[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Oocyte; PubMed=1325777 [NCBI, ExPASy, EBI, Israel, Japan] Wreggett K.A.; "Inositol monophosphatase is a highly conserved enzyme having localized structural similarity to both glycerol 3-phosphate dehydrogenase and haemoglobin."; Biochem. J. 286:147-152(1992).

Comments

FUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides.
CATALYTIC ACTIVITY: Myo-inositol phosphate + H₂O = myo-inositol + phosphate.
COFACTOR: Magnesium (By similarity).
ENZYME REGULATION: Inhibited by Li(+) (By similarity).
PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
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

X65513; CAA46486.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S24343; S24343.

NP_001095235.1; -.

3D structure databases

HSSP

P29218; 1IMF. [HSSP ENTRY / PDB]

SMR

P29219; 5-279.

ModBase

P29219.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0008934;	Molecular function: inositol-1(or 4)-monophosphatase 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).
GO:0005975;	Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000146; In_FB_phphtase.
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

PR00377; INFBPHPHTASE.
PR00378; INOSPHPHTASE.

ProDom

PD023420; Inositol_P; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

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

Genome annotation databases

GeneID

397905; -.

KEGG

xla:397905; -.

Phylogenomic databases

HOVERGEN

P29219; -.

Other

UniRef

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

Keywords

Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 285`	`285`	`Inositol monophosphatase.`	`PRO_0000142518`
`METAL`	`73 73`		`Magnesium 1 (By similarity).`
`METAL`	`93 93`		`Magnesium 1 (By similarity).`
`METAL`	`93 93`		`Magnesium 2 (By similarity).`
`METAL`	`95 95`		`Magnesium 1; via carbonyl oxygen (By similarity).`
`METAL`	`96 96`		`Magnesium 2 (By similarity).`
`METAL`	`224 224`		`Magnesium 2 (By similarity).`
`BINDING`	`96 96`		`Substrate (By similarity).`

Sequence information

Length: 285 AA [This is the length of the unprocessed precursor]

Molecular weight: 30729 Da [This is the MW of the unprocessed precursor]

CRC64: 34E9CD9A99231292 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEDRWQECMD FLAVSIARKA GSVVCAALKE DVSIMVKTSL APADLVTATD QKVEEMIISS 

        70         80         90        100        110        120 
IKEKYPSHSF IGEESVAAGA GSTLTDNPTW IIDPIDGTTN FVHRFPFVAV SIGFAVHKQV 

       130        140        150        160        170        180 
EFGVVYSCVE DKMYTGRKGK GSFCNGQKLQ VSGQKDITKS MIITELGSNR NPEFIKTVSL 

       190        200        210        220        230        240 
SNMERLLCIP IHGIRAVGTA AVNMCLVATG GADAYYEMGL HCWDMAAASV IVTEAGGTIL 

       250        260        270        280 
DATGGLFDLM SCRIISASSR EIAERIAKEL QIIPLERDDG KSTNS

P29219 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