ID   ARHL2_BOVIN             Reviewed;         365 AA.
AC   Q3SYV9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Poly(ADP-ribose) glycohydrolase ARH3;
DE            EC=3.2.1.143;
DE   AltName: Full=ADP-ribosylhydrolase 3;
DE   AltName: Full=[Protein ADP-ribosylarginine] hydrolase-like protein 2;
GN   Name=ADPRHL2; Synonyms=ARH3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only
CC       present transiently and is rapidly degraded by poly(ADP-ribose)
CC       glycohydrolase. Poly(ADP-ribose) metabolism may be required for
CC       maintenance of the normal function of neuronal cells. Generates
CC       ADP-ribose from poly-(ADP-ribose), but does not hydrolyze ADP-
CC       ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes poly(ADP-ribose) at glycosidic
CC       (1''-2') linkage of ribose-ribose bond to produce free ADP-ribose.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC103360; AAI03361.1; -; mRNA.
DR   IPI; IPI00692404; -.
DR   RefSeq; NP_001030417.1; -.
DR   UniGene; Bt.51810; -.
DR   SMR; Q3SYV9; 20-364.
DR   PRIDE; Q3SYV9; -.
DR   Ensembl; ENSBTAG00000021715; Bos taurus.
DR   GeneID; 521650; -.
DR   KEGG; bta:521650; -.
DR   HOVERGEN; Q3SYV9; -.
DR   BRENDA; 3.2.1.143; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IEA:EC.
DR   InterPro; IPR005502; Ribosyl_crysJ1.
DR   Pfam; PF03747; ADP_ribosyl_GH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus.
FT   CHAIN         1    365       Poly(ADP-ribose) glycohydrolase ARH3.
FT                                /FTId=PRO_0000277612.
FT   COMPBIAS      2      6       Poly-Ala.
FT   METAL        42     42       Magnesium 2 (By similarity).
FT   METAL        77     77       Magnesium 1 (By similarity).
FT   METAL        78     78       Magnesium 1 (By similarity).
FT   METAL        79     79       Magnesium 1 (By similarity).
FT   METAL       315    315       Magnesium 2 (By similarity).
FT   METAL       317    317       Magnesium 1 (By similarity).
FT   METAL       317    317       Magnesium 2 (By similarity).
FT   METAL       318    318       Magnesium 2 (By similarity).
SQ   SEQUENCE   365 AA;  39221 MW;  59F65453AABF2802 CRC64;
     MAAAAAMTAA GCGGAGAARS LSRFRGCLAG ALLGDCVGAV YEARDTVDLT SVLRQVQDLE
     PDPGSPGSAR TEALCYTDDT AMARALVQSL LAKEAFDEVD MAHRFAQEYK KDPDRGYGAG
     VITVFRKHLS PRCRDVFEPA RAQFNGKGSY GNGGAMRVAG ISLAYSSVQD VQKFARLSAQ
     LTHASSLGYN GAILQALAVH LALQGESSSE HFLEQLLGHM EELESDAQSV LDARELGMEE
     RPYSSRLKKI GELLEQDSVT REEVVSELGN GIAAFESVPT AIYCFLRCME PDPEIPSTFN
     SLQRTLVYSI SLGGDTDTIA TMAGAIAGAY YGMEQVPESW QQSCEGYEET DVLAQSLHRV
     FQKSL
//