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Protein

Inositol polyphosphate 1-phosphatase

Gene

INPP1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by Li+.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Magnesium 1
Binding sitei119 – 1191SubstrateBy similarity
Metal bindingi153 – 1531Magnesium 1By similarity
Metal bindingi153 – 1531Magnesium 2
Metal bindingi155 – 1551Magnesium 1; via carbonyl oxygen
Metal bindingi156 – 1561Magnesium 2
Metal bindingi317 – 3171Magnesium 2
Binding sitei317 – 3171SubstrateBy similarity

GO - Molecular functioni

  1. inositol-1,4-bisphosphate 1-phosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. phosphatidylinositol phosphorylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_212018. Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RKP21327.
UniPathwayiUPA00944.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol polyphosphate 1-phosphatase (EC:3.1.3.57)
Short name:
IPP
Short name:
IPPase
Gene namesi
Name:INPP1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Inositol polyphosphate 1-phosphatasePRO_0000142509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei318 – 3181PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP21327.
PRIDEiP21327.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009977.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2421Combined sources
Helixi26 – 294Combined sources
Turni40 – 434Combined sources
Helixi48 – 6821Combined sources
Helixi72 – 754Combined sources
Beta strandi76 – 805Combined sources
Beta strandi82 – 854Combined sources
Beta strandi91 – 933Combined sources
Helixi103 – 1108Combined sources
Turni111 – 1133Combined sources
Helixi117 – 1259Combined sources
Beta strandi134 – 1385Combined sources
Helixi145 – 1473Combined sources
Beta strandi148 – 1569Combined sources
Helixi158 – 1636Combined sources
Beta strandi176 – 1783Combined sources
Helixi179 – 1813Combined sources
Beta strandi183 – 1908Combined sources
Turni191 – 1933Combined sources
Beta strandi196 – 20813Combined sources
Turni210 – 2123Combined sources
Beta strandi215 – 23016Combined sources
Turni240 – 2423Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi264 – 2674Combined sources
Turni278 – 2814Combined sources
Beta strandi284 – 2874Combined sources
Helixi291 – 2999Combined sources
Beta strandi304 – 3085Combined sources
Helixi315 – 32612Combined sources
Turni327 – 3293Combined sources
Beta strandi331 – 3344Combined sources
Helixi335 – 3406Combined sources
Turni359 – 3646Combined sources
Beta strandi373 – 3775Combined sources
Helixi379 – 3857Combined sources
Turni390 – 3923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1INPX-ray2.30A1-400[»]
ProteinModelPortaliP21327.
SMRiP21327. Positions 1-400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21327.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni155 – 1584Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiNOG306469.
GeneTreeiENSGT00390000014061.
HOGENOMiHOG000007839.
HOVERGENiHBG006163.
InParanoidiP21327.
KOiK01107.
OMAiAGYKSLC.
OrthoDBiEOG7G4QG6.
TreeFamiTF314300.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDILQELLR VSEKAANIAR ACRQQETLFQ LLIEEKKEGE KNKKFAVDFK
60 70 80 90 100
TLADVLVQEV IKENMENKFP GLGKKIFGEE SNEFTNDLGE KIIMRLGPTE
110 120 130 140 150
EETVALLSKV LNGNKLASEA LAKVVHQDVF FSDPALDSVE INIPQDILGI
160 170 180 190 200
WVDPIDSTYQ YIKGSADITP NQGIFPSGLQ CVTVLIGVYD IQTGVPLMGV
210 220 230 240 250
INQPFVSQDL HTRRWKGQCY WGLSYLGTNI HSLLPPVSTR SNSEAQSQGT
260 270 280 290 300
QNPSSEGSCR FSVVISTSEK ETIKGALSHV CGERIFRAAG AGYKSLCVIL
310 320 330 340 350
GLADIYIFSE DTTFKWDSCA AHAILRAMGG GMVDLKECLE RNPDTGLDLP
360 370 380 390 400
QLVYHVGNEG AAGVDQWANK GGLIAYRSEK QLETFLSRLL QHLAPVATHT
Length:400
Mass (Da):43,965
Last modified:October 17, 2006 - v2
Checksum:i27917063A224D6A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841F → L in AAA30588 (PubMed:2175905).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55916 mRNA. Translation: AAA30588.1.
BC114863 mRNA. Translation: AAI14864.1.
PIRiA39254.
RefSeqiNP_776789.1. NM_174364.2.
XP_005202248.1. XM_005202191.2.
XP_005202249.1. XM_005202192.2.
XP_010800089.1. XM_010801787.1.
XP_010800090.1. XM_010801788.1.
XP_010800091.1. XM_010801789.1.
XP_010800092.1. XM_010801790.1.
UniGeneiBt.5174.

Genome annotation databases

EnsembliENSBTAT00000009977; ENSBTAP00000009977; ENSBTAG00000007584.
GeneIDi281869.
KEGGibta:281869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55916 mRNA. Translation: AAA30588.1.
BC114863 mRNA. Translation: AAI14864.1.
PIRiA39254.
RefSeqiNP_776789.1. NM_174364.2.
XP_005202248.1. XM_005202191.2.
XP_005202249.1. XM_005202192.2.
XP_010800089.1. XM_010801787.1.
XP_010800090.1. XM_010801788.1.
XP_010800091.1. XM_010801789.1.
XP_010800092.1. XM_010801790.1.
UniGeneiBt.5174.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1INPX-ray2.30A1-400[»]
ProteinModelPortaliP21327.
SMRiP21327. Positions 1-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009977.

Proteomic databases

PaxDbiP21327.
PRIDEiP21327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000009977; ENSBTAP00000009977; ENSBTAG00000007584.
GeneIDi281869.
KEGGibta:281869.

Organism-specific databases

CTDi3628.

Phylogenomic databases

eggNOGiNOG306469.
GeneTreeiENSGT00390000014061.
HOGENOMiHOG000007839.
HOVERGENiHBG006163.
InParanoidiP21327.
KOiK01107.
OMAiAGYKSLC.
OrthoDBiEOG7G4QG6.
TreeFamiTF314300.

Enzyme and pathway databases

UniPathwayiUPA00944.
ReactomeiREACT_212018. Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RKP21327.

Miscellaneous databases

EvolutionaryTraceiP21327.
NextBioi20805771.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiINPP_BOVIN
AccessioniPrimary (citable) accession number: P21327
Secondary accession number(s): Q1RMJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 17, 2006
Last modified: March 4, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.