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Q3SYV9 (ARHL2_BOVIN) 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length365 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 – 365365Poly(ADP-ribose) glycohydrolase ARH3
PRO_0000277612

Regions

Compositional bias2 – 65Poly-Ala

Sites

Metal binding421Magnesium 2 By similarity
Metal binding771Magnesium 1 By similarity
Metal binding781Magnesium 1 By similarity
Metal binding791Magnesium 1 By similarity
Metal binding3151Magnesium 2 By similarity
Metal binding3171Magnesium 1 By similarity
Metal binding3171Magnesium 2 By similarity
Metal binding3181Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SYV9 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 59F65453AABF2802

FASTA36539,221
        10         20         30         40         50         60 
MAAAAAMTAA GCGGAGAARS LSRFRGCLAG ALLGDCVGAV YEARDTVDLT SVLRQVQDLE 

        70         80         90        100        110        120 
PDPGSPGSAR TEALCYTDDT AMARALVQSL LAKEAFDEVD MAHRFAQEYK KDPDRGYGAG 

       130        140        150        160        170        180 
VITVFRKHLS PRCRDVFEPA RAQFNGKGSY GNGGAMRVAG ISLAYSSVQD VQKFARLSAQ 

       190        200        210        220        230        240 
LTHASSLGYN GAILQALAVH LALQGESSSE HFLEQLLGHM EELESDAQSV LDARELGMEE 

       250        260        270        280        290        300 
RPYSSRLKKI GELLEQDSVT REEVVSELGN GIAAFESVPT AIYCFLRCME PDPEIPSTFN 

       310        320        330        340        350        360 
SLQRTLVYSI SLGGDTDTIA TMAGAIAGAY YGMEQVPESW QQSCEGYEET DVLAQSLHRV 


FQKSL 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC103360 mRNA. Translation: AAI03361.1.
IPIIPI00692404.
RefSeqNP_001030417.1. NM_001035340.1.
UniGeneBt.51810.

3D structure databases

HSSPHSSP built from PDB template 2CWC based on UniProtKB Q5SMG9.
ProteinModelPortalQ3SYV9.
SMRQ3SYV9. Positions 19-364.
ModBaseSearch...

Proteomic databases

PRIDEQ3SYV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID521650.
KEGGbta:521650.

Organism-specific databases

CTD54936.

Phylogenomic databases

eggNOGmaNOG05037.
GeneTreeENSGT00390000015369.
HOVERGENHBG080863.
InParanoidQ3SYV9.
OrthoDBEOG466VMC.
PhylomeDBQ3SYV9.

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_BOVIN
AccessionPrimary (citable) accession number: Q3SYV9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 11, 2005
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