ADPRH_RAT
ID ADPRH_RAT Reviewed; 362 AA.
AC Q02589; Q66H27;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
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 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].
RC TISSUE=Brain;
RX PubMed=1375222; DOI=10.1016/s0021-9258(19)50043-6;
RA Moss J., Stanley S.J., Nightingale M.S., Murtagh J.J. Jr., Monaco L.,
RA Mishima K., Chen H.C., Williamson K.C., Tsai S.C.;
RT "Molecular and immunological characterization of ADP-ribosylarginine
RT hydrolases.";
RL J. Biol. Chem. 267:10481-10488(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP PROTEIN SEQUENCE OF 147-165, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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 -!- ACTIVITY REGULATION: Its activity is synergistically stimulated by
CC magnesium and dithiothreitol (DTT) in vitro.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P54922}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; M86341; AAA40691.1; -; mRNA.
DR EMBL; BC082065; AAH82065.1; -; mRNA.
DR PIR; A38135; A38135.
DR RefSeq; NP_899154.2; NM_183325.2.
DR RefSeq; XP_006248422.1; XM_006248360.3.
DR AlphaFoldDB; Q02589; -.
DR SMR; Q02589; -.
DR STRING; 10116.ENSRNOP00000034815; -.
DR iPTMnet; Q02589; -.
DR PhosphoSitePlus; Q02589; -.
DR jPOST; Q02589; -.
DR PaxDb; Q02589; -.
DR PRIDE; Q02589; -.
DR DNASU; 25371; -.
DR Ensembl; ENSRNOT00000038439; ENSRNOP00000034815; ENSRNOG00000027260.
DR GeneID; 25371; -.
DR KEGG; rno:25371; -.
DR UCSC; RGD:2052; rat.
DR CTD; 141; -.
DR RGD; 2052; Adprh.
DR eggNOG; ENOG502QPMI; Eukaryota.
DR GeneTree; ENSGT00530000063627; -.
DR HOGENOM; CLU_047061_0_0_1; -.
DR InParanoid; Q02589; -.
DR OMA; ACWWGAM; -.
DR OrthoDB; 1112828at2759; -.
DR PhylomeDB; Q02589; -.
DR TreeFam; TF329417; -.
DR PRO; PR:Q02589; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000027260; Expressed in thymus and 20 other tissues.
DR Genevisible; Q02589; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IDA:RGD.
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 Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..362
FT /note="ADP-ribosylhydrolase ARH1"
FT /id="PRO_0000157285"
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"
FT CONFLICT 252
FT /note="K -> Q (in Ref. 1; AAA40691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39961 MW; 6C941A940AEAE10E CRC64;
MGGGLIERYV AAMVLSAAGD TLGYFNGKWE FLRDGEKIHR QLAQMGDLEA IDVAQWRVSD
DTIMHLATAE ALMEAGSSPD LPQLYSLLAK HYRDCMGDMD GRAPGGACMQ NAMQLDPDRA
DGWRIPFNSH EGGCGAAMRA MCIGLRFPHP SQLDTLIQVS IESGRMTHHH PTGYLGSLAS
ALFTAYAVNG KSPRQWGKGL MEVLPEAKAY VTQSGYFVKE NLQHWSYFEK EWEKYLELRG
ILDGKSAPVF PKPFGVKERD QFYIEVSYSG WGGSSGHDAP MIAYDALLAA GDSWKELAHR
AFFHGGDSDS TATIAGCWWG VMHGFKGVNP SNYEKLEYRQ RLEEAGRALY SLGSKEDTIL
GP
