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Q2KIC5 (ITPA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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.

Sequence similarities

Belongs to the HAM1 NTPase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processnucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphate diphosphatase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 208207Inosine triphosphate pyrophosphatase
PRO_0000306869

Regions

Region14 – 196Substrate binding By similarity
Region72 – 732Substrate binding By similarity
Region149 – 1524Substrate binding By similarity
Region177 – 1782Substrate binding By similarity

Sites

Metal binding441Magnesium or manganese By similarity
Metal binding721Magnesium or manganese By similarity
Binding site561Substrate By similarity
Binding site1721Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KIC5 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: F49F922F60A8822B

FASTA20823,061
        10         20         30         40         50         60 
MAASLAGKKI VFVTGNAKKL EEVIQILGDK FPCTLVAQKI DLPEYQGEPD EISIRKCQEA 

        70         80         90        100        110        120 
ARQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLEKLKPEGL HQLLEGFQDK SAYALCTFAF 

       130        140        150        160        170        180 
STGDPNEPVR LFRGRTMGRI VVPRGCRDFG WDPCFQPDGY EQTYAEMPKA EKNTISHRFR 

       190        200 
ALLALQEYFS SLTPGVGDDH PSWGSGEG 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC112688 mRNA. Translation: AAI12689.1.
IPIIPI00702859.
RefSeqNP_001069750.1. NM_001076282.1.
UniGeneBt.53005.

3D structure databases

ProteinModelPortalQ2KIC5.
SMRQ2KIC5. Positions 1-192.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2KIC5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000018301; ENSBTAP00000018301; ENSBTAG00000013776.
GeneID613653.
KEGGbta:613653.

Organism-specific databases

CTD3704.

Phylogenomic databases

eggNOGmaNOG04379.
GeneTreeENSGT00390000015399.
HOVERGENHBG039521.
InParanoidQ2KIC5.
OrthoDBEOG4THVV4.
PhylomeDBQ2KIC5.

Family and domain databases

InterProIPR002637. Ham1p-like.
[Graphical view]
KOK01519.
PANTHERPTHR11067. Ham1p_like. 1 hit.
PfamPF01725. Ham1p_like. 1 hit.
[Graphical view]
TIGRFAMsTIGR00042. TIGR00042. 1 hit.
ProtoNetSearch...

Entry information

Entry nameITPA_BOVIN
AccessionPrimary (citable) accession number: Q2KIC5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 7, 2006
Last modified: November 16, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families