PMID- 10087200
OWN - NLM
STAT- MEDLINE
DCOM- 19990524
LR  - 20161124
IS  - 0888-7543 (Print)
IS  - 0888-7543 (Linking)
VI  - 56
IP  - 3
DP  - 1999 Mar 15
TI  - Multiple inositol polyphosphate phosphatase: evolution as a distinct group within
      the histidine phosphatase family and chromosomal localization of the human and
      mouse genes to chromosomes 10q23 and 19.
PG  - 324-36
AB  - Multiple inositol polyphosphate phosphatase is the only enzyme known to hydrolyze
      the abundant metabolites inositol pentakisphosphate and inositol
      hexakisphosphate. We have previously demonstrated that the chick homolog of
      multiple inositol polyphosphate phosphatase, designated HiPER1, has a role in
      growth plate chondrocyte differentiation. The relationship of these enzymes to
      intracellular signaling is obscure, and as part of our investigation we have
      examined the murine ((MMU)Minpp1) and human ((HSA)MINPP1) homologs. Northern blot
      analysis demonstrated expression of ((MMU)Minpp1 in a variety of mouse tissues,
      comparable to the expression of other mammalian homologs, but less restricted
      than the expression of HiPER1 in chick. A purified (MMU)Minpp1 fusion protein
      cleaved phosphate from inositol (1,3,4,5)-tetrakisphosphate and para-nitrophenyl 
      phosphate. When the presumptive active site histidine was altered to alanine by
      site-directed mutagenesis, enzyme activity was abolished, confirming the
      classification of (MMU)Minpp1 as a histidine phosphatase. The amino acid
      sequences of the murine and human MINPP proteins share >80% identity with the rat
      enzyme and >56% identity with HiPER1, with conservation of the C-terminal
      consensus sequence that retains proteins in the endoplasmic reticulum. The
      intron/exon structure of the mammalian (MMU)Minpp1 and (HSA)MINPP1 genes is also 
      conserved compared to the chick HiPER1 gene. Sequence analysis of plant and fruit
      fly MINPP homologs supports the hypothesis that the MINPP enzymes constitute a
      distinct evolutionary group within the histidine phosphatase family. We have
      mapped (HSA)MINPP1 to human chromosome 10q23 by fluorescence in situ
      hybridization, YAC screening, and radiation hybrid mapping. This assignment
      places (HSA)MINPP1 in a region of chromosome 10 that is frequently mutated in
      human cancers and places (HSA)MINPP1 proximal to the tumor suppressor PTEN, which
      maps to 10q23.3. Using a radiation hybrid panel, we localized (MMU)Minpp1 to a
      region of mouse chromosome 19 that includes the murine homolog of Pten. The
      evolutionary conservation of this novel enzyme within the inositol polyphosphate 
      pathway suggests a significant role for multiple inositol polyphosphate
      phosphatase throughout higher eukaryotes.
CI  - Copyright 1999 Academic Press.
FAU - Chi, H
AU  - Chi H
AD  - Department of Orthopaedics, University of Rochester School of Medicine and
      Dentistry, Rochester, New York 14642, USA.
FAU - Tiller, G E
AU  - Tiller GE
FAU - Dasouki, M J
AU  - Dasouki MJ
FAU - Romano, P R
AU  - Romano PR
FAU - Wang, J
AU  - Wang J
FAU - O'keefe, R J
AU  - O'keefe RJ
FAU - Puzas, J E
AU  - Puzas JE
FAU - Rosier, R N
AU  - Rosier RN
FAU - Reynolds, P R
AU  - Reynolds PR
LA  - eng
SI  - GENBANK/AF046908
SI  - GENBANK/AF046909
SI  - GENBANK/AF046910
SI  - GENBANK/AF046911
SI  - GENBANK/AF046912
SI  - GENBANK/AF046913
SI  - GENBANK/AF046914
SI  - GENBANK/AF046915
GR  - AR01925/AR/NIAMS NIH HHS/United States
GR  - AR38945/AR/NIAMS NIH HHS/United States
GR  - AR44091/AR/NIAMS NIH HHS/United States
GR  - etc.
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Genomics
JT  - Genomics
JID - 8800135
RN  - 0 (Genetic Markers)
RN  - 0 (HiPER1 protein, Gallus gallus)
RN  - 0 (Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tumor Suppressor Proteins)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
RN  - EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase)
RN  - EC 3.1.3.67 (PTEN Phosphohydrolase)
RN  - EC 3.1.3.67 (PTEN protein, human)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Chromosome Mapping
MH  - Chromosomes, Human, Pair 10/*genetics
MH  - Drosophila/genetics
MH  - Evolution, Molecular
MH  - Genetic Markers
MH  - Humans
MH  - In Situ Hybridization, Fluorescence
MH  - Mice
MH  - Models, Genetic
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - PTEN Phosphohydrolase
MH  - Phosphoric Monoester Hydrolases/classification/*genetics
MH  - Phylogeny
MH  - Proteins/genetics
MH  - Recombinant Proteins/genetics
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
MH  - *Tumor Suppressor Proteins
EDAT- 1999/03/24 00:00
MHDA- 1999/03/24 00:01
CRDT- 1999/03/24 00:00
PHST- 1999/03/24 00:00 [pubmed]
PHST- 1999/03/24 00:01 [medline]
PHST- 1999/03/24 00:00 [entrez]
AID - S0888-7543(98)95736-6 [pii]
AID - 10.1006/geno.1998.5736 [doi]
PST - ppublish
SO  - Genomics. 1999 Mar 15;56(3):324-36. doi: 10.1006/geno.1998.5736.