Abstract
We have derived the full-length sequences of the human and rat forms of the multiple inositol polyphosphate phosphatase (MIPP); their structural and functional comparison with a chick histidine acid phosphatase (HiPER1) has revealed new information: (1) MIPP is approximately 50% identical to HiPER1, but the ER-targeting domains are divergent; (2) MIPP appears to share the catalytic requirement of histidine acid phosphatases, namely, a C-terminal His residue remote from the RHGxRxP catalytic motif; (3) rat MIPP mRNA is up-regulated during chondrocyte hypertrophy. The latter observation provides a context for proposing that MIPP may aid bone mineralization and salvage the inositol moiety prior to apoptosis.
MeSH terms
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Acid Phosphatase / chemistry
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Acid Phosphatase / genetics*
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Acid Phosphatase / metabolism*
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Amino Acid Sequence
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Animals
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Base Sequence
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Chickens
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Chondrocytes / enzymology
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Cloning, Molecular
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DNA Primers / genetics
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Gene Expression Regulation, Developmental
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Humans
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In Situ Hybridization
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Molecular Sequence Data
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Osteogenesis
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Phosphoric Monoester Hydrolases / chemistry
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Phosphoric Monoester Hydrolases / genetics*
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Phosphoric Monoester Hydrolases / metabolism*
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Proteins / chemistry
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Proteins / genetics
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Proteins / metabolism
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Rats
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Sequence Homology, Amino Acid
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Up-Regulation
Substances
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DNA Primers
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HiPER1 protein, Gallus gallus
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Proteins
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Acid Phosphatase
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Phosphoric Monoester Hydrolases
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multiple inositol-polyphosphate phosphatase
Associated data
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GENBANK/AF084943
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GENBANK/AF084944