LMPD Database

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LMP002535

UniProt Annotations

Entry Information
Gene Nameinositol monophosphatase domain containing 1
Protein EntryIMPA3_MOUSE
UniProt IDQ80V26
SpeciesMouse
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=21 uM for 3'-phosphoadenosine 5'- phosphate (PAP) {ECO:0000269|PubMed:18695242}; Vmax=9.5 umol/min/mg enzyme {ECO:0000269|PubMed:18695242};
Catalytic ActivityAdenosine 3',5'-bisphosphate + H(2)O = adenosine 5'-phosphate + phosphate. {ECO:0000269|PubMed:18695242}.
Catalytic ActivityMyo-inositol phosphate + H(2)O = myo-inositol + phosphate. {ECO:0000269|PubMed:18695242}.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Developmental StageAt 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. {ECO:0000269|PubMed:18695242}.
Disruption PhenotypeMutant 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. {ECO:0000269|PubMed:18695242}.
Enzyme RegulationStrongly inhibited by lithium. {ECO:0000269|PubMed:18695242}.
FunctionMay 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. {ECO:0000269|PubMed:18695242}.
PathwayPolyol metabolism; myo-inositol biosynthesis; myo- inositol from D-glucose 6-phosphate: step 2/2.
PtmContains N-linked glycan resistant to endoglycosydase H. {ECO:0000250}.
SimilarityBelongs to the inositol monophosphatase family. {ECO:0000305}.
Subcellular LocationGolgi apparatus {ECO:0000269|PubMed:18695242}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.