P21327 (INPP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol polyphosphate 1-phosphatase
Short name=IPP
Short name=IPPase
EC=3.1.3.57

Gene names

Name:

INPP1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Lithium Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular_function	inositol-1,4-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 400

400

Inositol polyphosphate 1-phosphatase

PRO_0000142509

Regions

Region

155 – 158

4

Substrate binding By similarity

Sites

Metal binding

79

1

Magnesium 1

Metal binding

153

1

Magnesium 1 By similarity

Metal binding

153

1

Magnesium 2

Metal binding

155

1

Magnesium 1; via carbonyl oxygen

Metal binding

156

1

Magnesium 2

Metal binding

317

1

Magnesium 2

Binding site

119

1

Substrate By similarity

Binding site

317

1

Substrate By similarity

Amino acid modifications

Modified residue

318

1

Phosphoserine By similarity

Experimental info

Sequence conflict

84

1

F → L in AAA30588. Ref.1

Secondary structure

1

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400

Helix Strand Turn

Details...

Helix

4 – 24

21

Helix

26 – 29

4

Turn

40 – 43

4

Helix

48 – 68

21

Helix

72 – 75

4

Beta strand

76 – 80

5

Beta strand

82 – 85

4

Beta strand

91 – 93

3

Helix

103 – 110

8

Turn

111 – 113

3

Helix

117 – 125

9

Beta strand

134 – 138

5

Helix

145 – 147

3

Beta strand

148 – 156

9

Helix

158 – 163

6

Beta strand

176 – 178

3

Helix

179 – 181

3

Beta strand

183 – 190

8

Turn

191 – 193

3

Beta strand

196 – 208

13

Turn

210 – 212

3

Beta strand

215 – 230

16

Turn

240 – 242

3

Beta strand

258 – 261

4

Beta strand

264 – 267

4

Turn

278 – 281

4

Beta strand

284 – 287

4

Helix

291 – 299

9

Beta strand

304 – 308

5

Helix

315 – 326

12

Turn

327 – 329

3

Beta strand

331 – 334

4

Helix

335 – 340

6

Turn

359 – 364

6

Beta strand

373 – 377

5

Helix

379 – 385

7

Turn

390 – 392

3

Sequences

	Sequence		Length	Mass (Da)
	P21327 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 27917063A224D6A8	FASTA	400	43,965
	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

References

	« Hide 'large scale' referencesShow '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.

IPI

IPI00686250.

PIR

A39254.

RefSeq

NP_776789.1. NM_174364.2.

UniGene

Bt.5174.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1INP	X-ray	2.30	A	1-400	[»]

ProteinModelPortal

P21327.

SMR

P21327. Positions 1-400.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000009977.

Proteomic databases

PaxDb

P21327.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000009977; ENSBTAP00000009977; ENSBTAG00000007584.

GeneID

281869.

KEGG

bta:281869.

Organism-specific databases

CTD

3628.

Phylogenomic databases

eggNOG

NOG306469.

GeneTree

ENSGT00390000014061.

HOGENOM

HOG000007839.

HOVERGEN

HBG006163.

InParanoid

P21327.

KO

K01107.

OMA

TFKWDSC.

OrthoDB

EOG41C6WB.

Enzyme and pathway databases

SABIO-RK

P21327.

UniPathway

UPA00944.

Family and domain databases

InterPro

IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]

PANTHER

PTHR20854. PTHR20854. 1 hit.

Pfam

PF00459. Inositol_P. 1 hit.
[Graphical view]

PROSITE

PS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P21327.

NextBio

20805771.

Entry information

Entry name

INPP_BOVIN

Accession

Primary (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 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program