(data stored in ACNUC16162 zone)

HOGENOM: RAT11_PE442

ID   RAT11_PE442                          STANDARD;      PRT;   362 AA.
AC   RAT11_PE442; Q02589; Q66H27;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=[Protein ADP-ribosylarginine] hydrolase;
DE   Short=ADP-ribosylarginine hydrolase; EC=3.2.2 19;AltName:
DE   Full=ADP-ribose-L-arginine cleaving enzyme; (RAT11.PE442).
GN   Name=Adprh; Synonyms=Arh1;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT11.PE442.
CC       Rattus norvegicus chromosome 11 RGSC3.4  sequence 1..87759784
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:ADPRH_RAT
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: Its activity is synergistically stimulated by
CC       magnesium and dithiothreitol (DTT) in vitro.
CC   -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC   -!- GENE_FAMILY: HOG000007974 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000027260;ENSRNOT00000038439;ENSRNOP00000034815.
DR   EMBL; BC082065; - ;
DR   EMBL; M86341; - ;
DR   UniProtKB/Swiss-Prot; Q02589; Q66H27; -.
DR   EMBL; M86341; AAA40691.1; -; mRNA.
DR   EMBL; BC082065; AAH82065.1; -; mRNA.
DR   IPI; IPI00208197; -.
DR   PIR; A38135; A38135.
DR   RefSeq; NP_899154.2; NM_183325.2.
DR   UniGene; Rn.13315; -.
DR   ProteinModelPortal; Q02589; -.
DR   PRIDE; Q02589; -.
DR   Ensembl; ENSRNOT00000038439; ENSRNOP00000034815; ENSRNOG00000027260.
DR   GeneID; 25371; -.
DR   KEGG; rno:25371; -.
DR   NMPDR; fig|10116.3.peg.7179; -.
DR   UCSC; NM_183325; rat.
DR   CTD; 141; -.
DR   RGD; 2052; Adprh.
DR   eggNOG; roNOG09199; -.
DR   GeneTree; ENSGT00530000063627; -.
DR   InParanoid; Q02589; -.
DR   OMA; HWSYFQD; -.
DR   OrthoDB; EOG4QJRNH; -.
DR   PhylomeDB; Q02589; -.
DR   NextBio; 606385; -.
DR   ArrayExpress; Q02589; -.
DR   Genevestigator; Q02589; -.
DR   GermOnline; ENSRNOG00000027260; Rattus norvegicus.
DR   GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IMP:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051725; P:protein de-ADP-ribosylation; IEA:InterPro.
DR   InterPro; IPR012108; ADP-ribosylarg_hydro.
DR   InterPro; IPR005502; Ribosyl_crysJ1.
DR   Pfam; PF03747; ADP_ribosyl_GH; 1.
DR   PIRSF; PIRSF016939; ADP_ribslarg_hdr; 1.
DR   SUPFAM; SSF101478; Ribosyl_crysJ1; 1.
DR   HOGENOMDNA; RAT11.PE442; -.
KW   ENSRNOG00000027260820036002503210000011;
KW   Adprh; ADPRH_RAT; BC082065; M86341;
KW   Complete proteome; Direct protein sequencing; Hydrolase; Magnesium;
KW   Reference proteome.
SQ   SEQUENCE   362 AA;  UNKNOWN MW;  UNKNOWN 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
//

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