ADPRH_MOUSE
ID ADPRH_MOUSE Reviewed; 362 AA.
AC P54923;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 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], AND FUNCTION.
RX PubMed=8349667; DOI=10.1016/s0021-9258(17)46780-9;
RA Takada T., Iida K., Moss J.;
RT "Cloning and site-directed mutagenesis of human ADP-ribosylarginine
RT hydrolase.";
RL J. Biol. Chem. 268:17837-17843(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15893437; DOI=10.1016/j.gene.2005.02.016;
RA Aoki K., Kato J., Shoemaker M.T., Moss J.;
RT "Genomic organization and promoter analysis of the mouse ADP-
RT ribosylarginine hydrolase gene.";
RL Gene 351:83-95(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
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: 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:0000269|PubMed:8349667}.
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 -!- ACTIVITY REGULATION: Synergistically stimulated by magnesium and
CC dithiothreitol (DTT) in vitro. {ECO:0000269|PubMed:8349667}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P54922}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; L13290; AAA37259.1; -; mRNA.
DR EMBL; AF244347; AAF86223.1; -; mRNA.
DR EMBL; BC003437; AAH03437.1; -; mRNA.
DR CCDS; CCDS28167.1; -.
DR PIR; A47411; A47411.
DR RefSeq; NP_031440.1; NM_007414.3.
DR AlphaFoldDB; P54923; -.
DR SMR; P54923; -.
DR BioGRID; 197997; 1.
DR IntAct; P54923; 1.
DR MINT; P54923; -.
DR STRING; 10090.ENSMUSP00000002923; -.
DR iPTMnet; P54923; -.
DR PhosphoSitePlus; P54923; -.
DR REPRODUCTION-2DPAGE; P54923; -.
DR EPD; P54923; -.
DR PaxDb; P54923; -.
DR PeptideAtlas; P54923; -.
DR PRIDE; P54923; -.
DR ProteomicsDB; 281941; -.
DR Antibodypedia; 32747; 134 antibodies from 22 providers.
DR DNASU; 11544; -.
DR Ensembl; ENSMUST00000002923; ENSMUSP00000002923; ENSMUSG00000002844.
DR GeneID; 11544; -.
DR KEGG; mmu:11544; -.
DR UCSC; uc007zex.1; mouse.
DR CTD; 141; -.
DR MGI; MGI:1098234; Adprh.
DR VEuPathDB; HostDB:ENSMUSG00000002844; -.
DR eggNOG; ENOG502QPMI; Eukaryota.
DR GeneTree; ENSGT00530000063627; -.
DR HOGENOM; CLU_047061_0_0_1; -.
DR InParanoid; P54923; -.
DR OMA; ACWWGAM; -.
DR OrthoDB; 1112828at2759; -.
DR PhylomeDB; P54923; -.
DR TreeFam; TF329417; -.
DR BioGRID-ORCS; 11544; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adprh; mouse.
DR PRO; PR:P54923; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P54923; protein.
DR Bgee; ENSMUSG00000002844; Expressed in frontonasal prominence and 251 other tissues.
DR ExpressionAtlas; P54923; baseline and differential.
DR Genevisible; P54923; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IMP: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; IMP: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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..362
FT /note="ADP-ribosylhydrolase ARH1"
FT /id="PRO_0000157284"
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 362 AA; 40068 MW; E06BCAEF69BA7C4E CRC64;
MGGGLIERYV AAMVLSAAGD TLGYFNGKWE FIRDGETIHQ QLAQMGDLEA IDVARWRVSD
DTVMHLATAE ALMEAGQSPD LPRLYSLLAK HYRDCMGDMD GRAPGGACMQ NAMLLQPNRA
DGYRIPFNSH EGGCGAAMRA MCIGLRFPHP SQLDLLIQVS IESGRMTHHH PTGYLGSLAS
ALFTAYAVNG KSPWQWGKGL MEVLPEAKKY ITQSGYFVKE NLQHWSYFEK EWEKYLELRG
ILDGNSAPVF PQPFGVKERD QFYIDVSYSG WGGSSGHDAP MIAYDALLAA GDSWKELAHR
AFFHGGDSDS TAAIAGCWWG VMYGFKGVNP ANYEKLEYRQ RLEEAGRALY SLGSKEDPVL
DP
