ID   ADPRH_HUMAN             Reviewed;         357 AA.
AC   P54922; B2R8H1; D3DN83;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-JAN-2012, entry version 92.
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; CH471052; EAW79563.1; -; 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; NM_001125.2.
DR   UniGene; Hs.99884; -.
DR   PDB; 3HFW; X-ray; 1.92 A; A=1-357.
DR   PDBsum; 3HFW; -.
DR   ProteinModelPortal; P54922; -.
DR   SMR; P54922; 1-357.
DR   MINT; MINT-7288433; -.
DR   STRING; P54922; -.
DR   PhosphoSite; P54922; -.
DR   DMDM; 1703392; -.
DR   OGP; P54922; -.
DR   PRIDE; P54922; -.
DR   Ensembl; ENST00000357003; ENSP00000349496; ENSG00000144843.
DR   Ensembl; ENST00000465513; ENSP00000417430; ENSG00000144843.
DR   Ensembl; ENST00000478399; ENSP00000420200; ENSG00000144843.
DR   Ensembl; ENST00000478927; ENSP00000417528; ENSG00000144843.
DR   GeneID; 141; -.
DR   KEGG; hsa:141; -.
DR   UCSC; uc003ecs.1; human.
DR   CTD; 141; -.
DR   GeneCards; GC03P119298; -.
DR   H-InvDB; HIX0030805; -.
DR   HGNC; HGNC:269; ADPRH.
DR   HPA; CAB001701; -.
DR   MIM; 603081; gene.
DR   neXtProt; NX_P54922; -.
DR   PharmGKB; PA24590; -.
DR   eggNOG; prNOG14273; -.
DR   GeneTree; ENSGT00530000063627; -.
DR   HOGENOM; HBG715225; -.
DR   HOVERGEN; HBG050462; -.
DR   InParanoid; P54922; -.
DR   OMA; HWSYFQD; -.
DR   OrthoDB; EOG4QJRNH; -.
DR   PhylomeDB; P54922; -.
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:InterPro.
DR   GO; GO:0051725; P:protein de-ADP-ribosylation; IEA:InterPro.
DR   InterPro; IPR012108; ADP-ribosylarg_hydro.
DR   InterPro; IPR005502; Ribosyl_crysJ1.
DR   KO; K01245; -.
DR   Pfam; PF03747; ADP_ribosyl_GH; 1.
DR   PIRSF; PIRSF016939; ADP_ribslarg_hdr; 1.
DR   SUPFAM; SSF101478; Ribosyl_crysJ1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Hydrolase; Magnesium;
KW   Reference proteome.
FT   CHAIN         1    357       [Protein ADP-ribosylarginine] hydrolase.
FT                                /FTId=PRO_0000157283.
FT   HELIX         2     12
FT   HELIX        32     39
FT   HELIX        55     69
FT   HELIX        76     90
FT   HELIX        91     93
FT   HELIX       103    109
FT   HELIX       132    134
FT   HELIX       145    147
FT   HELIX       148    157
FT   HELIX       173    183
FT   HELIX       188    190
FT   TURN        196    198
FT   HELIX       199    208
FT   HELIX       213    219
FT   HELIX       221    233
FT   HELIX       252    261
FT   HELIX       273    284
FT   HELIX       289    296
FT   HELIX       303    309
FT   HELIX       325    327
FT   TURN        328    330
FT   HELIX       334    346
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
//