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Q80V26 (IMPA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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 monophosphatase 3

Short name=IMP 3
Short name=IMPase 3
EC=3.1.3.25
EC=3.1.3.7
Alternative name(s):
Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase
Short name=Golgi-resident PAP phosphatase
Short name=gPAPP
Inositol monophosphatase domain-containing protein 1
Inositol-1(or 4)-monophosphatase 3
Myo-inositol monophosphatase A3
Gene names
Name:Impad1
Synonyms:Impa3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Ref.4

Catalytic activity

Myo-inositol phosphate + H2O = myo-inositol + phosphate. Ref.4

Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate. Ref.4

Cofactor

Magnesium By similarity.

Enzyme regulation

Strongly inhibited by lithium. Ref.4

Pathway

Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.

Subcellular location

Golgi apparatus. Golgi apparatustrans-Golgi network membrane; Single-pass type II membrane protein By similarity Ref.4.

Developmental stage

At 18.5 dpc, widely expressed with enhanced levels in brain, spinal cord, lung and kidney, including medulla and cortex. In the developing brain, strongly expressed in the neopallial cortex and throughout the cerebellum with intense expression within the developing Purkinje cells and adjacent choroid plexus. Strong expression also observed within the pons and throughout the medulla oblongata. In the lung, expressed in individual pneumocytes and particularly in cells surrounding developing bronchi/bronchioles. Moderate expression in chondrocytes of costal cartilage and in the surrounding perichondrium. Ref.4

Post-translational modification

Contains N-linked glycan resistant to endoglycosydase H By similarity.

Disruption phenotype

Mutant animals experience severe respiratory distress and died within minutes after birth. At 18.5 dpc, lungs exhibit small alveolar spaces and thickened septa. The rib cage cartilage is hypocellular with abnormal, fibrous-appearing extracellular matrix. Animals show severe skeletal abnormalities, most notably in the longitudinal growth of bones formed by endochondral ossification. The length of the axial skeleton is reduced. The appendicular bones of the upper limbs, as well as the ilium, femur, tibia and fibula of the lower limbs are markedly shorter than in wild-type littermates. The rib cages display malformation characterized by reduced sternal length and correspondingly diminished rib spacing. The process of intramembranous ossification is normal. Mutant animals exhibit a deficiency in glycosaminoglycan sulfation. Mutant cartilage and lung exhibit a substantial decrease in chondroitin 4-sulfate and an increase in nonsulfated chondroitin compared with wild type tissue. Ref.4

Sequence similarities

Belongs to the inositol monophosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=21 µM for 3'-phosphoadenosine 5'- phosphate (PAP) Ref.4

Vmax=9.5 µmol/min/mg enzyme

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchondrocyte development

Inferred from mutant phenotype PubMed 18539921. Source: MGI

chondroitin sulfate metabolic process

Inferred from mutant phenotype PubMed 18539921Ref.4. Source: MGI

dephosphorylation

Inferred from direct assay Ref.4. Source: GOC

embryonic digit morphogenesis

Inferred from mutant phenotype PubMed 18539921. Source: MGI

endochondral ossification

Inferred from mutant phenotype PubMed 18539921. Source: MGI

inositol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

phosphatidylinositol phosphorylation

Inferred from electronic annotation. Source: InterPro

post-embryonic development

Inferred from mutant phenotype PubMed 18539921Ref.4. Source: MGI

skeletal system development

Inferred from mutant phenotype Ref.4. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from sequence orthology Ref.4. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function3'(2'),5'-bisphosphate nucleotidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3'-nucleotidase activity

Inferred from direct assay Ref.4. Source: MGI

inositol monophosphate 1-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol monophosphate 3-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol monophosphate 4-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Inositol monophosphatase 3
PRO_0000289042

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3321Helical; Potential
Topological domain34 – 356323Lumenal Potential
Region174 – 1774Substrate binding By similarity

Sites

Metal binding1311Magnesium 1 By similarity
Metal binding1721Magnesium 1 By similarity
Metal binding1721Magnesium 2 By similarity
Metal binding1741Magnesium 1; via carbonyl oxygen By similarity
Metal binding1751Magnesium 2 By similarity
Metal binding2981Magnesium 2 By similarity
Binding site1311Substrate By similarity
Binding site2981Substrate By similarity

Amino acid modifications

Glycosylation2571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q80V26 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F01BF0082F5C7C82

FASTA35638,616
        10         20         30         40         50         60 
MAPMGIRLSP LGVAVFFLLG LGVLYHLYSG FLAGRFSLFG LGSEPAAGEA EVASDGGTVD 

        70         80         90        100        110        120 
LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK 

       130        140        150        160        170        180 
TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY 

       190        200        210        220        230        240 
TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS 

       250        260        270        280        290        300 
RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC 

       310        320        330        340        350 
AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGH 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary tumor.
[4]"A role for a lithium-inhibited Golgi nucleotidase in skeletal development and sulfation."
Frederick J.P., Tafari A.T., Wu S.M., Megosh L.C., Chiou S.T., Irving R.P., York J.D.
Proc. Natl. Acad. Sci. U.S.A. 105:11605-11612(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TOPOLOGY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL772346 Genomic DNA. Translation: CAM23643.1.
CH466538 Genomic DNA. Translation: EDL05698.1.
BC048776 mRNA. Translation: AAH48776.1.
BC138209 mRNA. Translation: AAI38210.1.
BC145952 mRNA. Translation: AAI45953.1.
CCDSCCDS17947.1.
RefSeqNP_808398.1. NM_177730.3.
UniGeneMm.218889.
Mm.369779.

3D structure databases

ProteinModelPortalQ80V26.
SMRQ80V26. Positions 61-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000082013.

PTM databases

PhosphoSiteQ80V26.

Proteomic databases

MaxQBQ80V26.
PaxDbQ80V26.
PRIDEQ80V26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084949; ENSMUSP00000082013; ENSMUSG00000066324.
GeneID242291.
KEGGmmu:242291.
UCSCuc008rxc.2. mouse.

Organism-specific databases

CTD54928.
MGIMGI:1915720. Impad1.

Phylogenomic databases

eggNOGCOG1218.
GeneTreeENSGT00530000063462.
HOGENOMHOG000290671.
HOVERGENHBG062091.
InParanoidA6H6P6.
KOK15759.
OMANVQINTE.
OrthoDBEOG7CG71H.
PhylomeDBQ80V26.
TreeFamTF314300.

Enzyme and pathway databases

UniPathwayUPA00823; UER00788.

Gene expression databases

BgeeQ80V26.
CleanExMM_IMPAD1.
GenevestigatorQ80V26.

Family and domain databases

InterProIPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERPTHR20854. PTHR20854. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEPS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIMPAD1. mouse.
NextBio385292.
PROQ80V26.
SOURCESearch...

Entry information

Entry nameIMPA3_MOUSE
AccessionPrimary (citable) accession number: Q80V26
Secondary accession number(s): A6H6P6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 94 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot