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Q8CG72

- ARHL2_MOUSE

UniProt

Q8CG72 - ARHL2_MOUSE

Protein

Poly(ADP-ribose) glycohydrolase ARH3

Gene

Adprhl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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

    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

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

    GO - Biological processi

    1. cellular response to superoxide Source: MGI

    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 1 Publication. Mitochondrion matrix By similarity. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI
    4. nucleus Source: MGI

    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 – 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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 92 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