P54116 · STOM_MOUSE

  • Protein
    Stomatin
  • Gene
    Stom
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytoskeleton
Cellular Componentendoplasmic reticulum
Cellular Componentmelanosome
Cellular Componentmembrane raft
Cellular Componentmitochondrion
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Molecular Functionidentical protein binding
Molecular Functionion channel inhibitor activity
Molecular Functionprotein homodimerization activity
Molecular FunctionRNA polymerase binding
Biological Processpositive regulation by host of viral genome replication
Biological Processpositive regulation of protein targeting to membrane
Biological Processpositive regulation of viral process
Biological Processregulation of monoatomic ion transmembrane transport

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Stomatin
  • Alternative names
    • Erythrocyte band 7 integral membrane protein
    • Erythrocyte membrane protein band 7.2
    • Protein 7.2b

Gene names

    • Name
      Stom
    • Synonyms
      Epb7.2
      , Epb72

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • BALB/cJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P54116
  • Secondary accessions
    • O88988
    • Q3UP81
    • Q60744
    • Q62455

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Peripheral membrane protein
Cell membrane
; Lipid-anchor
Membrane raft
Melanosome
Cytoplasmic vesicle
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.

TypeIDPosition(s)Description
Topological domain1-31Cytoplasmic
Intramembrane32-52
Topological domain53-284Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis97Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-109 and D-145.
Mutagenesis109Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-145.
Mutagenesis145Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-109.
Mutagenesis182Does not abolish interaction with ASIC3, but abolishes regulation of ASIC2 and ASIC3 channel activity.
Mutagenesis197Abolishes homodimerization and oligomerization. Abolishes regulation of ASIC2 and ASIC3 channel activity.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue, lipidation.

TypeIDPosition(s)Description
ChainPRO_00000940281-284Stomatin
Modified residue18Phosphoserine
Lipidation30S-palmitoyl cysteine
Lipidation87S-palmitoyl cysteine
Modified residue161Phosphoserine
Modified residue244Phosphoserine

Keywords

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO P54116Asic3 O352403EBI-8004826, EBI-982374
BINARY P54116Stom P541165EBI-8004826, EBI-8004826

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region265-273Required for homooligomerization
Region267-269Required for lipid raft association
Region273-284Interaction with LANCL1

Sequence similarities

Belongs to the band 7/mec-2 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    284
  • Mass (Da)
    31,375
  • Last updated
    2007-01-09 v3
  • Checksum
    AB7CC0E5FF2DF4A9
MSDKRQSSHVQSQRIPESFRENSKTELGACGWILVAASFFFVIITFPISIWICIKIVKEYERVIIFRLGRILQGGAKGPGLFFILPCTDSLIKVDMRTISFDIPPQEVLTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNALGTKNLSQILSDREEIAHHMQSTLDDATDDWGIKVERVEIKDVKLPVQLQRAMAAEAEAAREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPVDMLQGIMGSNH

Sequence caution

The sequence AAB18857.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict3in Ref. 4; AAC64173
Sequence conflict37in Ref. 2; CAA62503
Sequence conflict40in Ref. 2; CAA62503
Sequence conflict43in Ref. 2; CAA62503
Sequence conflict91in Ref. 2; CAA62503
Sequence conflict273in Ref. 2; CAA62503
Sequence conflict283in Ref. 2; CAA62503

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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