A0A8C3SVL1 · A0A8C3SVL1_CHESE
- ProteinPhosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids571 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate. Regulates the level of these phosphoinositides critical for various biological processes including autophagy initiation and autophagosome maturation.
Catalytic activity
- 1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphateThis reaction proceeds in the forward direction.
- 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphateThis reaction proceeds in the forward direction.
- 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) + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 258-261 | substrate | ||||
Sequence: NKAK | ||||||
Binding site | 283-284 | substrate | ||||
Sequence: NI | ||||||
Active site | 345 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 345-351 | substrate | ||||
Sequence: CSDGWDR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | early endosome membrane | |
Molecular Function | phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity | |
Molecular Function | phosphatidylinositol-3-phosphate phosphatase activity | |
Biological Process | phosphatidylinositol dephosphorylation |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Durocryptodira > Americhelydia > Chelydroidea > Chelydridae > Chelydra
Accessions
- Primary accessionA0A8C3SVL1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Early endosome membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MMVSELLLFSFFHLLA | ||||||
Chain | PRO_5034057806 | 17-571 | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2 | |||
Sequence: KDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGASSRGENSYGLEIVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLPLFAFEYREVFPENGWKVYDPILEYRRQGIPNESWRITKINERYELCDTYPAILVVPVNIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQSIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLSMLILDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNDCFLMIILDHLYSCLFGTFLCSSEQQRVKESLPKKTLSLWSYINSQLEDFTNPLYVCYSNHVLYPVASMRHLELWVGYYIRWNPRMKPQEPVHSRYKELLAKRAELQKKVEELQREITNRSTSSSERAGSPAQCVTPVQTVV |
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 133-508 | Myotubularin phosphatase | ||||
Sequence: GWKVYDPILEYRRQGIPNESWRITKINERYELCDTYPAILVVPVNIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQSIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLSMLILDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNDCFLMIILDHLYSCLFGTFLCSSEQQRVKESLPKKTLSLWSYINSQLEDFTNPLYVCYSNHVLYPVASMRHLELWVGYY | ||||||
Domain | 314-361 | Tyrosine specific protein phosphatases | ||||
Sequence: THWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLSML | ||||||
Region | 544-571 | Disordered | ||||
Sequence: REITNRSTSSSERAGSPAQCVTPVQTVV | ||||||
Compositional bias | 546-571 | Polar residues | ||||
Sequence: ITNRSTSSSERAGSPAQCVTPVQTVV |
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length571
- Mass (Da)66,073
- Last updated2022-01-19 v1
- Checksum3152C34DED0943DF
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8C3SQL2 | A0A8C3SQL2_CHESE | 643 | |||
A0A8C3SRQ6 | A0A8C3SRQ6_CHESE | 583 | |||
A0A8C3SS37 | A0A8C3SS37_CHESE | 602 | |||
A0A8C3SV56 | A0A8C3SV56_CHESE | 571 | |||
A0A8C3SUK9 | A0A8C3SUK9_CHESE | 577 | |||
A0A8C3SV00 | A0A8C3SV00_CHESE | 569 | |||
A0A8C3STP2 | A0A8C3STP2_CHESE | 641 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 546-571 | Polar residues | ||||
Sequence: ITNRSTSSSERAGSPAQCVTPVQTVV |
Keywords
- Technical term