ID   ARHL2_MOUSE             Reviewed;         370 AA.
AC   Q8CG72; A3KFY3; Q80UW9; Q8R575; Q921U6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-NOV-2009, entry version 55.
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   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] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22065832; PubMed=12070318; DOI=10.1110/ps.0200602;
RA   Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P.,
RA   Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.;
RT   "The family of toxin-related ecto-ADP-ribosyltransferases in humans
RT   and the mouse.";
RL   Protein Sci. 11:1657-1670(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Liver, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
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).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16278211; DOI=10.1074/jbc.M510290200;
RA   Oka S., Kato J., Moss J.;
RT   "Identification and characterization of a mammalian 39-kDa poly(ADP-
RT   ribose) glycohydrolase.";
RL   J. Biol. Chem. 281:705-713(2006).
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. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CG72-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CG72-2; Sequence=VSP_023037;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
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; AJ427296; CAD20317.1; -; mRNA.
DR   EMBL; AK143583; BAE25451.1; -; mRNA.
DR   EMBL; AK147034; BAE27626.1; -; mRNA.
DR   EMBL; AK169070; BAE40857.1; -; mRNA.
DR   EMBL; AK171780; BAE42660.1; -; mRNA.
DR   EMBL; AL606976; CAM45877.1; -; Genomic_DNA.
DR   EMBL; BC010639; AAH10639.1; -; mRNA.
DR   EMBL; BC023177; AAH23177.2; -; mRNA.
DR   EMBL; BC045203; AAH45203.1; -; mRNA.
DR   IPI; IPI00322267; -.
DR   IPI; IPI00828376; -.
DR   RefSeq; NP_598644.1; -.
DR   UniGene; Mm.11285; -.
DR   PDB; 2QTY; X-ray; 1.80 A; A/B=25-369.
DR   PDBsum; 2QTY; -.
DR   STRING; Q8CG72; -.
DR   PRIDE; Q8CG72; -.
DR   Ensembl; ENSMUST00000102617; ENSMUSP00000099677; ENSMUSG00000042558; Mus musculus.
DR   GeneID; 100206; -.
DR   KEGG; mmu:100206; -.
DR   UCSC; uc008ute.1; mouse.
DR   CTD; 100206; -.
DR   MGI; MGI:2140364; Adprhl2.
DR   HOVERGEN; Q8CG72; -.
DR   OMA; DTIASMA; -.
DR   BRENDA; 3.2.1.143; 244.
DR   NextBio; 354321; -.
DR   ArrayExpress; Q8CG72; -.
DR   Bgee; Q8CG72; -.
DR   CleanEx; MM_ADPRHL2; -.
DR   Genevestigator; Q8CG72; -.
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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Magnesium;
KW   Metal-binding; Nucleus.
FT   CHAIN         1    370       Poly(ADP-ribose) glycohydrolase ARH3.
FT                                /FTId=PRO_0000277614.
FT   COMPBIAS      2     11       Poly-Ala.
FT   COMPBIAS     16     19       Poly-Gly.
FT   METAL        47     47       Magnesium 2 (By similarity).
FT   METAL        82     82       Magnesium 1 (By similarity).
FT   METAL        83     83       Magnesium 1 (By similarity).
FT   METAL        84     84       Magnesium 1 (By similarity).
FT   METAL       320    320       Magnesium 2 (By similarity).
FT   METAL       322    322       Magnesium 1 (By similarity).
FT   METAL       322    322       Magnesium 2 (By similarity).
FT   METAL       323    323       Magnesium 2 (By similarity).
FT   VAR_SEQ       1     86       Missing (in isoform 2).
FT                                /FTId=VSP_023037.
FT   CONFLICT     77     77       E -> Q (in Ref. 4; AAH23177).
FT   HELIX        25     29
FT   TURN         45     48
FT   HELIX        54     62
FT   HELIX        83     98
FT   HELIX       103    116
FT   HELIX       127    133
FT   HELIX       143    146
FT   TURN        147    149
FT   TURN        167    169
FT   HELIX       173    185
FT   HELIX       198    208
FT   HELIX       214    221
FT   HELIX       225    228
FT   HELIX       232    239
FT   HELIX       247    254
FT   HELIX       266    272
FT   HELIX       279    281
FT   HELIX       283    292
FT   HELIX       306    315
FT   HELIX       321    327
FT   HELIX       343    346
FT   HELIX       353    366
SQ   SEQUENCE   370 AA;  39414 MW;  3251113C67432A8D CRC64;
     MAVAAAAAAT AMSAAGGGGA SAARSISRFR GCLAGALLGD CVGAVYEAHD TVSLASVLSH
     VESLEPDPGT PGSARTETLY YTDDTAMTRA LVQSLLAKEA FDEVDMAHRF AQEYKKDPDR
     GYGAGVITVF KKLLNPKCRD VYEPARAQFN GKGSYGNGGA MRVAGISLAY SSVQDVQKFA
     RLSAQLTHAS SLGYNGAILQ ALAVHLALQG VSSSEHFLEQ LLGHMEELEG DAQSVLDAKE
     LGMEERPYSS RLKKVGELLD QDVVSREEVV SELGNGIAAF ESVPTAIYCF LRCMEPHPEI
     PSTFNSLQRT LIYSISLGGD TDTIATMAGA IAGAYYGMEQ VPESWQQSCE GFEETDVLAQ
     SLHRVFQESS
//