[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Brain; PubMed=2175905 [NCBI, ExPASy, EBI, Israel, Japan] York J.D., Majerus P.W.; "Isolation and heterologous expression of a cDNA encoding bovine inositol polyphosphate 1-phosphatase."; Proc. Natl. Acad. Sci. U.S.A. 87:9548-9552(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Thymus; NIH - Mammalian Gene Collection (MGC) project; Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[3]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS. DOI=10.1021/bi00249a002; PubMed=7947723 [NCBI, ExPASy, EBI, Israel, Japan] York J.D., Ponder J.W., Chen Z.-W., Mathews F.S., Majerus P.W.; "Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution."; Biochemistry 33:13164-13171(1994).

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: 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.
SIMILARITY: Belongs to the inositol monophosphatase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M55916; AAA30588.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114863; AAI14864.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A39254; A39254.

NP_776789.1; -.

3D structure databases

PDB

1INP; X-ray; 2.30 A; A=1-400.

[ExPASy / RCSB / EBI]

PDBsum

1INP; -.

ModBase

P21327.

Ontologies

GO:0004441;	Molecular function: inositol-1,4-bisphosphate 1-phosphatase activity (inferred from electronic annotation from EC).
GO:0031403;	Molecular function: lithium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000760; Inositol_P.
Graphical view of domain structure.

PANTHER

PTHR20854; Inositol_P; 1.

Pfam

PF00459; Inositol_P; 1.
Pfam graphical view of domain structure.

PRINTS

PR00378; INOSPHPHTASE.

PROSITE

PS00629; IMP_1; 1.
PS00630; IMP_2; 1.

ProtoNet

P21327.

Genome annotation databases

Ensembl

ENSBTAG00000007584; Bos taurus. [Contig view]

GeneID

281869; -.

KEGG

bta:281869; -.

Phylogenomic databases

HOVERGEN

P21327; -.

Other

LinkHub

P21327; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Hydrolase; Lithium; Magnesium; Metal-binding; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 400`	`400`	`Inositol polyphosphate 1-phosphatase.`	`PRO_0000142509`
`METAL`	`79 79`		`Magnesium 1.`
`METAL`	`153 153`		`Magnesium 1 (By similarity).`
`METAL`	`153 153`		`Magnesium 2.`
`METAL`	`155 155`		`Magnesium 1; via carbonyl oxygen.`
`METAL`	`156 156`		`Magnesium 2.`
`METAL`	`317 317`		`Magnesium 2.`
`MOD_RES`	`318 318`		`Phosphoserine (By similarity).`
`CONFLICT`	`84 84`		`F -> L (in Ref. 1; AAA30588).`
`HELIX`	`4 24`	`21`
`HELIX`	`26 29`	`4`
`TURN`	`40 43`	`4`
`HELIX`	`48 68`	`21`
`HELIX`	`72 75`	`4`
`STRAND`	`76 80`	`5`
`STRAND`	`82 85`	`4`
`STRAND`	`91 93`	`3`
`HELIX`	`103 110`	`8`
`TURN`	`111 113`	`3`
`HELIX`	`117 125`	`9`
`STRAND`	`134 138`	`5`
`HELIX`	`145 147`	`3`
`STRAND`	`148 156`	`9`
`HELIX`	`158 163`	`6`
`STRAND`	`176 178`	`3`
`HELIX`	`179 181`	`3`
`STRAND`	`183 190`	`8`
`TURN`	`191 193`	`3`
`STRAND`	`196 208`	`13`
`TURN`	`210 212`	`3`
`STRAND`	`215 230`	`16`
`TURN`	`240 242`	`3`
`STRAND`	`258 261`	`4`
`STRAND`	`264 267`	`4`
`TURN`	`278 281`	`4`
`STRAND`	`284 287`	`4`
`HELIX`	`291 299`	`9`
`STRAND`	`304 308`	`5`
`HELIX`	`315 326`	`12`
`TURN`	`327 329`	`3`
`STRAND`	`331 334`	`4`
`HELIX`	`335 340`	`6`
`TURN`	`359 364`	`6`
`STRAND`	`373 377`	`5`
`HELIX`	`379 385`	`7`
`TURN`	`390 392`	`3`

Sequence information

Length: 400 AA [This is the length of the unprocessed precursor]

Molecular weight: 43965 Da [This is the MW of the unprocessed precursor]

CRC64: 27917063A224D6A8 [This is a checksum on the sequence]

        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

P21327 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools