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Protein

Inosine triphosphate pyrophosphatase

Gene

ITPA

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

A nucleoside triphosphate + H2O = a nucleotide + diphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 1 divalent metal cation per subunit; can use either Mg2+ or Mn2+.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Magnesium or manganeseUniRule annotation
Binding sitei55 – 551SubstrateUniRule annotation
Metal bindingi71 – 711Magnesium or manganeseUniRule annotation
Binding sitei171 – 1711SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-GGA-15869. Metabolism of nucleotides.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine triphosphate pyrophosphataseUniRule annotation (EC:3.6.1.19UniRule annotation)
Short name:
ITPaseUniRule annotation
Short name:
Inosine triphosphataseUniRule annotation
Alternative name(s):
Non-canonical purine NTP pyrophosphataseUniRule annotation
Non-standard purine NTP pyrophosphataseUniRule annotation
Nucleoside-triphosphate diphosphataseUniRule annotation
Nucleoside-triphosphate pyrophosphataseUniRule annotation
Short name:
NTPaseUniRule annotation
Gene namesi
Name:ITPAUniRule annotation
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 8

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Inosine triphosphate pyrophosphatasePRO_0000413102Add
BLAST

Proteomic databases

PaxDbiF1NLH9.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005130.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 186Substrate bindingUniRule annotation
Regioni71 – 722Substrate bindingUniRule annotation
Regioni148 – 1514Substrate bindingUniRule annotation
Regioni176 – 1772Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the HAM1 NTPase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3222. Eukaryota.
COG0127. LUCA.
GeneTreeiENSGT00390000015399.
InParanoidiF1NLH9.
KOiK01519.
OMAiPNFPRTI.

Family and domain databases

Gene3Di3.90.950.10. 1 hit.
HAMAPiMF_03148. HAM1_NTPase.
InterProiIPR002637. Ham1p-like.
IPR027502. ITPase.
IPR029001. ITPase-like_fam.
[Graphical view]
PANTHERiPTHR11067. PTHR11067. 1 hit.
PfamiPF01725. Ham1p_like. 1 hit.
[Graphical view]
SUPFAMiSSF52972. SSF52972. 1 hit.
TIGRFAMsiTIGR00042. TIGR00042. 1 hit.

Sequencei

Sequence statusi: Complete.

F1NLH9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPVRRSVV FVTGNAKKLE EVTQILGDSS PYTLVARKID LPEYQGEPDE
60 70 80 90 100
ISVQKCREAA RQIRGPVIVE DTCLCFNALG GLPGPYIKWF LEKLKPEGLY
110 120 130 140 150
KLLAGFEDKS AYALCTFAFS TGNPEEPVKL FKGQTHGVIV EPRGPRDFGW
160 170 180 190 200
DPCFQPDGYD QTYAELPKAV KNSISHRYRA LSELSAFFLQ SNPTEAPSSP

S
Length:201
Mass (Da):22,262
Last modified:October 19, 2011 - v2
Checksum:i7723F1019E2C3BA9
GO

Sequence databases

RefSeqiNP_001258859.1. NM_001271930.2.
UniGeneiGga.11897.

Genome annotation databases

EnsembliENSGALT00000005139; ENSGALP00000005130; ENSGALG00000003250.
GeneIDi424390.
KEGGigga:424390.

Cross-referencesi

Sequence databases

RefSeqiNP_001258859.1. NM_001271930.2.
UniGeneiGga.11897.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005130.

Proteomic databases

PaxDbiF1NLH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000005139; ENSGALP00000005130; ENSGALG00000003250.
GeneIDi424390.
KEGGigga:424390.

Organism-specific databases

CTDi3704.

Phylogenomic databases

eggNOGiKOG3222. Eukaryota.
COG0127. LUCA.
GeneTreeiENSGT00390000015399.
InParanoidiF1NLH9.
KOiK01519.
OMAiPNFPRTI.

Enzyme and pathway databases

ReactomeiR-GGA-15869. Metabolism of nucleotides.

Miscellaneous databases

PROiF1NLH9.

Family and domain databases

Gene3Di3.90.950.10. 1 hit.
HAMAPiMF_03148. HAM1_NTPase.
InterProiIPR002637. Ham1p-like.
IPR027502. ITPase.
IPR029001. ITPase-like_fam.
[Graphical view]
PANTHERiPTHR11067. PTHR11067. 1 hit.
PfamiPF01725. Ham1p_like. 1 hit.
[Graphical view]
SUPFAMiSSF52972. SSF52972. 1 hit.
TIGRFAMsiTIGR00042. TIGR00042. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
    Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
    , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
    Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Red jungle fowl.

Entry informationi

Entry nameiITPA_CHICK
AccessioniPrimary (citable) accession number: F1NLH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 8, 2016
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.