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Q8CG72 (ARHL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(ADP-ribose) glycohydrolase ARH3
EC=3.2.1.143
Alternative name(s):
ADP-ribosylhydrolase 3
[Protein ADP-ribosylarginine] hydrolase-like protein 2
Gene names
Name:Adprhl2
Synonyms:Arh3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells. Generates ADP-ribose from poly-(ADP-ribose), but does not hydrolyze ADP-ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds By similarity.

Catalytic activity

Hydrolyzes poly(ADP-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-ribose.

Cofactor

Binds 2 magnesium ions per subunit. Ref.6

Subunit structure

Monomer. Ref.6

Subcellular location

Cytoplasm. Nucleus Ref.5.

Tissue specificity

Ubiquitous. Ref.5

Sequence similarities

Belongs to the ADP-ribosylglycohydrolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(ADP-ribose) glycohydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CG72-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8CG72-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Poly(ADP-ribose) glycohydrolase ARH3
PRO_0000277614

Regions

Compositional bias2 – 1110Poly-Ala
Compositional bias16 – 194Poly-Gly

Sites

Metal binding471Magnesium 2
Metal binding821Magnesium 1
Metal binding831Magnesium 1
Metal binding841Magnesium 1
Metal binding3201Magnesium 2
Metal binding3221Magnesium 1
Metal binding3221Magnesium 2
Metal binding3231Magnesium 2

Natural variations

Alternative sequence1 – 8686Missing in isoform 2.
VSP_023037

Experimental info

Sequence conflict771E → Q in AAH23177. Ref.4

Secondary structure

1 ............................................ 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3251113C67432A8D

FASTA37039,414
        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

« Hide

Isoform 2 [UniParc].

Checksum: 01B66A15E6625CBF
Show »

FASTA28431,043

References

« Hide 'large scale' references
[1]"The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse."
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.
Protein Sci. 11:1657-1670(2002) [PubMed: 12070318] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6J.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Kidney, Liver and Spleen.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: FVB/N-3.
Tissue: Mammary gland.
[5]"Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase."
Oka S., Kato J., Moss J.
J. Biol. Chem. 281:705-713(2006) [PubMed: 16278211] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Structure of mouse ADP-ribosylhydrolase 3 (mARH3)."
Mueller-Dieckmann C., Kernstock S., Mueller-Dieckmann J., Weiss M.S., Koch-Nolte F.
Acta Crystallogr. F 64:156-162(2008) [PubMed: 18323597] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-369, SUBUNIT, COFACTOR, MAGNESIUM-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ427296 mRNA. Translation: CAD20317.1.
AK143583 mRNA. Translation: BAE25451.1.
AK147034 mRNA. Translation: BAE27626.1.
AK169070 mRNA. Translation: BAE40857.1.
AK171780 mRNA. Translation: BAE42660.1.
AL606976 Genomic DNA. Translation: CAM45877.1.
BC010639 mRNA. Translation: AAH10639.1.
BC023177 mRNA. Translation: AAH23177.2.
BC045203 mRNA. Translation: AAH45203.1.
IPIIPI00322267.
IPI00828376.
RefSeqNP_598644.1. NM_133883.2.
UniGeneMm.11285.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTYX-ray1.80A/B25-369[»]
ProteinModelPortalQ8CG72.
SMRQ8CG72. Positions 25-369.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8CG72.

PTM databases

PhosphoSiteQ8CG72.

Proteomic databases

PRIDEQ8CG72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102617; ENSMUSP00000099677; ENSMUSG00000042558.
GeneID100206.
KEGGmmu:100206.
UCSCuc008ute.1. mouse.

Organism-specific databases

CTD54936.
MGIMGI:2140364. Adprhl2.

Phylogenomic databases

GeneTreeENSGT00390000015369.
HOGENOMHBG444652.
HOVERGENHBG080863.
InParanoidQ8CG72.
OMAEPARAQF.
PhylomeDBQ8CG72.

Enzyme and pathway databases

BRENDA3.2.1.143. 3474.

Gene expression databases

ArrayExpressQ8CG72.
BgeeQ8CG72.
CleanExMM_ADPRHL2.
GenevestigatorQ8CG72.

Family and domain databases

InterProIPR005502. Ribosyl_crysJ1.
[Graphical view]
KOK11687.
PfamPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMSSF101478. Ribosyl_crysJ1. 1 hit.
ProtoNetSearch...

Other

NextBio354321.
SOURCESearch...

Entry information

Entry nameARHL2_MOUSE
AccessionPrimary (citable) accession number: Q8CG72
Secondary accession number(s): A3KFY3 expand/collapse secondary AC list , Q80UW9, Q8R575, Q921U6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: March 1, 2003
Last modified: December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents