P54116 · STOM_MOUSE
- ProteinStomatin
- GeneStom
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids284 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | melanosome | |
Cellular Component | membrane raft | |
Cellular Component | mitochondrion | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | identical protein binding | |
Molecular Function | ion channel inhibitor activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | RNA polymerase binding | |
Biological Process | positive regulation by host of viral genome replication | |
Biological Process | positive regulation of protein targeting to membrane | |
Biological Process | positive regulation of viral process | |
Biological Process | regulation of monoatomic ion transmembrane transport |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStomatin
- 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 accessionP54116
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Cell membrane ; Lipid-anchor
Note: Localizes to juxtanuclear structure probably derived from the Golgi apparatus. Colocalizes with cortical actin microfilaments at small plasma membrane protrusions. Associates with alpha-granular lipid rafts. Translocates from the alpha-granular lipid rafts to the cell membrane on thrombin activation and selectively enriched in released microvesicles. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Features
Showing features for topological domain, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-31 | Cytoplasmic | ||||
Sequence: MSDKRQSSHVQSQRIPESFRENSKTELGACG | ||||||
Intramembrane | 32-52 | |||||
Sequence: WILVAASFFFVIITFPISIWI | ||||||
Topological domain | 53-284 | Cytoplasmic | ||||
Sequence: CIKIVKEYERVIIFRLGRILQGGAKGPGLFFILPCTDSLIKVDMRTISFDIPPQEVLTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNALGTKNLSQILSDREEIAHHMQSTLDDATDDWGIKVERVEIKDVKLPVQLQRAMAAEAEAAREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPVDMLQGIMGSNH |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 97 | Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-109 and D-145. | ||||
Sequence: R → D | ||||||
Mutagenesis | 109 | Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-145. | ||||
Sequence: L → D | ||||||
Mutagenesis | 145 | Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-109. | ||||
Sequence: L → D | ||||||
Mutagenesis | 182 | Does not abolish interaction with ASIC3, but abolishes regulation of ASIC2 and ASIC3 channel activity. | ||||
Sequence: T → W | ||||||
Mutagenesis | 197 | Abolishes homodimerization and oligomerization. Abolishes regulation of ASIC2 and ASIC3 channel activity. | ||||
Sequence: V → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094028 | 1-284 | Stomatin | |||
Sequence: MSDKRQSSHVQSQRIPESFRENSKTELGACGWILVAASFFFVIITFPISIWICIKIVKEYERVIIFRLGRILQGGAKGPGLFFILPCTDSLIKVDMRTISFDIPPQEVLTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNALGTKNLSQILSDREEIAHHMQSTLDDATDDWGIKVERVEIKDVKLPVQLQRAMAAEAEAAREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPVDMLQGIMGSNH | ||||||
Modified residue | 18 | Phosphoserine | ||||
Sequence: S | ||||||
Lipidation | 30 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 87 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 161 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 244 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all sensory neurons of the dorsal root ganglia. In the CNS, expressed in many neurons of the spinal cord, medulla and pons. Expressed only in scattered neurons in the cortex, hippocampus, thalamus and basal ganglia. In the cerebellum, expressed in all Purkinje cells (at protein level). Widely expressed with high levels in heart, liver, skeletal muscle and testis and low levels in lung, brain and spleen.
Developmental stage
First expressed in the developing embryo at 11.5 dpc when target innervation is complete. Expression continues into adulthood.
Gene expression databases
Interaction
Subunit
Interacts with LANCL1 (By similarity).
Interacts with SLC2A1 (By similarity).
Interacts with SLC4A1; this interaction positively regulates SLC4A1 activity (By similarity).
Identified in large complexes with SLC40A1, SLC14A1, SLC29A1 and AQP1 (By similarity).
Homodimer and higher order homooligomers (By similarity).
The homodimer is banana-shaped (By similarity).
Interacts with ASIC1, ASIC2 and ASIC3 (PubMed:15471860, PubMed:22850675).
Interacts with STOML1; may redistribute STOM from the plasma membrane to late endosomes (By similarity).
Interacts with SLC2A1 (By similarity).
Interacts with SLC4A1; this interaction positively regulates SLC4A1 activity (By similarity).
Identified in large complexes with SLC40A1, SLC14A1, SLC29A1 and AQP1 (By similarity).
Homodimer and higher order homooligomers (By similarity).
The homodimer is banana-shaped (By similarity).
Interacts with ASIC1, ASIC2 and ASIC3 (PubMed:15471860, PubMed:22850675).
Interacts with STOML1; may redistribute STOM from the plasma membrane to late endosomes (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P54116 | Asic3 O35240 | 3 | EBI-8004826, EBI-982374 | |
BINARY | P54116 | Stom P54116 | 5 | EBI-8004826, EBI-8004826 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 265-273 | Required for homooligomerization | ||||
Sequence: STIVFPLPV | ||||||
Region | 267-269 | Required for lipid raft association | ||||
Sequence: IVF | ||||||
Region | 273-284 | Interaction with LANCL1 | ||||
Sequence: VDMLQGIMGSNH |
Sequence similarities
Belongs to the band 7/mec-2 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length284
- Mass (Da)31,375
- Last updated2007-01-09 v3
- ChecksumAB7CC0E5FF2DF4A9
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 4; AAC64173 | ||||
Sequence: D → V | ||||||
Sequence conflict | 37 | in Ref. 2; CAA62503 | ||||
Sequence: A → V | ||||||
Sequence conflict | 40 | in Ref. 2; CAA62503 | ||||
Sequence: F → I | ||||||
Sequence conflict | 43 | in Ref. 2; CAA62503 | ||||
Sequence: I → L | ||||||
Sequence conflict | 91 | in Ref. 2; CAA62503 | ||||
Sequence: L → F | ||||||
Sequence conflict | 273 | in Ref. 2; CAA62503 | ||||
Sequence: V → I | ||||||
Sequence conflict | 283 | in Ref. 2; CAA62503 | ||||
Sequence: N → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U17297 EMBL· GenBank· DDBJ | AAA75024.1 EMBL· GenBank· DDBJ | mRNA | ||
X91043 EMBL· GenBank· DDBJ | CAA62503.1 EMBL· GenBank· DDBJ | mRNA | ||
U50999 EMBL· GenBank· DDBJ | AAB18857.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
U50993 EMBL· GenBank· DDBJ | AAB18857.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
U50994 EMBL· GenBank· DDBJ | AAB18857.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
U50995 EMBL· GenBank· DDBJ | AAB18857.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
U50996 EMBL· GenBank· DDBJ | AAB18857.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
U50997 EMBL· GenBank· DDBJ | AAB18857.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
U50998 EMBL· GenBank· DDBJ | AAB18857.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AF093620 EMBL· GenBank· DDBJ | AAC64173.1 EMBL· GenBank· DDBJ | mRNA | ||
AK139242 EMBL· GenBank· DDBJ | BAE23930.1 EMBL· GenBank· DDBJ | mRNA | ||
AK143724 EMBL· GenBank· DDBJ | BAE25516.1 EMBL· GenBank· DDBJ | mRNA | ||
AK148975 EMBL· GenBank· DDBJ | BAE28708.1 EMBL· GenBank· DDBJ | mRNA | ||
AK149689 EMBL· GenBank· DDBJ | BAE29028.1 EMBL· GenBank· DDBJ | mRNA | ||
AK149821 EMBL· GenBank· DDBJ | BAE29103.1 EMBL· GenBank· DDBJ | mRNA | ||
AK149991 EMBL· GenBank· DDBJ | BAE29219.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151129 EMBL· GenBank· DDBJ | BAE30137.1 EMBL· GenBank· DDBJ | mRNA |