ADPRH_BOVIN
ID ADPRH_BOVIN Reviewed; 353 AA.
AC Q32KR8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ADP-ribosylhydrolase ARH1 {ECO:0000305};
DE EC=3.2.2.19 {ECO:0000250|UniProtKB:P54922};
DE AltName: Full=ADP-ribose-L-arginine cleaving enzyme;
DE AltName: Full=[Protein ADP-ribosylarginine] hydrolase;
DE Short=ADP-ribosylarginine hydrolase;
GN Name=ADPRH; Synonyms=ARH1;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically acts as an arginine mono-ADP-ribosylhydrolase by
CC mediating the removal of mono-ADP-ribose attached to arginine residues
CC on proteins. {ECO:0000250|UniProtKB:P54922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-
CC ribose + L-arginyl-[protein]; Xref=Rhea:RHEA:14885, Rhea:RHEA-
CC COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29965, ChEBI:CHEBI:57967, ChEBI:CHEBI:142554;
CC EC=3.2.2.19; Evidence={ECO:0000250|UniProtKB:P54922};
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:P54922};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P54922};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:P54922};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P54922}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; BC109957; AAI09958.1; -; mRNA.
DR RefSeq; NP_001033643.1; NM_001038554.1.
DR AlphaFoldDB; Q32KR8; -.
DR SMR; Q32KR8; -.
DR STRING; 9913.ENSBTAP00000049744; -.
DR PaxDb; Q32KR8; -.
DR PRIDE; Q32KR8; -.
DR Ensembl; ENSBTAT00000072794; ENSBTAP00000062367; ENSBTAG00000009391.
DR GeneID; 525738; -.
DR KEGG; bta:525738; -.
DR CTD; 141; -.
DR VEuPathDB; HostDB:ENSBTAG00000009391; -.
DR VGNC; VGNC:25690; ADPRH.
DR eggNOG; ENOG502QPMI; Eukaryota.
DR GeneTree; ENSGT00940000159279; -.
DR HOGENOM; CLU_047061_0_0_1; -.
DR InParanoid; Q32KR8; -.
DR OrthoDB; 1112828at2759; -.
DR TreeFam; TF329417; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000009391; Expressed in liver and 108 other tissues.
DR ExpressionAtlas; Q32KR8; baseline and differential.
DR GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; ISS:UniProtKB.
DR GO; GO:0051725; P:protein de-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0036211; P:protein modification process; ISS:UniProtKB.
DR Gene3D; 1.10.4080.10; -; 1.
DR InterPro; IPR012108; ADP-ribosylarg_hydro.
DR InterPro; IPR005502; Ribosyl_crysJ1.
DR InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR Pfam; PF03747; ADP_ribosyl_GH; 1.
DR PIRSF; PIRSF016939; ADP_ribslarg_hdr; 1.
DR SUPFAM; SSF101478; SSF101478; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..353
FT /note="ADP-ribosylhydrolase ARH1"
FT /id="PRO_0000247292"
FT REGION 106..108
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT REGION 168..170
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT REGION 268..270
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT REGION 274..275
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54922"
SQ SEQUENCE 353 AA; 39152 MW; 1FE3280025C0D274 CRC64;
MCGALMERYV AAMVLSAAGD ALGYFNGKWE FLQNGEKIHR QLAQLGGLDA IDVERWRVSD
DTVMHLATAE ALLEAGKVSD LTHLYSLLAK HYQDCMGDMD GRAPGGASVQ NAMLLEPDKA
DGWRIPFNSH EGGCGAAMRA MCIGLRFPHS SQLDSLIQVS IESGRMTHHH PTGYLGALVS
ALFTAYAVNG KPPQQWGRGL MEVLPEAKKY IVQSGFFVEQ NLQHWSYFQD QWEKYLKLRG
IWDGKSAPTF PKPFDVKERD QFYSSVSYSG WGGSSGHDAP MIAYDAILAA GDSWKELAHR
AFFHGGDSDS TAAIAGCWWG VMYGFKGVSP SNYEKLEYRN RLEETARALY SLR
