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Protein

Poly(ADP-ribose) glycohydrolase ARH3

Gene

Adprhl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Due to catalytic inactivity of PARG mitochondrial isoforms, ARH3 is the only PAR hydrolyzing enzyme in mitochondria (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Magnesium 2
Metal bindingi82 – 821Magnesium 1
Metal bindingi83 – 831Magnesium 1
Metal bindingi84 – 841Magnesium 1
Binding sitei260 – 2601SubstrateBy similarity
Metal bindingi320 – 3201Magnesium 2
Metal bindingi322 – 3221Magnesium 1
Metal bindingi322 – 3221Magnesium 2
Metal bindingi323 – 3231Magnesium 2

GO - Molecular functioni

GO - Biological processi

  • cellular response to superoxide Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.143. 3474.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Adprhl2
Synonyms:Arh3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2140364. Adprhl2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 370337Poly(ADP-ribose) glycohydrolase ARH3PRO_0000277614Add
BLAST

Proteomic databases

MaxQBiQ8CG72.
PaxDbiQ8CG72.
PRIDEiQ8CG72.

PTM databases

PhosphoSiteiQ8CG72.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8CG72.
CleanExiMM_ADPRHL2.
GenevestigatoriQ8CG72.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiQ8CG72. 1 interaction.
MINTiMINT-4383260.
STRINGi10090.ENSMUSP00000099677.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 4319Combined sources
Helixi44 – 463Combined sources
Helixi54 – 629Combined sources
Helixi83 – 9816Combined sources
Helixi103 – 11614Combined sources
Turni118 – 1214Combined sources
Helixi124 – 13310Combined sources
Helixi143 – 1464Combined sources
Helixi148 – 1514Combined sources
Helixi158 – 1614Combined sources
Helixi164 – 1696Combined sources
Helixi173 – 18513Combined sources
Helixi191 – 20919Combined sources
Helixi214 – 22815Combined sources
Helixi232 – 2398Combined sources
Turni240 – 2423Combined sources
Helixi247 – 25913Combined sources
Helixi266 – 2738Combined sources
Beta strandi276 – 2783Combined sources
Helixi279 – 2813Combined sources
Helixi283 – 29210Combined sources
Helixi306 – 31510Combined sources
Helixi321 – 33616Combined sources
Helixi338 – 3403Combined sources
Helixi343 – 3464Combined sources
Helixi352 – 36615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTYX-ray1.80A/B25-369[»]
ProteinModelPortaliQ8CG72.
SMRiQ8CG72. Positions 25-369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CG72.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 1110Poly-Ala
Compositional biasi16 – 194Poly-Gly

Sequence similaritiesi

Belongs to the ADP-ribosylglycohydrolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1397.
GeneTreeiENSGT00390000015369.
HOGENOMiHOG000225333.
HOVERGENiHBG080863.
InParanoidiQ8CG72.
KOiK11687.
OMAiTEALYYT.
OrthoDBiEOG7D2FFB.
PhylomeDBiQ8CG72.
TreeFamiTF324754.

Family and domain databases

InterProiIPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMiSSF101478. SSF101478. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CG72-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAVAAAAAAT AMSAAGGGGA SAARSISRFR GCLAGALLGD CVGAVYEAHD
60 70 80 90 100
TVSLASVLSH VESLEPDPGT PGSARTETLY YTDDTAMTRA LVQSLLAKEA
110 120 130 140 150
FDEVDMAHRF AQEYKKDPDR GYGAGVITVF KKLLNPKCRD VYEPARAQFN
160 170 180 190 200
GKGSYGNGGA MRVAGISLAY SSVQDVQKFA RLSAQLTHAS SLGYNGAILQ
210 220 230 240 250
ALAVHLALQG VSSSEHFLEQ LLGHMEELEG DAQSVLDAKE LGMEERPYSS
260 270 280 290 300
RLKKVGELLD QDVVSREEVV SELGNGIAAF ESVPTAIYCF LRCMEPHPEI
310 320 330 340 350
PSTFNSLQRT LIYSISLGGD TDTIATMAGA IAGAYYGMEQ VPESWQQSCE
360 370
GFEETDVLAQ SLHRVFQESS
Length:370
Mass (Da):39,414
Last modified:March 1, 2003 - v1
Checksum:i3251113C67432A8D
GO
Isoform 2 (identifier: Q8CG72-2) [UniParc]FASTAAdd to basket

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

Show »
Length:284
Mass (Da):31,043
Checksum:i01B66A15E6625CBF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771E → Q in AAH23177 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8686Missing in isoform 2. 1 PublicationVSP_023037Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18650.1. [Q8CG72-1]
RefSeqiNP_598644.1. NM_133883.2. [Q8CG72-1]
UniGeneiMm.11285.

Genome annotation databases

EnsembliENSMUST00000102617; ENSMUSP00000099677; ENSMUSG00000042558. [Q8CG72-1]
GeneIDi100206.
KEGGimmu:100206.
UCSCiuc008ute.1. mouse. [Q8CG72-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18650.1. [Q8CG72-1]
RefSeqiNP_598644.1. NM_133883.2. [Q8CG72-1]
UniGeneiMm.11285.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTYX-ray1.80A/B25-369[»]
ProteinModelPortaliQ8CG72.
SMRiQ8CG72. Positions 25-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CG72. 1 interaction.
MINTiMINT-4383260.
STRINGi10090.ENSMUSP00000099677.

PTM databases

PhosphoSiteiQ8CG72.

Proteomic databases

MaxQBiQ8CG72.
PaxDbiQ8CG72.
PRIDEiQ8CG72.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102617; ENSMUSP00000099677; ENSMUSG00000042558. [Q8CG72-1]
GeneIDi100206.
KEGGimmu:100206.
UCSCiuc008ute.1. mouse. [Q8CG72-1]

Organism-specific databases

CTDi54936.
MGIiMGI:2140364. Adprhl2.

Phylogenomic databases

eggNOGiCOG1397.
GeneTreeiENSGT00390000015369.
HOGENOMiHOG000225333.
HOVERGENiHBG080863.
InParanoidiQ8CG72.
KOiK11687.
OMAiTEALYYT.
OrthoDBiEOG7D2FFB.
PhylomeDBiQ8CG72.
TreeFamiTF324754.

Enzyme and pathway databases

BRENDAi3.2.1.143. 3474.

Miscellaneous databases

EvolutionaryTraceiQ8CG72.
NextBioi354321.
PROiQ8CG72.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CG72.
CleanExiMM_ADPRHL2.
GenevestigatoriQ8CG72.

Family and domain databases

InterProiIPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMiSSF101478. SSF101478. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Kidney, Liver and Spleen.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-369, SUBUNIT, COFACTOR, MAGNESIUM-BINDING SITES.

Entry informationi

Entry nameiARHL2_MOUSE
AccessioniPrimary (citable) accession number: Q8CG72
Secondary accession number(s): A3KFY3
, Q80UW9, Q8R575, Q921U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: March 1, 2003
Last modified: May 27, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.