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P21327 (INPP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Inositol polyphosphate 1-phosphatase

Short name=IPP
Short name=IPPase
EC=3.1.3.57
Gene names
Name:INPP1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-trisphosphate (forming inositol 3,4-bisphosphate) with a 4-fold higher affinity for the bisphosphate.

Sequence similarities

Belongs to the inositol monophosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Inositol polyphosphate 1-phosphatase
PRO_0000142509

Regions

Region155 – 1584Substrate binding By similarity

Sites

Metal binding791Magnesium 1
Metal binding1531Magnesium 1 By similarity
Metal binding1531Magnesium 2
Metal binding1551Magnesium 1; via carbonyl oxygen
Metal binding1561Magnesium 2
Metal binding3171Magnesium 2
Binding site1191Substrate By similarity
Binding site3171Substrate By similarity

Amino acid modifications

Modified residue3181Phosphoserine By similarity

Experimental info

Sequence conflict841F → L in AAA30588. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P21327 [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

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55916 mRNA. Translation: AAA30588.1.
BC114863 mRNA. Translation: AAI14864.1.
PIRA39254.
RefSeqNP_776789.1. NM_174364.2.
XP_005202248.1. XM_005202191.1.
XP_005202249.1. XM_005202192.1.
XP_005202250.1. XM_005202193.1.
XP_005202251.1. XM_005202194.1.
UniGeneBt.5174.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1INPX-ray2.30A1-400[»]
ProteinModelPortalP21327.
SMRP21327. Positions 1-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000009977.

Proteomic databases

PaxDbP21327.
PRIDEP21327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000009977; ENSBTAP00000009977; ENSBTAG00000007584.
GeneID281869.
KEGGbta:281869.

Organism-specific databases

CTD3628.

Phylogenomic databases

eggNOGNOG306469.
GeneTreeENSGT00390000014061.
HOGENOMHOG000007839.
HOVERGENHBG006163.
InParanoidP21327.
KOK01107.
OMAAGAGYKS.
OrthoDBEOG7G4QG6.
TreeFamTF314300.

Enzyme and pathway databases

SABIO-RKP21327.
UniPathwayUPA00944.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERPTHR20854. PTHR20854. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21327.
NextBio20805771.

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: April 16, 2014
This is version 109 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways