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UniProtKB/Swiss-Prot entry Q8CG72


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARHL2_MOUSE
Primary accession number Q8CG72
Secondary accession numbers Q80UW9 Q8R575 Q921U6
Integrated into Swiss-Prot on February 6, 2007
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 51)
Name and origin of the protein
Protein name Poly(ADP-ribose) glycohydrolase ARH3
Synonyms EC 3.2.1.143
ADP-ribosylhydrolase 3
[Protein ADP-ribosylarginine] hydrolase-like protein 2
Gene name
Name: Adprhl2
Synonyms: Arh3
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
DOI=10.1110/ps.0200602; PubMed=12070318 [NCBI, ExPASy, EBI, Israel, Japan]
Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P., Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.;
"The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse.";
Protein Sci. 11:1657-1670(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD;
TISSUE=Kidney, Liver, and Spleen;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=FVB/N-3;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M510290200; PubMed=16278211 [NCBI, ExPASy, EBI, Israel, Japan]
Oka S., Kato J., Moss J.;
"Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase.";
J. Biol. Chem. 281:705-713(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ427296; CAD20317.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK143583; BAE25451.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK147034; BAE27626.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169070; BAE40857.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK171780; BAE42660.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010639; AAH10639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023177; AAH23177.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC045203; AAH45203.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00322267; -.
IPI00828376; -.
RefSeq NP_598644.1; -.
UniGene Mm.11285
3D structure databases
PDB
2QTY; X-ray; 1.80 A; A/B=25-369.[ExPASy / RCSB / EBI]
PDBsum 2QTY; -.
ModBase Q8CG72.
Enzyme and pathway databases
BRENDA 3.2.1.143; 244.
Organism-specific databases
MGI MGI:2140364; Adprhl2.
Gene expression databases
ArrayExpress Q8CG72; -.
Bgee Q8CG72; -.
CleanEx MM_ADPRHL2; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004649; Molecular function: poly(ADP-ribose) glycohydrolase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR005502; Ribosyl_crysJ1.
Graphical view of domain structure.
Pfam PF03747; ADP_ribosyl_GH; 1.
Pfam graphical view of domain structure.
Genome annotation databases
Ensembl ENSMUSG00000042558; Mus musculus. [Contig view]
GeneID 100206; -.
KEGG mmu:100206; -.
Phylogenomic databases
HOVERGEN Q8CG72; -.
OMA Q8CG72; DTIASMA.
Other
NextBio 354321; -.
SOURCE Adprhl2; Mus musculus.
ProtoNet Q8CG72.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   370  370     Poly(ADP-ribose) glycohydrolase ARH3. PRO_0000277614
COMPBIAS   2    11  10     Poly-Ala. 
COMPBIAS   16    19  4     Poly-Gly. 
METAL   47    47        Magnesium 2 (By similarity). 
METAL   82    82        Magnesium 1 (By similarity). 
METAL   83    83        Magnesium 1 (By similarity). 
METAL   84    84        Magnesium 1 (By similarity). 
METAL   320   320        Magnesium 2 (By similarity). 
METAL   322   322        Magnesium 1 (By similarity). 
METAL   322   322        Magnesium 2 (By similarity). 
METAL   323   323        Magnesium 2 (By similarity). 
VAR_SEQ   1    86        Missing (in isoform 2). VSP_023037
CONFLICT   77    77        E -> Q (in Ref. 3; AAH23177). 
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 39414 Da [This is the MW of the unprocessed precursor] CRC64: 3251113C67432A8D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVAAAAAAT AMSAAGGGGA SAARSISRFR GCLAGALLGD CVGAVYEAHD TVSLASVLSH 

        70         80         90        100        110        120 
VESLEPDPGT PGSARTETLY YTDDTAMTRA LVQSLLAKEA FDEVDMAHRF AQEYKKDPDR 

       130        140        150        160        170        180 
GYGAGVITVF KKLLNPKCRD VYEPARAQFN GKGSYGNGGA MRVAGISLAY SSVQDVQKFA 

       190        200        210        220        230        240 
RLSAQLTHAS SLGYNGAILQ ALAVHLALQG VSSSEHFLEQ LLGHMEELEG DAQSVLDAKE 

       250        260        270        280        290        300 
LGMEERPYSS RLKKVGELLD QDVVSREEVV SELGNGIAAF ESVPTAIYCF LRCMEPHPEI 

       310        320        330        340        350        360 
PSTFNSLQRT LIYSISLGGD TDTIATMAGA IAGAYYGMEQ VPESWQQSCE GFEETDVLAQ 

       370 
SLHRVFQESS 

Q8CG72 in FASTA format

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