STML3_MOUSE
ID STML3_MOUSE Reviewed; 287 AA.
AC Q6PE84; Q66JM3; Q8K4P4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Stomatin-like protein 3;
DE Short=SLP-3;
DE AltName: Full=Stomatin-related olfactory protein;
GN Name=Stoml3; Synonyms=Sro;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12122055; DOI=10.1523/jneurosci.22-14-05931.2002;
RA Kobayakawa K., Hayashi R., Morita K., Miyamichi K., Oka Y., Tsuboi A.,
RA Sakano H.;
RT "Stomatin-related olfactory protein, SRO, specifically expressed in the
RT murine olfactory sensory neurons.";
RL J. Neurosci. 22:5931-5937(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17167420; DOI=10.1038/nature05394;
RA Wetzel C., Hu J., Riethmacher D., Benckendorff A., Harder L., Eilers A.,
RA Moshourab R., Kozlenkov A., Labuz D., Caspani O., Erdmann B., Machelska H.,
RA Heppenstall P.A., Lewin G.R.;
RT "A stomatin-domain protein essential for touch sensation in the mouse.";
RL Nature 445:206-209(2007).
RN [4]
RP INTERACTION WITH PIEZO1 AND PIEZO2, MUTAGENESIS OF PRO-40; 89-LEU-ARG-90;
RP ARG-90 AND VAL-190, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24662763; DOI=10.1038/ncomms4520;
RA Poole K., Herget R., Lapatsina L., Ngo H.D., Lewin G.R.;
RT "Tuning Piezo ion channels to detect molecular-scale movements relevant for
RT fine touch.";
RL Nat. Commun. 5:3520-3520(2014).
CC -!- FUNCTION: Required for the function of many mechanoreceptors. Modulate
CC mechanotransduction channels and acid-sensing ion channels (ASIC)
CC proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their
CC sensitivity to mechanical stimulations. {ECO:0000269|PubMed:24662763}.
CC -!- SUBUNIT: Homodimer. Interacts with PIEZO1 and PIEZO2.
CC {ECO:0000269|PubMed:24662763}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12122055,
CC ECO:0000269|PubMed:24662763}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:12122055}. Note=Detected in lipid rafts, in apical
CC dendrites and in olfactory cilia.
CC -!- TISSUE SPECIFICITY: Expressed by all dorsal root ganglion neurons and
CC is selectively expressed in neuronal tissues. Detected in olfactory
CC epithelium. {ECO:0000269|PubMed:12122055, ECO:0000269|PubMed:17167420}.
CC -!- DISRUPTION PHENOTYPE: In deficient mice 35% of skin mechanoreceptors do
CC not respond to mechanical stimuli. In addition, mechanosensitive ion
CC channels find in many sensory neurons do not function. Tactile-driven
CC behaviors are also impaired in mutant mice, including touch-evoked pain
CC caused by neuropathic injury. {ECO:0000269|PubMed:17167420}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58224.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH80859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB085692; BAC05692.1; -; mRNA.
DR EMBL; BC058224; AAH58224.1; ALT_INIT; mRNA.
DR EMBL; BC080859; AAH80859.1; ALT_INIT; mRNA.
DR CCDS; CCDS17347.1; -.
DR RefSeq; NP_694796.1; NM_153156.1.
DR AlphaFoldDB; Q6PE84; -.
DR SMR; Q6PE84; -.
DR BioGRID; 230826; 2.
DR STRING; 10090.ENSMUSP00000029307; -.
DR PhosphoSitePlus; Q6PE84; -.
DR jPOST; Q6PE84; -.
DR MaxQB; Q6PE84; -.
DR PaxDb; Q6PE84; -.
DR PRIDE; Q6PE84; -.
DR ProteomicsDB; 254592; -.
DR Antibodypedia; 2442; 105 antibodies from 18 providers.
DR DNASU; 229277; -.
DR Ensembl; ENSMUST00000029307; ENSMUSP00000029307; ENSMUSG00000027744.
DR GeneID; 229277; -.
DR KEGG; mmu:229277; -.
DR UCSC; uc008pew.1; mouse.
DR CTD; 161003; -.
DR MGI; MGI:2388072; Stoml3.
DR VEuPathDB; HostDB:ENSMUSG00000027744; -.
DR eggNOG; KOG2621; Eukaryota.
DR GeneTree; ENSGT01030000234614; -.
DR HOGENOM; CLU_024949_3_0_1; -.
DR InParanoid; Q6PE84; -.
DR OMA; MFQVTDP; -.
DR OrthoDB; 1062075at2759; -.
DR PhylomeDB; Q6PE84; -.
DR TreeFam; TF105750; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 229277; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Stoml3; mouse.
DR PRO; PR:Q6PE84; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6PE84; protein.
DR Bgee; ENSMUSG00000027744; Expressed in olfactory epithelium and 23 other tissues.
DR ExpressionAtlas; Q6PE84; baseline and differential.
DR Genevisible; Q6PE84; MM.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR043202; Band-7_stomatin-like.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
DR InterPro; IPR028519; SLP3.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR PANTHER; PTHR10264:SF49; PTHR10264:SF49; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR PROSITE; PS01270; BAND_7; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..287
FT /note="Stomatin-like protein 3"
FT /id="PRO_0000094034"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27105"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27105"
FT MUTAGEN 40
FT /note="P->S: Mis-localization predominantly to the
FT cytoplasmic compartment."
FT /evidence="ECO:0000269|PubMed:24662763"
FT MUTAGEN 89..90
FT /note="LR->EE: Abolishes the activity of STOML3."
FT /evidence="ECO:0000269|PubMed:24662763"
FT MUTAGEN 90
FT /note="R->S: Abolishes STOML3 modulation of
FT mechanosensitive currents."
FT /evidence="ECO:0000269|PubMed:24662763"
FT MUTAGEN 190
FT /note="V->P: Reduced oligomerization. Does not sensitize
FT mechanically gated currents."
FT /evidence="ECO:0000269|PubMed:24662763"
FT CONFLICT 220
FT /note="E -> V (in Ref. 2; AAH80859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 31591 MW; BD8FAC8A6E998AD6 CRC64;
MDSPEKLEKN NLVGTNKSRL GVCGWILFFL SFLLMLVTFP ISVWMCLKII KEYERAVVFR
LGRIQADKAK GPGLILVLPC IDVFVKVDLR TVTCNIPPQE ILTRDSVTTQ VDGVVYYRIY
SAVSAVANVN DVHQATFLLA QTTLRNVLGT QTLSQILSGR EEIAHSIQTL LDDATELWGI
RVARVEIKDV RIPVQLQRSM AAEAEATREA RAKVLAAEGE MNASKSLKSA SMVLAESPVA
LQLRYLQTLT TVATEKNSTI VFPLPMNILE GIGGISYGNN KKVTAKA
