Reviewed, UniProtKB/Swiss-Prot Q8CG72 (ARHL2_MOUSE)

Names and origin

Protein names

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 names

Name:	Adprhl2
Synonyms:	Arh3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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. Nucleus. Ref.4
Tissue specificity	Ubiquitous. Ref.4
Sequence similarities	Belongs to the ADP-ribosylglycohydrolase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW poly(ADP-ribose) glycohydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8CG72-1)

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.

Isoform 2 (identifier: Q8CG72-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 370	370	Poly(ADP-ribose) glycohydrolase ARH3		PRO_0000277614
Regions
	Compositional bias	2 – 11	10	Poly-Ala
	Compositional bias	16 – 19	4	Poly-Gly
Sites
	Metal binding	47	1	Magnesium 2 By similarity
	Metal binding	82	1	Magnesium 1 By similarity
	Metal binding	83	1	Magnesium 1 By similarity
	Metal binding	84	1	Magnesium 1 By similarity
	Metal binding	320	1	Magnesium 2 By similarity
	Metal binding	322	1	Magnesium 1 By similarity
	Metal binding	322	1	Magnesium 2 By similarity
	Metal binding	323	1	Magnesium 2 By similarity
Natural variations
	Alternative sequence	1 – 86	86	Missing in isoform 2.		VSP_023037
Experimental info
	Sequence conflict	77	1	E → Q in AAH23177. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 3251113C67432A8D	FASTA	370	39,414
	10 20 30 40 50 60 MAVAAAAAAT AMSAAGGGGA SAARSISRFR GCLAGALLGD CVGAVYEAHD TVSLASVLSH 70 80 90 100 110 120 VESLEPDPGT PGSARTETLY YTDDTAMTRA LVQSLLAKEA FDEVDMAHRF AQEYKKDPDR 130 140 150 160 170 180 GYGAGVITVF KKLLNPKCRD VYEPARAQFN GKGSYGNGGA MRVAGISLAY SSVQDVQKFA 190 200 210 220 230 240 RLSAQLTHAS SLGYNGAILQ ALAVHLALQG VSSSEHFLEQ LLGHMEELEG DAQSVLDAKE 250 260 270 280 290 300 LGMEERPYSS RLKKVGELLD QDVVSREEVV SELGNGIAAF ESVPTAIYCF LRCMEPHPEI 310 320 330 340 350 360 PSTFNSLQRT LIYSISLGGD TDTIATMAGA IAGAYYGMEQ VPESWQQSCE GFEETDVLAQ 370 SLHRVFQESS
	Isoform 2. Checksum: 01B66A15E6625CBF	FASTA	284	31,043
	10 20 30 40 50 60 MTRALVQSLL AKEAFDEVDM AHRFAQEYKK DPDRGYGAGV ITVFKKLLNP KCRDVYEPAR 70 80 90 100 110 120 AQFNGKGSYG NGGAMRVAGI SLAYSSVQDV QKFARLSAQL THASSLGYNG AILQALAVHL 130 140 150 160 170 180 ALQGVSSSEH FLEQLLGHME ELEGDAQSVL DAKELGMEER PYSSRLKKVG ELLDQDVVSR 190 200 210 220 230 240 EEVVSELGNG IAAFESVPTA IYCFLRCMEP HPEIPSTFNS LQRTLIYSIS LGGDTDTIAT 250 260 270 280 MAGAIAGAYY GMEQVPESWQ QSCEGFEETD VLAQSLHRVF QESS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 12070318] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Kidney, Liver and Spleen.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: FVB/N-3. Tissue: Mammary gland.
[4]	"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: 16278211] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC010639 mRNA. Translation: AAH10639.1.
BC023177 mRNA. Translation: AAH23177.2.
BC045203 mRNA. Translation: AAH45203.1.

IPI

IPI00322267.
IPI00828376.

RefSeq

NP_598644.1.

UniGene

Mm.11285

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QTY	X-ray	1.80	A/B	25-369	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSMUSG00000042558. Mus musculus. [Contig view]

GeneID

100206.

KEGG

mmu:100206.

Organism-specific databases

MGI

MGI:2140364. Adprhl2.

Phylogenomic databases

HOVERGEN

Q8CG72.

OMA

Q8CG72. DTIASMA.

Enzyme and pathway databases

BRENDA

3.2.1.143. 244.

Gene expression databases

ArrayExpress

Q8CG72.

Bgee

Q8CG72.

CleanEx

MM_ADPRHL2.

Family and domain databases

InterPro

IPR005502. Ribosyl_crysJ1.
[Graphical view]

Pfam

PF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

354321.

SOURCE

Search...

Entry information

Entry name

ARHL2_MOUSE

Accession

Primary (citable) accession number: Q8CG72
Secondary accession number(s): Q80UW9, Q8R575, Q921U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 6, 2007
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)