Q9N589 · MTMR1_CAEEL
- ProteinPhosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1
- Genemtm-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids588 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lipid phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Negatively regulates accumulation of PI3P on intracellular vesicles (PubMed:19816564, PubMed:21490059).
Negatively regulates phagocytosis of apoptotic cells probably by limiting the recruitment and/or the activation of ced-5, ced-2 and ced-12 complex (PubMed:19816564, PubMed:21490059).
In addition, may positively regulate phagosome maturation by promoting recycling of apoptotic receptor ced-1 back to the plasma membrane (PubMed:21490059).
Essential for embryonic and larval development (PubMed:19816564).
May promote migration of distal tip cells (PubMed:19816564).
Negatively regulates phagocytosis of apoptotic cells probably by limiting the recruitment and/or the activation of ced-5, ced-2 and ced-12 complex (PubMed:19816564, PubMed:21490059).
In addition, may positively regulate phagosome maturation by promoting recycling of apoptotic receptor ced-1 back to the plasma membrane (PubMed:21490059).
Essential for embryonic and larval development (PubMed:19816564).
May promote migration of distal tip cells (PubMed:19816564).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
- 1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 293 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 293 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 316 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 316 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 317 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 317 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Active site | 378 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 379 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 379 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 379 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 380 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 380 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 381 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 381 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 381 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 382 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 382 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 382 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 383 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 383 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 383 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 384 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 384 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 384 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 420 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 424 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 424 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical cortex | |
Cellular Component | apical plasma membrane | |
Cellular Component | cell cortex | |
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | phagocytic cup | |
Cellular Component | plasma membrane | |
Molecular Function | phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity | |
Molecular Function | phosphatidylinositol-3-phosphate phosphatase activity | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Biological Process | negative regulation of endocytosis | |
Biological Process | negative regulation of engulfment of apoptotic cell | |
Biological Process | phagocytosis | |
Biological Process | phosphatidylinositol dephosphorylation | |
Biological Process | phospholipid dephosphorylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ9N589
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Apical cell membrane ; Peripheral membrane protein
Note: Transiently co-localizes with phagocytic receptor ced-1 at the pseudopods during phagocytosis of apoptotic cells.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown causes an increase in PI3P levels in intracellular vesicles. Also causes an increase in germline cell corpse engulfment, although corpses fail to be cleared. RNAi-mediated knockdown in ced-1, ced-6, ced-2, ced-10 or ced-7 mutant background partially restores cell corpses engulfment.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 106 | In op309; severe reduction in PI3P and PI(3,5)P2 dephosphorylation. Increased levels of PI3P in intracellular vesicles. Restores the engulfment of cell corpses in a ced-6 n1813 mutant background. | ||||
Sequence: G → E |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000436175 | 1-588 | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1 | |||
Sequence: MDDRGNNSGEVGEFASSSMIQESIDLKLLAAESLIWTEKNVTYFGPLGKFPGKIVITRYRMVFLVGDGGKMYEQWKLDIPLGQVSRIEKVGRKTTSVAKRGDDNYGFTIYCKDYRVYRFTCNPASSDRKNVCDSLNRYAFPLSHNLPMFASVHAAETPRLMKDGWKIYSAEKEYERLGIPNSRLWKEVDINKDYKFSETYPRTFVIPTVSWEEGKPFVKKLGEFRSKERIPVLSWINQTTLASISRCSQPMTGISGKRSAEDERHLTNIMNANANCRELLILDARPAVNAKLNKAKGGGYEENYVNAPLTFLNIHNIHVVRDSLKRLLAALIPRVDEKGYYKALDESKWLNHVQSILEGAVKAVFNVDTEKQSVLIHCSDGWDRTAQLTSLAMIQLDSYYRTIEGFIVLIEKEWCSFGHKFGERIGHGDDNYSDGERSPVFVQFCDCLWQIMRQFPWAFEFTQELLICMLDELYACRYGTFLYNSEKIRLKDKKCDETTISFWSYVLENKKKFRNPMFKHGKSNKVINVNPSLCGLHVWIDYYARSNPYVVTPNHEDVQQPGAQFVDEKKQLLDEIMALDDAAQKLTA |
Proteomic databases
Expression
Tissue specificity
Expressed in embryo, larva and in adults (PubMed:19816564, PubMed:21490059).
Expressed in a few head and tail neurons (PubMed:12788949).
Expressed in hypodermis, body wall and pharyngeal muscles, sheath cells, vulva, distal tip cells and coelomocytes (PubMed:19816564, PubMed:21490059).
Expressed in a few head and tail neurons (PubMed:12788949).
Expressed in hypodermis, body wall and pharyngeal muscles, sheath cells, vulva, distal tip cells and coelomocytes (PubMed:19816564, PubMed:21490059).
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-91 | GRAM | ||||
Sequence: IQESIDLKLLAAESLIWTEKNVTYFGPLGKFPGKIVITRYRMVFLVGDGGKMYEQWKLDIPLGQVSRIEKVG | ||||||
Domain | 164-543 | Myotubularin phosphatase | ||||
Sequence: GWKIYSAEKEYERLGIPNSRLWKEVDINKDYKFSETYPRTFVIPTVSWEEGKPFVKKLGEFRSKERIPVLSWINQTTLASISRCSQPMTGISGKRSAEDERHLTNIMNANANCRELLILDARPAVNAKLNKAKGGGYEENYVNAPLTFLNIHNIHVVRDSLKRLLAALIPRVDEKGYYKALDESKWLNHVQSILEGAVKAVFNVDTEKQSVLIHCSDGWDRTAQLTSLAMIQLDSYYRTIEGFIVLIEKEWCSFGHKFGERIGHGDDNYSDGERSPVFVQFCDCLWQIMRQFPWAFEFTQELLICMLDELYACRYGTFLYNSEKIRLKDKKCDETTISFWSYVLENKKKFRNPMFKHGKSNKVINVNPSLCGLHVWIDYY | ||||||
Coiled coil | 563-588 | |||||
Sequence: AQFVDEKKQLLDEIMALDDAAQKLTA |
Domain
The GRAM domain is required for localization to the plasma membrane.
The myotubularin phosphatase domain is required for localization to the plasma membrane.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length588
- Mass (Da)67,593
- Last updated2002-06-01 v2
- Checksum99D74883745D2A28
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284601 EMBL· GenBank· DDBJ | CCD66194.1 EMBL· GenBank· DDBJ | Genomic DNA |