ID   ADPRH_HUMAN             Reviewed;         357 AA.
AC   P54922; B2R8H1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-NOV-2009, entry version 74.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
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 [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
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DR   EMBL; L13291; AAA35555.1; -; mRNA.
DR   EMBL; AK313369; BAG36168.1; -; mRNA.
DR   EMBL; CH471052; EAW79562.1; -; Genomic_DNA.
DR   EMBL; BC063883; AAH63883.1; -; mRNA.
DR   EMBL; BC074769; AAH74769.1; -; mRNA.
DR   IPI; IPI00009258; -.
DR   PIR; B47411; B47411.
DR   RefSeq; NP_001116.1; -.
DR   UniGene; Hs.99884; -.
DR   STRING; P54922; -.
DR   PhosphoSite; P54922; -.
DR   OGP; P54922; -.
DR   PRIDE; P54922; -.
DR   Ensembl; ENST00000357003; ENSP00000349496; ENSG00000144843; Homo sapiens.
DR   Ensembl; ENST00000451955; ENSP00000413806; ENSG00000144843; Homo sapiens.
DR   GeneID; 141; -.
DR   KEGG; hsa:141; -.
DR   UCSC; uc003ecs.1; human.
DR   CTD; 141; -.
DR   GeneCards; GC03P120781; -.
DR   H-InvDB; HIX0030805; -.
DR   HGNC; HGNC:269; ADPRH.
DR   HPA; CAB001701; -.
DR   MIM; 603081; gene.
DR   PharmGKB; PA24590; -.
DR   HOGENOM; P54922; -.
DR   HOVERGEN; P54922; -.
DR   OMA; IPFNSHE; -.
DR   BRENDA; 3.2.2.19; 247.
DR   NextBio; 561; -.
DR   ArrayExpress; P54922; -.
DR   Bgee; P54922; -.
DR   CleanEx; HS_ADPRH; -.
DR   Genevestigator; P54922; -.
DR   GermOnline; ENSG00000144843; Homo sapiens.
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   1: Evidence at protein level;
KW   Complete proteome; Hydrolase; Magnesium.
FT   CHAIN         1    357       [Protein ADP-ribosylarginine] hydrolase.
FT                                /FTId=PRO_0000157283.
SQ   SEQUENCE   357 AA;  39507 MW;  4E23B12FAE84F12B CRC64;
     MEKYVAAMVL SAAGDALGYY NGKWEFLQDG EKIHRQLAQL GGLDALDVGR WRVSDDTVMH
     LATAEALVEA GKAPKLTQLY YLLAKHYQDC MEDMDGRAPG GASVHNAMQL KPGKPNGWRI
     PFNSHEGGCG AAMRAMCIGL RFPHHSQLDT LIQVSIESGR MTHHHPTGYL GALASALFTA
     YAVNSRPPLQ WGKGLMELLP EAKKYIVQSG YFVEENLQHW SYFQTKWENY LKLRGILDGE
     SAPTFPESFG VKERDQFYTS LSYSGWGGSS GHDAPMIAYD AVLAAGDSWK ELAHRAFFHG
     GDSDSTAAIA GCWWGVMYGF KGVSPSNYEK LEYRNRLEET ARALYSLGSK EDTVISL
//