB:A1Z1Q3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017;
CC Evidence={ECO:0000250|UniProtKB:A1Z1Q3};
CC -!- ACTIVITY REGULATION: Subject to product inhibition by ADP-ribose.
CC {ECO:0000250|UniProtKB:A1Z1Q3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A1Z1Q3}.
CC Note=Recruited to DNA lesions, probably via mono-APD-ribosylated
CC proteins. {ECO:0000250|UniProtKB:A1Z1Q3}.
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DR EMBL; BC060026; AAH60026.1; -; mRNA.
DR RefSeq; NP_001083167.1; NM_001089698.1.
DR AlphaFoldDB; Q6PAV8; -.
DR SMR; Q6PAV8; -.
DR BioGRID; 100110; 1.
DR IntAct; Q6PAV8; 1.
DR DNASU; 398781; -.
DR GeneID; 398781; -.
DR KEGG; xla:398781; -.
DR CTD; 398781; -.
DR Xenbase; XB-GENE-17341478; macrod2.L.
DR OrthoDB; 937161at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398781; Expressed in brain and 17 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140293; F:ADP-ribosylglutamate hydrolase activity; ISS:UniProtKB.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; ISS:UniProtKB.
DR GO; GO:0051725; P:protein de-ADP-ribosylation; ISS:UniProtKB.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 2: Evidence at transcript level;
KW DNA damage; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..418
FT /note="ADP-ribose glycohydrolase MACROD2"
FT /id="PRO_0000300463"
FT DOMAIN 57..238
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 238..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 95..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 183..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
SQ SEQUENCE 418 AA; 46354 MW; 3F6DC29218EEA94D CRC64;
MYQSNKKKRL WKEEKERLLN MTRDERRKEY REYVSLDKIP SLMEELKSKA SSDDESPEEI
QVKNSLCEKV SFYKGDITQL EVDAIVNAAN TSLLGGGGVD GCIHRASGPS LLAECRELGG
CETGQAKITC GYELPAKYVI HTVGPIARGH ITPNHKQDLA SCYNSSLTLA TENDIRTIAF
PCISTGIYGY PNEPAANVAL TTVKEFLKKN RDKIDRVIFC VFLEVDFKIY KRKLNEFFPK
DGGDDEEGEK GDSDEMKEDT EGKPQSPPMK KIKEKKEDTP APDSPDEEYS AEEATGNTQD
MTAMSLETNE GNDVSSPATD PLKEGEELSE AKITGEKISV EPKTPEPEDA KMTVEEKSQE
QEDSENMETS QPKVSGETED LDGDSEEPSD VQKEIASPSN ETCQESDPKD TNDDANEA
