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-NOV-2009, entry version 72.
DE   RecName: Full=[Protein ADP-ribosylarginine] hydrolase;
DE            Short=ADP-ribosylarginine hydrolase;
DE            EC=3.2.2.19;
DE   AltName: Full=ADP-ribose-L-arginine cleaving enzyme;
GN   Name=Adprh; Synonyms=Arh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93352593; PubMed=8349667;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the reverse reaction of mono-ADP-ribosylation.
CC   -!- CATALYTIC ACTIVITY: Protein-N(omega)-(ADP-D-ribosyl)-L-arginine +
CC       H(2)O = ADP-ribose + protein-L-arginine.
CC   -!- CATALYTIC ACTIVITY: N(omega)-(ADP-D-ribosyl)-L-arginine + H(2)O =
CC       ADP-ribose + L-arginine.
CC   -!- ENZYME REGULATION: Synergistically stimulated by magnesium and
CC       dithiothreitol (DTT) in vitro.
CC   -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
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DR   EMBL; L13290; AAA37259.1; -; mRNA.
DR   EMBL; AF244347; AAF86223.1; -; mRNA.
DR   EMBL; BC003437; AAH03437.1; -; mRNA.
DR   IPI; IPI00111149; -.
DR   PIR; A47411; A47411.
DR   RefSeq; NP_031440.1; -.
DR   UniGene; Mm.20047; -.
DR   STRING; P54923; -.
DR   PhosphoSite; P54923; -.
DR   REPRODUCTION-2DPAGE; P54923; -.
DR   PRIDE; P54923; -.
DR   Ensembl; ENSMUST00000002923; ENSMUSP00000002923; ENSMUSG00000002844; Mus musculus.
DR   GeneID; 11544; -.
DR   KEGG; mmu:11544; -.
DR   UCSC; uc007zex.1; mouse.
DR   CTD; 11544; -.
DR   MGI; MGI:1098234; Adprh.
DR   HOGENOM; P54923; -.
DR   HOVERGEN; P54923; -.
DR   OMA; IPFNSHE; -.
DR   BRENDA; 3.2.2.19; 244.
DR   NextBio; 279014; -.
DR   ArrayExpress; P54923; -.
DR   Bgee; P54923; -.
DR   CleanEx; MM_ADPRH; -.
DR   Genevestigator; P54923; -.
DR   GermOnline; ENSMUSG00000002844; Mus musculus.
DR   GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IMP:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051725; P:protein amino acid de-ADP-ribosylation; IEA:InterPro.
DR   InterPro; IPR012108; ADP-ribosylarg_hydro.
DR   InterPro; IPR005502; Ribosyl_crysJ1.
DR   PANTHER; PTHR22957:SF7; ADP-ribosylarg_hydro; 1.
DR   Pfam; PF03747; ADP_ribosyl_GH; 1.
DR   PIRSF; PIRSF016939; ADP_ribslarg_hdr; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium.
FT   CHAIN         1    362       [Protein ADP-ribosylarginine] hydrolase.
FT                                /FTId=PRO_0000157284.
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
//