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Reviewed, UniProtKB/Swiss-Prot Q66HT8 (ARHL2_DANRE)

Last modified July 28, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
ORF Names: zgc:92867
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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

Magnesium By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the ADP-ribosylglycohydrolase family.

Sequence caution

The sequence AAH81683.1 differs from that shown. Reason: Miscellaneous discrepancy. Unlikely isoform. Aberrant splice sites.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(ADP-ribose) glycohydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Poly(ADP-ribose) glycohydrolase ARH3
PRO_0000277616

Sites

Metal binding351Magnesium 2 By similarity
Metal binding651Magnesium 1 By similarity
Metal binding661Magnesium 1 By similarity
Metal binding671Magnesium 1 By similarity
Metal binding3041Magnesium 2 By similarity
Metal binding3061Magnesium 1 By similarity
Metal binding3061Magnesium 2 By similarity
Metal binding3071Magnesium 2 By similarity

Experimental info

Sequence conflict3451R → H in AAI52162. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q66HT8-1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: FC07F4F67AB7B784

FASTA37040,103
        10         20         30         40         50         60 
MSAAARVVAP VMMLSRFRGA LVGSVLGDCI GGEFEGAVDV PLDRVLQHLS ALEDDTRGDG 

        70         80         90        100        110        120 
ILQYSDDTAM MRCVADSLLT RMTFDERDMA QRFAKEYSHS PGRGYGSGVV QVLRKLASPH 

       130        140        150        160        170        180 
LKDVFQPAQA QFGGRGSFGN GGAMRAVPFA LAFRSRADVR KYSRFGAMLT HSCSLGYNGA 

       190        200        210        220        230        240 
ALQALAVHLS LQGALALPKD FIDKLISEME ELEKDETAKH DAKALNLSEF PYCSRLHRVK 

       250        260        270        280        290        300 
ELMDKTSVSI EEVISELGNG IAALQSVPTA IFCVLYCLEP QDGLPERFGG LERTIAYSLA 

       310        320        330        340        350        360 
LGGDTDTIAC MAGAIAGAHY GIDSIPLSWQ VSCEGVDEAD DLARRLYDLY CLPQHNEDRG 

       370 
NNQPHTTNTD 

« Hide

References

[1]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Ovary.

Cross-references

Sequence databases

BC081683 mRNA. Translation: AAH81683.1. Sequence problems.
BC152161 mRNA. Translation: AAI52162.1.
IPIIPI00772976.
RefSeqNP_001004565.1.
UniGeneDr.148637
Dr.80280

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSDART00000011706; ENSDARP00000027022; ENSDARG00000019338; Danio rerio. [Genome view]
GeneID796446.
KEGGdre:796446.

Organism-specific databases

ZFINZDB-GENE-040912-85. zgc:92867.

Phylogenomic databases

HOVERGENQ66HT8.

Enzyme and pathway databases

BRENDA3.2.1.143. 96826.

Gene expression databases

ArrayExpressQ66HT8.
BgeeQ66HT8.

Family and domain databases

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

Entry information

Entry nameARHL2_DANRE
AccessionPrimary (citable) accession number: Q66HT8
Secondary accession number(s): A7MCF6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: September 2, 2008
Last modified: July 28, 2009
This is version 39 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectZebrafish annotation project

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents