IMPA1_CAEEL
ID IMPA1_CAEEL Reviewed; 285 AA.
AC Q19420; A5A8G3; A5A8G4; A5JYT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Inositol monophosphatase ttx-7;
DE Short=IMP;
DE Short=IMPase;
DE EC=3.1.3.25 {ECO:0000250|UniProtKB:P29218};
DE AltName: Full=Abnormal thermotaxis protein 7;
DE AltName: Full=D-galactose 1-phosphate phosphatase {ECO:0000250|UniProtKB:P29218};
DE EC=3.1.3.94 {ECO:0000250|UniProtKB:P29218};
DE AltName: Full=Inositol-1(or 4)-monophosphatase;
GN Name=ttx-7; ORFNames=F13G3.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-216.
RX PubMed=17158747; DOI=10.1101/gad.1497806;
RA Tanizawa Y., Kuhara A., Inada H., Kodama E., Mizuno T., Mori I.;
RT "Inositol monophosphatase regulates localization of synaptic components and
RT behavior in the mature nervous system of C. elegans.";
RL Genes Dev. 20:3296-3310(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18403676; DOI=10.1126/science.1148922;
RA Kuhara A., Okumura M., Kimata T., Tanizawa Y., Takano R., Kimura K.D.,
RA Inada H., Matsumoto K., Mori I.;
RT "Temperature sensing by an olfactory neuron in a circuit controlling
RT behavior of C. elegans.";
RL Science 320:803-807(2008).
CC -!- FUNCTION: Responsible for the provision of inositol required for
CC synthesis of phosphatidylinositol and polyphosphoinositides. Has broad
CC substrate specificity and can use myo-inositol monophosphates, myo-
CC inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-
CC inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate,
CC glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and
CC 2'-AMP as substrates (By similarity). Required in central interneurons
CC of the mature nervous system for correct localization of synaptic
CC components. Required for thermotaxis. {ECO:0000250|UniProtKB:P29218,
CC ECO:0000269|PubMed:17158747, ECO:0000269|PubMed:18403676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000250|UniProtKB:P29218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate;
CC Xref=Rhea:RHEA:29315, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58336; EC=3.1.3.94;
CC Evidence={ECO:0000250|UniProtKB:P29218};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29218};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+), Ca(2+) and Mn(2+), but also by
CC Mg(2+) at concentrations above 3 mM. {ECO:0000250|UniProtKB:P29218}.
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17158747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q19420-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q19420-2; Sequence=VSP_029919;
CC -!- TISSUE SPECIFICITY: Isoform 1 is strongly expressed in the AFD and RIA
CC neurons of the head, in the tail and in coelomocytes. Isoform 1 is
CC weakly expressed in nerve cord motor neurons, intestine, and the
CC somatic gonad. {ECO:0000269|PubMed:17158747}.
CC -!- DISRUPTION PHENOTYPE: Worms lacking ttx-7 display defects in
CC thermotaxis behavior and localization of synaptic proteins in RIA
CC neurons yet appear morphologically normal.
CC {ECO:0000269|PubMed:17158747, ECO:0000269|PubMed:18403676}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AB303038; BAF62082.1; -; mRNA.
DR EMBL; AB303039; BAF62083.1; -; mRNA.
DR EMBL; Z71259; CAA95791.4; -; Genomic_DNA.
DR EMBL; Z71259; CAN86622.3; -; Genomic_DNA.
DR PIR; T20855; T20855.
DR RefSeq; NP_001122453.2; NM_001128981.3. [Q19420-1]
DR RefSeq; NP_001122454.2; NM_001128982.3. [Q19420-2]
DR AlphaFoldDB; Q19420; -.
DR SMR; Q19420; -.
DR BioGRID; 37919; 1.
DR STRING; 6239.F13G3.5a.1; -.
DR EPD; Q19420; -.
DR PaxDb; Q19420; -.
DR PeptideAtlas; Q19420; -.
DR EnsemblMetazoa; F13G3.5a.1; F13G3.5a.1; WBGene00008765. [Q19420-1]
DR EnsemblMetazoa; F13G3.5a.2; F13G3.5a.2; WBGene00008765. [Q19420-1]
DR EnsemblMetazoa; F13G3.5b.1; F13G3.5b.1; WBGene00008765. [Q19420-2]
DR GeneID; 172477; -.
DR KEGG; cel:CELE_F13G3.5; -.
DR UCSC; F13G3.5a; c. elegans. [Q19420-1]
DR CTD; 172477; -.
DR WormBase; F13G3.5a; CE47972; WBGene00008765; ttx-7. [Q19420-1]
DR WormBase; F13G3.5b; CE48079; WBGene00008765; ttx-7. [Q19420-2]
DR eggNOG; KOG2951; Eukaryota.
DR GeneTree; ENSGT00940000169763; -.
DR HOGENOM; CLU_044118_1_0_1; -.
DR InParanoid; Q19420; -.
DR OMA; HAWDCLA; -.
DR OrthoDB; 915621at2759; -.
DR PhylomeDB; Q19420; -.
DR Reactome; R-CEL-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:Q19420; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008765; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; ISS:WormBase.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052834; F:inositol monophosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0031403; F:lithium ion binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0035418; P:protein localization to synapse; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0043052; P:thermotaxis; IMP:UniProtKB.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR020552; Inositol_monoPase_Li-sen.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR00378; LIIMPHPHTASE.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Lithium; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..285
FT /note="Inositol monophosphatase ttx-7"
FT /id="PRO_0000142519"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT VAR_SEQ 159..198
FT /note="LLSKGVLCQSLGLHNRVQFGDRWLDIAQSNMRNQVMAGVR -> FIAESVLI
FT LQLGSIRSPVMQKSFVDSYKTVMFDKQCH (in isoform b)"
FT /evidence="ECO:0000303|PubMed:17158747"
FT /id="VSP_029919"
FT MUTAGEN 216
FT /note="G->E: In nj40; induces defects in thermotaxis."
FT /evidence="ECO:0000269|PubMed:17158747"
SQ SEQUENCE 285 AA; 30994 MW; 4CCC57E06640C7BB CRC64;
MVFQPIHEEE QVFVDYAIEL VKKAGTLVRT AFDSPESKVD TKSSNTDLVT ETDQAVEKLL
IEGLSERFKG HRFIGEESVA GGAKIEWTDA PTWIIDPIDG TTNFVHRIPM IAICVGLAIK
KQIRAGIVYN PITNELYLAQ LGKGAFKNGF PIRASKNQLL SKGVLCQSLG LHNRVQFGDR
WLDIAQSNMR NQVMAGVRGH RSFGSAAINM VMVAQGSCDG YVEYGIHAWD VAAPSIIVTE
AGGVVTDPTG SPFDVMSRKV LCAGTAELGR DLSACLTHVD FEPEA
