Stomatin-like protein 3 (STOML3)

The protein contains 291 amino acids for an estimated molecular weight of 32135 Da.

 

Required for the function of many mechanoreceptors. Modulate mechanotransduction channels and acid-sensing ion channels (ASIC) proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their sensitivity to mechanical stimulations. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 66%
Model score: 0
No model available.

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No binding partner found

The reference OMIM entry for this protein is 608327

Stomatin-like protein 3; stoml3
Stomatin-related olfactory protein; sro

CLONING

Kobayakawa et al. (2002) cloned mouse Stoml3, which they designated Sro. The deduced 287-amino acid Stoml3 protein has a calculated molecular mass of 32 kD. It contains 2 N-terminal hydrophobic domains followed by a central stomatin (STOM; 133090) signature sequence shared with mouse stomatin and human podocin (604766). Stoml3 shows a combination of beta sheet-rich and alpha helix-rich structures found in other stomatin family members. The N terminus of Stoml3 also has 3 consensus sequences for cys palmitoylation. Northern blot analysis of several mouse tissues detected a 1.8-kb Stoml3 transcript only in olfactory epithelium. In situ hybridization detected mouse Stoml3 transcript only in olfactory sensory neurons (OSNs) of the main olfactory epithelium. It was not detected in vomeronasal neurons. Stoml3 was abundant in most apical dendrites of OSNs, including olfactory cilia. Immunoprecipitation revealed that Stoml3 associated with adenylyl cyclase-3 (600291) and caveolin-1 (601047) in the low-density membrane fraction of olfactory cilia.

GENE FUNCTION

Kobayakawa et al. (2002) found that antibodies raised against mouse Stoml3 stimulated cAMP production in fractionated olfactory cilia membranes. They hypothesized that STOML3 may play a role in modulating odorant signals in the lipid rafts of olfactory cilia.

GENE STRUCTURE

Kobayakawa et al. (2002) identified an OLF1 (164343) motif, which is commonly found in the promoter regions of genes involved in olfactory signaling, within the promoter regions of the mouse and human STOML3 genes.

MAPPING

Hartz (2003) mapped the STOML3 gene to chromosome 13q13 based on an alignment of the STOML3 sequence (GenBank GENBANK BC025760) with the genomic sequence.

ANIMAL MODEL

Wetzel et al. (2007) generated mice deficient in Slp3. They were viable and fertile. Wetzel et al. (2007) found that about 35% of skin mechanoreceptors did not respond to mechanical stimuli in Slp3-deficient mice. In addition, mechanosensitive ion channels found in many sensory neurons did not function without Slp3. Tactile-driven behaviors were also impaired in Slp3 mutant mice, including touch-evoked pain caused by neuropathic injury. Wetzel et al. (2007) concluded that SLP3 is indispensable for the function of a subset of cutaneous mechanoreceptors, and their data supported the idea that this protein is an essential subunit of a mammalian mechanotransducer. ... More on the omim web site

Subscribe to this protein entry history

Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 608327 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).