Q9EP69 · SAC1_MOUSE
- ProteinPhosphatidylinositol-3-phosphatase SAC1
- GeneSacm1l
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids587 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 3-phosphate (PtdIns3P) and has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:32931550).
Shows a very robust PtdIns4P phosphatase activity when it binds PtdIns4P in a 'cis' configuration in the cellular environment, with much less activity seen when it binds PtdIns4P in 'trans' configuration (By similarity).
PtdIns4P phosphatase activity (when it binds PtdIns4P in 'trans' configuration) is enhanced in the presence of PLEKHA3 (By similarity).
Shows a very robust PtdIns4P phosphatase activity when it binds PtdIns4P in a 'cis' configuration in the cellular environment, with much less activity seen when it binds PtdIns4P in 'trans' configuration (By similarity).
PtdIns4P phosphatase activity (when it binds PtdIns4P in 'trans' configuration) is enhanced in the presence of PLEKHA3 (By similarity).
Catalytic activity
- 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.
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphateThis reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | AMPA glutamate receptor complex | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | endoplasmic reticulum-plasma membrane contact site | |
Cellular Component | glutamatergic synapse | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Molecular Function | phosphatase activity | |
Molecular Function | phosphatidylinositol-3,5-bisphosphate phosphatase activity | |
Molecular Function | phosphatidylinositol-3-phosphate phosphatase activity | |
Molecular Function | phosphatidylinositol-4-phosphate phosphatase activity | |
Biological Process | exocytic insertion of neurotransmitter receptor to postsynaptic membrane | |
Biological Process | neurotransmitter receptor transport to postsynaptic membrane | |
Biological Process | phosphatidylinositol dephosphorylation | |
Biological Process | vesicle-mediated transport in synapse |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol-3-phosphatase SAC1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9EP69
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Golgi apparatus membrane ; Multi-pass membrane protein
Note: Trafficking between the ER and Golgi is regulated by nutrient status and by TMEM39A. Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) in the presence of phosphatidylinositol-4,5-bisphosphate.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-520 | Cytoplasmic | ||||
Sequence: MAAAAYEHLKLHITPEKFYVEACDDGADDVLIIDRVSTEVTLAVKKDVPPSAVTRPIFGILGTIHLVAGNYLVVITKKMKVGECFNHAVWRATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLSMDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYSGNRASFVQTRGSIPIFWSQRPNLKYKPHPQISKVANHMDGFQRHFDSQVIIYGKQVIINLVNHKGSEKPLEQTFANMVSSLGSGMIRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGKVVTNQDGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKTYKNAWADNANACAKQYAGTGALKTDFTRTGKRTQLGLLMDGFNSLLRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWK | ||||||
Transmembrane | 521-541 | Helical | ||||
Sequence: FLALPIIMVVAFSMCIICLLM | ||||||
Topological domain | 542-548 | Lumenal | ||||
Sequence: AGDTWTE | ||||||
Transmembrane | 549-569 | Helical | ||||
Sequence: TLAYVLFWGVASIGTFFIILY | ||||||
Topological domain | 570-587 | Cytoplasmic | ||||
Sequence: NGKDFVDAPRLVQKEKID |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000317172 | 1-587 | Phosphatidylinositol-3-phosphatase SAC1 | |||
Sequence: MAAAAYEHLKLHITPEKFYVEACDDGADDVLIIDRVSTEVTLAVKKDVPPSAVTRPIFGILGTIHLVAGNYLVVITKKMKVGECFNHAVWRATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLSMDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYSGNRASFVQTRGSIPIFWSQRPNLKYKPHPQISKVANHMDGFQRHFDSQVIIYGKQVIINLVNHKGSEKPLEQTFANMVSSLGSGMIRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGKVVTNQDGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKTYKNAWADNANACAKQYAGTGALKTDFTRTGKRTQLGLLMDGFNSLLRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID | ||||||
Modified residue | 456 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in brain, lung, liver and kidney, and at lower levels in spleen and skeletal muscle.
Gene expression databases
Interaction
Subunit
Interacts with TMEM39A (By similarity).
Interacts with SEC23A and SEC24A; this interaction is reduced in the absence of TMEM39A (By similarity).
Interacts with PLEKHA3 and VAPA and/or VAPB to form a ternary complex (By similarity).
Interacts with SACM1L; the interaction regulates SACM1L phosphatidylinositol-3-phosphatase activity and translocation to endoplasmic reticulum/trans Golgi network in a malonyl-CoA dependent manner (PubMed:32931550).
Interacts with SEC23A and SEC24A; this interaction is reduced in the absence of TMEM39A (By similarity).
Interacts with PLEKHA3 and VAPA and/or VAPB to form a ternary complex (By similarity).
Interacts with SACM1L; the interaction regulates SACM1L phosphatidylinositol-3-phosphatase activity and translocation to endoplasmic reticulum/trans Golgi network in a malonyl-CoA dependent manner (PubMed:32931550).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9EP69 | pipB2 A0A0F6B5H5 | 3 | EBI-6908224, EBI-27033185 | |
XENO | Q9EP69 | sseL A0A0F6B423 | 4 | EBI-6908224, EBI-13953897 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 122-451 | SAC | ||||
Sequence: LNHVLSMDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYSGNRASFVQTRGSIPIFWSQRPNLKYKPHPQISKVANHMDGFQRHFDSQVIIYGKQVIINLVNHKGSEKPLEQTFANMVSSLGSGMIRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGKVVTNQDGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKTYKNAWADNANACAKQYAG | ||||||
Region | 452-587 | Essential for phosphatidylinositol-4-phosphate phosphatase activity | ||||
Sequence: TGALKTDFTRTGKRTQLGLLMDGFNSLLRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length587
- Mass (Da)66,944
- Last updated2001-03-01 v1
- ChecksumBCC73A3A2B912C98
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F8MPK9 | A0A5F8MPK9_MOUSE | Sacm1l | 609 | ||
A0A1L1SR59 | A0A1L1SR59_MOUSE | Sacm1l | 36 |
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ297526 EMBL· GenBank· DDBJ | CAC01937.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ245720 EMBL· GenBank· DDBJ | CAC20672.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122390 EMBL· GenBank· DDBJ | BAC65672.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK089174 EMBL· GenBank· DDBJ | BAC40778.1 EMBL· GenBank· DDBJ | mRNA | ||
AK161111 EMBL· GenBank· DDBJ | BAE36196.1 EMBL· GenBank· DDBJ | mRNA | ||
AK171080 EMBL· GenBank· DDBJ | BAE42234.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005489 EMBL· GenBank· DDBJ | AAH05489.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117752 EMBL· GenBank· DDBJ | AAI17753.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117753 EMBL· GenBank· DDBJ | AAI17754.1 EMBL· GenBank· DDBJ | mRNA |