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Reviewed, UniProtKB/Swiss-Prot P21327 (INPP_BOVIN)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Inositol polyphosphate 1-phosphatase
      Short name=IPPase
      Short name=IPP
    EC=3.1.3.57
Gene names
Name: INPP1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.

Cofactor

Magnesium.

Enzyme regulation

Inhibited by Li+.

Pathway

Signal transduction; phosphatidylinositol signaling pathway.

Subunit structure

Monomer.

Miscellaneous

Acts on inositol 1,4-bisphosphate and inositol 1,3,4-triphosphate (forming inositol 3,4-bisphosphate) with a 4-fold higher affinity for the bisphosphate.

Sequence similarities

Belongs to the inositol monophosphatase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Inositol polyphosphate 1-phosphatase
PRO_0000142509

Sites

Metal binding791Magnesium 1
Metal binding1531Magnesium 1 By similarity
Metal binding1531Magnesium 2
Metal binding1551Magnesium 1; via carbonyl oxygen
Metal binding1561Magnesium 2
Metal binding3171Magnesium 2

Amino acid modifications

Modified residue3181Phosphoserine By similarity

Experimental info

Sequence conflict841F → L in AAA30588. Ref.1

Secondary structure

1 .................................................................... 400
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P21327-1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 27917063A224D6A8

FASTA40043,965
        10         20         30         40         50         60 
MSDILQELLR VSEKAANIAR ACRQQETLFQ LLIEEKKEGE KNKKFAVDFK TLADVLVQEV 

        70         80         90        100        110        120 
IKENMENKFP GLGKKIFGEE SNEFTNDLGE KIIMRLGPTE EETVALLSKV LNGNKLASEA 

       130        140        150        160        170        180 
LAKVVHQDVF FSDPALDSVE INIPQDILGI WVDPIDSTYQ YIKGSADITP NQGIFPSGLQ 

       190        200        210        220        230        240 
CVTVLIGVYD IQTGVPLMGV INQPFVSQDL HTRRWKGQCY WGLSYLGTNI HSLLPPVSTR 

       250        260        270        280        290        300 
SNSEAQSQGT QNPSSEGSCR FSVVISTSEK ETIKGALSHV CGERIFRAAG AGYKSLCVIL 

       310        320        330        340        350        360 
GLADIYIFSE DTTFKWDSCA AHAILRAMGG GMVDLKECLE RNPDTGLDLP QLVYHVGNEG 

       370        380        390        400 
AAGVDQWANK GGLIAYRSEK QLETFLSRLL QHLAPVATHT

« Hide

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References

« Hide 'large scale' references
[1]"Isolation and heterologous expression of a cDNA encoding bovine inositol polyphosphate 1-phosphatase."
York J.D., Majerus P.W.
Proc. Natl. Acad. Sci. U.S.A. 87:9548-9552(1990) [PubMed: 2175905] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.
[3]"Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution."
York J.D., Ponder J.W., Chen Z.-W., Mathews F.S., Majerus P.W.
Biochemistry 33:13164-13171(1994) [PubMed: 7947723] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.

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Cross-references

Sequence databases

M55916 mRNA. Translation: AAA30588.1.
BC114863 mRNA. Translation: AAI14864.1.
IPIIPI00686250.
PIRA39254.
RefSeqNP_776789.1.
UniGeneBt.5174

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1INPX-ray2.30A1-400[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000007584. Bos taurus. [Contig view]
GeneID281869.
KEGGbta:281869.

Phylogenomic databases

HOVERGENP21327.
OMAP21327. FKWDSCA.

Enzyme and pathway databases

BRENDA3.1.3.57. 251.

Family and domain databases

InterProIPR000760. Inositol_P.
[Graphical view]
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00378. INOSPHPHTASE.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameINPP_BOVIN
AccessionPrimary (citable) accession number: P21327
Secondary accession number(s): Q1RMJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents