MACD1_BOVIN
ID MACD1_BOVIN Reviewed; 325 AA.
AC Q2KHU5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ADP-ribose glycohydrolase MACROD1 {ECO:0000305};
DE AltName: Full=MACRO domain-containing protein 1;
DE AltName: Full=O-acetyl-ADP-ribose deacetylase MACROD1;
DE EC=3.1.1.106 {ECO:0000250|UniProtKB:Q9BQ69};
DE AltName: Full=Protein LRP16;
DE AltName: Full=[Protein ADP-ribosylaspartate] hydrolase MACROD1 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:Q9BQ69};
DE AltName: Full=[Protein ADP-ribosylglutamate] hydrolase MACROD1 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:Q9BQ69};
GN Name=MACROD1; Synonyms=LRP16;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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. Plays a role in estrogen signaling.
CC Binds to androgen receptor (AR) and amplifies the transactivation
CC function of AR in response to androgen. May play an important role in
CC carcinogenesis and/or progression of hormone-dependent cancers by feed-
CC forward mechanism that activates ESR1 transactivation. Could be an ESR1
CC coactivator, providing a positive feedback regulatory loop for ESR1
CC signal transduction. Could be involved in invasive growth by down-
CC regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated
CC transcription activity. {ECO:0000250|UniProtKB:Q9BQ69}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose +
CC H(+); Xref=Rhea:RHEA:59244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:142723;
CC EC=3.1.1.106; Evidence={ECO:0000250|UniProtKB:Q9BQ69};
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 EC=3.1.1.106; Evidence={ECO:0000250|UniProtKB:Q9BQ69};
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:Q9BQ69};
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:Q9BQ69};
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:Q9BQ69};
CC -!- ACTIVITY REGULATION: Subject to competitive inhibition by the product
CC ADP-ribose. {ECO:0000250|UniProtKB:Q9BQ69}.
CC -!- SUBUNIT: Interacts with ESR1; Interacts in a manner that is estrogen
CC independent but is enhanced by estrogen. Interacts (via macro domain)
CC with AR. {ECO:0000250|UniProtKB:Q9BQ69}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BQ69}.
CC Note=Recruited to DNA lesions, probably via mono-APD-ribosylated
CC proteins. {ECO:0000250|UniProtKB:Q9BQ69}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC112879; AAI12880.1; -; mRNA.
DR RefSeq; NP_001039974.1; NM_001046509.1.
DR AlphaFoldDB; Q2KHU5; -.
DR SMR; Q2KHU5; -.
DR STRING; 9913.ENSBTAP00000022832; -.
DR PaxDb; Q2KHU5; -.
DR PRIDE; Q2KHU5; -.
DR Ensembl; ENSBTAT00000022832; ENSBTAP00000022832; ENSBTAG00000017181.
DR GeneID; 613568; -.
DR KEGG; bta:613568; -.
DR CTD; 28992; -.
DR VEuPathDB; HostDB:ENSBTAG00000017181; -.
DR VGNC; VGNC:56272; MACROD1.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000161450; -.
DR HOGENOM; CLU_046550_4_1_1; -.
DR InParanoid; Q2KHU5; -.
DR OrthoDB; 937161at2759; -.
DR TreeFam; TF341440; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000017181; Expressed in longissimus thoracis muscle and 107 other tissues.
DR ExpressionAtlas; Q2KHU5; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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 GO; GO:0042278; P:purine nucleoside metabolic process; IBA:GO_Central.
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 Acetylation; Hydrolase; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..325
FT /note="ADP-ribose glycohydrolase MACROD1"
FT /id="PRO_0000300460"
FT DOMAIN 141..322
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 21..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 172..174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 179..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 267..273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT MOD_RES 96
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT MOD_RES 129
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ69"
SQ SEQUENCE 325 AA; 35569 MW; 9FC586B54CC85DDB CRC64;
MFLQSRVSRL LAQLRAAGQL LGAPRPWPGP SPGATRTRSS ACGPPASLSA HHPRARTSAG
VGAWGAAAVG RRAGVRTWAP LAMAAKVDLS TSTDWKEAKS FLKGLSDKQR EEHYFCRDFV
RLKKIPTWKE TAKGVTVKVE EPKYKKDKQL NEKISLFRGD ITKLEVDAIV NAANSSLLGG
GGVDGCIHRA AGPLLTDECR TLQNCETGKA KITCGYRLPA KYVIHTVGPI AHGEPSASQA
AELRSCYLSS LDLLLEHRLR SAAFPCISTG VFGYPNEAAA EVVLTALREW LEQHKDKVDR
LIICVFLEKD ENIYRERLPH YFPVA
