Q9D892 (ITPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inosine triphosphate pyrophosphatase
Short name=ITPase
Short name=Inosine triphosphatase
EC=3.6.1.19

Alternative name(s):
Non-canonical purine NTP pyrophosphatase
Non-standard purine NTP pyrophosphatase
Nucleoside-triphosphate diphosphatase
Nucleoside-triphosphate pyrophosphatase
Short name=NTPase

Gene names

Name:

Itpa

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 › Mus

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Ref.3 Ref.4
Catalytic activity	A nucleoside triphosphate + H2O = a nucleotide + diphosphate.
Cofactor	Binds 1 divalent metal cation ion per subunit; can use either magnesium or manganese By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Disruption phenotype	Accumulates ITP in erythrocytes. Accumulates inosine in RNA and deoxyinosine in DNA. Ref.4
Sequence similarities	Belongs to the HAM1 NTPase family.
Biophysicochemical properties	Kinetic parameters: Vmax values are similar for dITP, dHAPTP and dGTP. KM=24.9 µM for dITP Ref.3 KM=38.4 µM for dHAPTP KM=667 µM for dGTP

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphate diphosphatase activity Inferred from direct assay. Source: MGI nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 198	197	Inosine triphosphate pyrophosphatase		PRO_0000178281
Regions
	Region	14 – 19	6	Substrate binding By similarity
	Region	72 – 73	2	Substrate binding By similarity
	Region	149 – 152	4	Substrate binding By similarity
	Region	177 – 178	2	Substrate binding By similarity
Sites
	Metal binding	44	1	Magnesium or manganese By similarity
	Metal binding	72	1	Magnesium or manganese By similarity
	Binding site	56	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Experimental info
	Sequence conflict	32	1	P → Q in BAB25571. Ref.2
	Sequence conflict	54	1	I → M in BAB25571. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9D892 [UniParc]. Last modified April 23, 2003. Version 2. Checksum: D70337E3D2001A9E	FASTA	198	21,897
	10 20 30 40 50 60 MAASLVGKKI VFVTGNAKKL EEVIQILGDN FPCTLEAQKI DLPEYQGEPD EISIQKCREA 70 80 90 100 110 120 ARQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLQKLKPEGL HQLLAGFEDK SAYALCTFAL 130 140 150 160 170 180 STGDPSQPVL LFRGQTSGQI VMPRGSRDFG WDPCFQPDGY EQTYAEMPKS EKNTISHRFR 190 ALHKLQEYFS VAAGAGDH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Strain: C57BL/6J. Tissue: Small intestine.
[2]	"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]. Strain: C57BL/6. Tissue: Eye.
[3]	"Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase." Burgis N.E., Cunningham R.P. J. Biol. Chem. 282:3531-3538(2007) [PubMed: 17090528] [Abstract] Cited for: SUBSTRATE SPECIFICITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"ITPA protein, an enzyme that eliminates deaminated purine nucleoside triphosphates in cells." Sakumi K., Abolhassani N., Behmanesh M., Iyama T., Tsuchimoto D., Nakabeppu Y. Mutat. Res. 703:43-50(2010) [PubMed: 20601097] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK008279 mRNA. Translation: BAB25571.1. BC026508 mRNA. Translation: AAH26508.1.
IPI	IPI00678003.
RefSeq	NP_080198.2. NM_025922.2.
UniGene	Mm.21399.
3D structure databases
ProteinModelPortal	Q9D892.
SMR	Q9D892. Positions 1-189.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9D892. 1 interaction.
STRING	Q9D892.
PTM databases
PhosphoSite	Q9D892.
2D gel databases
REPRODUCTION-2DPAGE	Q9D892.
Proteomic databases
PRIDE	Q9D892.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000103193; ENSMUSP00000099482; ENSMUSG00000074797.
GeneID	16434.
KEGG	mmu:16434.
Organism-specific databases
CTD	3704.
MGI	MGI:96622. Itpa.
Phylogenomic databases
GeneTree	ENSGT00390000015399.
HOGENOM	HBG697237.
HOVERGEN	HBG039521.
InParanoid	Q9D892.
OMA	ARQVQGP.
OrthoDB	EOG4THVV4.
PhylomeDB	Q9D892.
Gene expression databases
ArrayExpress	Q9D892.
Bgee	Q9D892.
Genevestigator	Q9D892.
GermOnline	ENSMUSG00000075019. Mus musculus.
Family and domain databases
InterPro	IPR002637. Ham1p-like. [Graphical view]
KO	K01519.
PANTHER	PTHR11067. Ham1p_like. 1 hit.
Pfam	PF01725. Ham1p_like. 1 hit. [Graphical view]
TIGRFAMs	TIGR00042. TIGR00042. 1 hit.
ProtoNet	Search...
Other
NextBio	289677.
SOURCE	Search...

Entry information

Entry name

ITPA_MOUSE

Accession

Primary (citable) accession number: Q9D892
Secondary accession number(s): Q8R0Q8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	April 23, 2003
Last modified:	November 16, 2011
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program