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Q8CG72

- ARHL2_MOUSE

UniProt

Q8CG72 - ARHL2_MOUSE

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Protein

Poly(ADP-ribose) glycohydrolase ARH3

Gene
Adprhl2, Arh3
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

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 – 2601Substrate By similarity
Metal bindingi320 – 3201Magnesium 2
Metal bindingi322 – 3221Magnesium 1
Metal bindingi322 – 3221Magnesium 2
Metal bindingi323 – 3231Magnesium 2

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. poly(ADP-ribose) glycohydrolase activity Source: UniProtKB-EC
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: Chromosome 4

Organism-specific databases

MGIiMGI:2140364. Adprhl2.

Subcellular locationi

Cytoplasm. Mitochondrion matrix By similarity. Nucleus 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333Mitochondrion Reviewed predictionAdd
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 – 4319
Helixi44 – 463
Helixi54 – 629
Helixi83 – 9816
Helixi103 – 11614
Turni118 – 1214
Helixi124 – 13310
Helixi143 – 1464
Helixi148 – 1514
Helixi158 – 1614
Helixi164 – 1696
Helixi173 – 18513
Helixi191 – 20919
Helixi214 – 22815
Helixi232 – 2398
Turni240 – 2423
Helixi247 – 25913
Helixi266 – 2738
Beta strandi276 – 2783
Helixi279 – 2813
Helixi283 – 29210
Helixi306 – 31510
Helixi321 – 33616
Helixi338 – 3403
Helixi343 – 3464
Helixi352 – 36615

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTYX-ray1.80A/B25-369[»]
ProteinModelPortaliQ8CG72.
SMRiQ8CG72. Positions 25-369.

Miscellaneous databases

EvolutionaryTraceiQ8CG72.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1397.
GeneTreeiENSGT00390000015369.
HOGENOMiHOG000225333.
HOVERGENiHBG080863.
InParanoidiA3KFY3.
KOiK11687.
OMAiYKKDPDR.
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. Align

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

MAVAAAAAAT AMSAAGGGGA SAARSISRFR GCLAGALLGD CVGAVYEAHD    50
TVSLASVLSH VESLEPDPGT PGSARTETLY YTDDTAMTRA LVQSLLAKEA 100
FDEVDMAHRF AQEYKKDPDR GYGAGVITVF KKLLNPKCRD VYEPARAQFN 150
GKGSYGNGGA MRVAGISLAY SSVQDVQKFA RLSAQLTHAS SLGYNGAILQ 200
ALAVHLALQG VSSSEHFLEQ LLGHMEELEG DAQSVLDAKE LGMEERPYSS 250
RLKKVGELLD QDVVSREEVV SELGNGIAAF ESVPTAIYCF LRCMEPHPEI 300
PSTFNSLQRT LIYSISLGGD TDTIATMAGA IAGAYYGMEQ VPESWQQSCE 350
GFEETDVLAQ SLHRVFQESS 370
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8686Missing in isoform 2. VSP_023037Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771E → Q in AAH23177. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18650.1. [Q8CG72-1 ]
RefSeqi NP_598644.1. NM_133883.2. [Q8CG72-1 ]
UniGenei Mm.11285.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QTY X-ray 1.80 A/B 25-369 [» ]
ProteinModelPortali Q8CG72.
SMRi Q8CG72. Positions 25-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8CG72. 1 interaction.
MINTi MINT-4383260.
STRINGi 10090.ENSMUSP00000099677.

PTM databases

PhosphoSitei Q8CG72.

Proteomic databases

MaxQBi Q8CG72.
PaxDbi Q8CG72.
PRIDEi Q8CG72.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102617 ; ENSMUSP00000099677 ; ENSMUSG00000042558 . [Q8CG72-1 ]
GeneIDi 100206.
KEGGi mmu:100206.
UCSCi uc008ute.1. mouse. [Q8CG72-1 ]

Organism-specific databases

CTDi 54936.
MGIi MGI:2140364. Adprhl2.

Phylogenomic databases

eggNOGi COG1397.
GeneTreei ENSGT00390000015369.
HOGENOMi HOG000225333.
HOVERGENi HBG080863.
InParanoidi A3KFY3.
KOi K11687.
OMAi YKKDPDR.
OrthoDBi EOG7D2FFB.
PhylomeDBi Q8CG72.
TreeFami TF324754.

Enzyme and pathway databases

BRENDAi 3.2.1.143. 3474.

Miscellaneous databases

EvolutionaryTracei Q8CG72.
NextBioi 354321.
PROi Q8CG72.
SOURCEi Search...

Gene expression databases

Bgeei Q8CG72.
CleanExi MM_ADPRHL2.
Genevestigatori Q8CG72.

Family and domain databases

InterProi IPR005502. Ribosyl_crysJ1.
[Graphical view ]
Pfami PF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view ]
SUPFAMi SSF101478. SSF101478. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 91 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

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