Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5ZI51 (ARHL2_CHICK)

Last modified September 1, 2009. Version 29. 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

Hide | Top

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: RCJMB04_30e5
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Hide | Top

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Hide | Top

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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Poly(ADP-ribose) glycohydrolase ARH3
PRO_0000277615

Sites

Metal binding411Magnesium 2 By similarity
Metal binding791Magnesium 1 By similarity
Metal binding801Magnesium 1 By similarity
Metal binding811Magnesium 1 By similarity
Metal binding3171Magnesium 2 By similarity
Metal binding3201Magnesium 2 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q5ZI51-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 605113FC6622FF89

FASTA36739,909
        10         20         30         40         50         60 
MAAAGAGSGR AAVSRSRPPP ARFRGCLAGA LLGDCLGAVF EGRSVVKLPD LLSFLRGLEP 

        70         80         90        100        110        120 
PGGEGEPAGS ARRETLSYTD DTAMSRCVVQ SLLAKREFDE VDMAKRFAEE YKKEPNRGYG 

       130        140        150        160        170        180 
MAVVNVFKKL LSPQCSDVFE PARAQFNGKG SYGNGGAMRV AGIPLTYSDV QDVKKFAKLS 

       190        200        210        220        230        240 
AELTHANSLG YNGAILQALA VHLALQGEVS RETFLEQLIS HMEDIEADDK SLTDARALGF 

       250        260        270        280        290        300 
EDLPFSRRLK KIKEFLELSS VPKEDVLFEL GNGIAALRSV PTAIYSFLRC MEADPDIPEH 

       310        320        330        340        350        360 
YNNLQRTIIY CISLGGDTNT IATMAGAIAG AYYGEEQVPP SWEQSCEAFQ ETQKMANSLH 


ELYCQQL

« Hide

Hide | Top

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005) [PubMed: 15642098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Hide | Top

Cross-references

Sequence databases

AJ720933 mRNA. Translation: CAG32592.1.
IPIIPI00587371.
RefSeqNP_001006312.1.
UniGeneGga.42574

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSGALT00000003624; ENSGALP00000003617; ENSGALG00000002304; Gallus gallus. [Genome view]
GeneID419626.
KEGGgga:419626.

Organism-specific databases

CTD419626.

Phylogenomic databases

HOVERGENQ5ZI51.

Enzyme and pathway databases

BRENDA3.2.1.143. 4.

Family and domain databases

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

Hide | Top

Entry information

Entry nameARHL2_CHICK
AccessionPrimary (citable) accession number: Q5ZI51
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: November 23, 2004
Last modified: September 1, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Hide | Top

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