Q22712 · MTMR3_CAEEL
- ProteinPhosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3
- Genemtm-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1006 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Preferentially dephosphorylates phosphatidylinositol 3-phosphate (PI3P), and has some activity towards phosphatidylinositol 3,5-bisphosphate (PI35P) (PubMed:18393358, PubMed:25124690).
Positively regulates autophagy and is recruited to autophagosomes by PI3P where it catalyzes PI3P turnover to promote autophagosome maturation (PubMed:25124690).
Thought to have a role in maintenance of muscle function (PubMed:18393358).
Involved in locomotion and lifespan determination (PubMed:18393358).
Positively regulates autophagy and is recruited to autophagosomes by PI3P where it catalyzes PI3P turnover to promote autophagosome maturation (PubMed:25124690).
Thought to have a role in maintenance of muscle function (PubMed:18393358).
Involved in locomotion and lifespan determination (PubMed:18393358).
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-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + 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
Activity regulation
Inhibited by sodium vanadate and peroxide.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 377 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 377 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 402 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 402 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 403 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 403 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Active site | 463 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 464 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 464 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 465 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 465 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 466 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 466 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 467 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 467 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 468 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 468 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 469 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 469 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 505 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 509 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 509 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 824 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 827 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 845 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 848 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 853 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 856 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 875 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 878 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3
- 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 accessionQ22712
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Worms exhibit a 2-fold increase in PI3P, sluggish body movement with progressive deterioration and defects in gestation.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 67-1006 | In tm4475; viable but display 36% embryonic lethality and 45% larval arrest. Reduces survival of L1 larvae in nutrient-deprived conditions. Defective autophagosome maturation and degradation of autophagic protein aggregates. | ||||
Sequence: Missing | ||||||
Mutagenesis | 463 | Abolished phosphatase activity towards phosphatidylinositol 3-phosphate (PI3P) phosphatidylinositol 3,5-bisphosphate (PI35P). | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094947 | 1-1006 | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 | |||
Sequence: MTVTSSAAIDIGGGGGGRRSDRLDSDRTSEDMSFIASPANESFQIGASFVDVQNESSGSIDTATATLHELNYTFGMPPVTEESENMPQNYETVVELLPGEERAPINKLTEFPIEGGSLFVTNFRIVVILKDKEVEEALRFLVFPLQDIEQIDLAIPAFIHLSLKIGRMFTICFKTAEDAALVHKILYTAFQRLNRPISSIYTSRPQDWTSKNTDNPMQSLNAFAWKFSEAVDELDRDGKLPSWLLRADSVAQEITHIDFNRLGMSEHFQISSVNENFEVCPTYPEKIIVPKGITDDDIRKGAPYRSIGRFPAVIWRCRKTRAVLMRSSQPQVGILSWRNPTDEKIIEEAVKASRIEGEEKKQFIIMDARGYTSAFANRARSGGFENTEYYQQAKLEFLGLPNIHAVRGSFNNVRTMLHNLGPNEQLLTSLQTTGWLLNLSNLLVNAANCADHLSKGHSVLVHCSDGWDRTTQVTTLAKIMLDEYYRTVKGFEELIRRDWIAFGHKLYDRQLVAFGNWGTSDERSPVFLQFLEAVRHLQREQPTLFQFTHAYLIKLAKHAYSGLFGSFLFNSHKERREAMEKCKGTLVDIWRFIGPHNEEYVNQSFDEHYTGAVKPVNVSVINLRVWHEVFADEEEHYTQIFSPKEERPLSGCTTPMNTSTSTNLVKSKSSESINSLNVDGSAKESSQQHPTCSTTPSDNTNSLPMSTSFIQQSLYQPKVRGVAAIDRDGVIRFEDDEQAMLRKKNKLRAEEIRRKDEKIEELRRRAVLDTNKVSPGQRQSYSESDVETTGTLERVMSDVSMVDPVNELPHFKPNTTWEGESGHCAYCKKEFNKLSVYVEDRQHHCRNCGRVVCEDCSKNRFSVIEEGKSVQKRACDSCYDSMHETDLKLSSSSTTTTSSSTKIENDSNVPGLDNNSDNVSENVSENAIPDIIVEEKEAEDPIKEAESPSKETKCPKTLRNFISFSPKSSMRKNKVHSRDPLKSIDEGSSSQQAESDDVLDVNEQPL |
Proteomic databases
Expression
Tissue specificity
Expressed in the body wall muscle and in eggs (PubMed:18393358).
Expressed in head neurons (PubMed:12788949).
Expressed in the intestine (PubMed:18393358, PubMed:25124690).
Expressed in pharyngeal cells, vulval muscle cells and cells of the tail region (PubMed:25124690).
Expressed in head neurons (PubMed:12788949).
Expressed in the intestine (PubMed:18393358, PubMed:25124690).
Expressed in pharyngeal cells, vulval muscle cells and cells of the tail region (PubMed:25124690).
Developmental stage
Expressed in most cells during embryogenesis (PubMed:25124690).
Expressed most strongly in the egg with expression present in L1 but reducing through to L3 where it is very weak. No expression was found in L4. Strong expression is also seen in egg-laying adults and post-reproductive adults
Expressed most strongly in the egg with expression present in L1 but reducing through to L3 where it is very weak. No expression was found in L4. Strong expression is also seen in egg-laying adults and post-reproductive adults
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MTVTSSAAIDIGGGGGGRRSDRLDSDRTS | ||||||
Domain | 224-630 | Myotubularin phosphatase | ||||
Sequence: AWKFSEAVDELDRDGKLPSWLLRADSVAQEITHIDFNRLGMSEHFQISSVNENFEVCPTYPEKIIVPKGITDDDIRKGAPYRSIGRFPAVIWRCRKTRAVLMRSSQPQVGILSWRNPTDEKIIEEAVKASRIEGEEKKQFIIMDARGYTSAFANRARSGGFENTEYYQQAKLEFLGLPNIHAVRGSFNNVRTMLHNLGPNEQLLTSLQTTGWLLNLSNLLVNAANCADHLSKGHSVLVHCSDGWDRTTQVTTLAKIMLDEYYRTVKGFEELIRRDWIAFGHKLYDRQLVAFGNWGTSDERSPVFLQFLEAVRHLQREQPTLFQFTHAYLIKLAKHAYSGLFGSFLFNSHKERREAMEKCKGTLVDIWRFIGPHNEEYVNQSFDEHYTGAVKPVNVSVINLRVWHEVF | ||||||
Region | 641-705 | Disordered | ||||
Sequence: FSPKEERPLSGCTTPMNTSTSTNLVKSKSSESINSLNVDGSAKESSQQHPTCSTTPSDNTNSLPM | ||||||
Compositional bias | 651-705 | Polar residues | ||||
Sequence: GCTTPMNTSTSTNLVKSKSSESINSLNVDGSAKESSQQHPTCSTTPSDNTNSLPM | ||||||
Zinc finger | 818-883 | FYVE-type | ||||
Sequence: EGESGHCAYCKKEFNKLSVYVEDRQHHCRNCGRVVCEDCSKNRFSVIEEGKSVQKRACDSCYDSMH | ||||||
Compositional bias | 886-925 | Polar residues | ||||
Sequence: DLKLSSSSTTTTSSSTKIENDSNVPGLDNNSDNVSENVSE | ||||||
Region | 886-1006 | Disordered | ||||
Sequence: DLKLSSSSTTTTSSSTKIENDSNVPGLDNNSDNVSENVSENAIPDIIVEEKEAEDPIKEAESPSKETKCPKTLRNFISFSPKSSMRKNKVHSRDPLKSIDEGSSSQQAESDDVLDVNEQPL | ||||||
Compositional bias | 930-953 | Basic and acidic residues | ||||
Sequence: DIIVEEKEAEDPIKEAESPSKETK | ||||||
Compositional bias | 954-970 | Polar residues | ||||
Sequence: CPKTLRNFISFSPKSSM | ||||||
Compositional bias | 984-998 | Polar residues | ||||
Sequence: IDEGSSSQQAESDDV |
Domain
Interacts with phosphatidylinositol 3-phosphate (PI3P) via the FYVE-type domain.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q22712-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Namea
- Length1,006
- Mass (Da)113,614
- Last updated2008-09-02 v2
- ChecksumBEFC03296E74DB1A
Q22712-2
- Nameb
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035035 | 41-44 | in isoform b | |||
Sequence: Missing | ||||||
Compositional bias | 651-705 | Polar residues | ||||
Sequence: GCTTPMNTSTSTNLVKSKSSESINSLNVDGSAKESSQQHPTCSTTPSDNTNSLPM | ||||||
Compositional bias | 886-925 | Polar residues | ||||
Sequence: DLKLSSSSTTTTSSSTKIENDSNVPGLDNNSDNVSENVSE | ||||||
Alternative sequence | VSP_035036 | 891-965 | in isoform b | |||
Sequence: SSSTTTTSSSTKIENDSNVPGLDNNSDNVSENVSENAIPDIIVEEKEAEDPIKEAESPSKETKCPKTLRNFISFS → RATSLSEMSSFDSFGPSSPPASSTSSSSLNMLASMSPTRPQPIPISCKSSSNSISSPRPSPGEFSRHSSTQAVKG | ||||||
Compositional bias | 930-953 | Basic and acidic residues | ||||
Sequence: DIIVEEKEAEDPIKEAESPSKETK | ||||||
Compositional bias | 954-970 | Polar residues | ||||
Sequence: CPKTLRNFISFSPKSSM | ||||||
Alternative sequence | VSP_035037 | 966-1006 | in isoform b | |||
Sequence: Missing | ||||||
Compositional bias | 984-998 | Polar residues | ||||
Sequence: IDEGSSSQQAESDDV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF031519 EMBL· GenBank· DDBJ | AAC78763.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
DQ988041 EMBL· GenBank· DDBJ | ABK59970.1 EMBL· GenBank· DDBJ | mRNA | ||
BX284603 EMBL· GenBank· DDBJ | CAA88884.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284603 EMBL· GenBank· DDBJ | CAB61017.2 EMBL· GenBank· DDBJ | Genomic DNA |