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Q5ZI51 (ARHL2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
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

Binds 2 magnesium ions per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the ADP-ribosylglycohydrolase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal 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 – 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

Sequences

Sequence LengthMass (Da)Tools
Q5ZI51 [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

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:R6.1-R6.9(2005) [PubMed: 15642098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ720933 mRNA. Translation: CAG32592.1.
IPIIPI00587371.
RefSeqNP_001006312.1. NM_001006312.1.
UniGeneGga.42574.

3D structure databases

HSSPHSSP built from PDB template 2CWC based on UniProtKB Q5SMG9.
ProteinModelPortalQ5ZI51.
SMRQ5ZI51. Positions 21-363.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID419626.
KEGGgga:419626.

Organism-specific databases

CTD54936.

Phylogenomic databases

eggNOGveNOG05984.
GeneTreeENSGT00390000015369.
HOGENOMHBG444652.
HOVERGENHBG080863.
InParanoidQ5ZI51.
OrthoDBEOG466VMC.
PhylomeDBQ5ZI51.

Family and domain databases

InterProIPR005502. Ribosyl_crysJ1.
[Graphical view]
KOK11687.
PfamPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMSSF101478. Ribosyl_crysJ1. 1 hit.
ProtoNetSearch...

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: December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families