MEC2_CAEEL
ID MEC2_CAEEL Reviewed; 481 AA.
AC Q27433;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mechanosensory protein 2;
GN Name=mec-2 {ECO:0000312|WormBase:F14D12.4a};
GN ORFNames=F14D12.4 {ECO:0000312|WormBase:F14D12.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Bristol N2;
RX PubMed=7477350; DOI=10.1038/378292a0;
RA Huang M., Gu G., Ferguson E.L., Chalfie M.;
RT "A stomatin-like protein necessary for mechanosensation in C. elegans.";
RL Nature 378:292-295(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE DEGENERIN CHANNEL COMPLEX, AND INTERACTION
RP WITH MEC-6 AND MEC-4.
RX PubMed=12478294; DOI=10.1038/nature01205;
RA Chelur D.S., Ernstrom G.G., Goodman M.B., Yao C.A., Chen L., O'Hagan R.,
RA Chalfie M.;
RT "The mechanosensory protein MEC-6 is a subunit of the C. elegans touch-cell
RT degenerin channel.";
RL Nature 420:669-673(2002).
CC -!- FUNCTION: Subunit of an amiloride-sensitive cation channel (degenerin
CC channel complex) permeable for sodium, potassium, lithium and N-
CC methylglucamine, and required for mechanosensory transduction (touch
CC sensitivity) (PubMed:12478294). Positively regulates the activity of
CC the putative mechanosensory transduction channel. May link the
CC mechanosensory channel and the microtubule cytoskeleton of the touch
CC receptor neurons. Required for the function of a set of six touch
CC receptor neurons. {ECO:0000269|PubMed:12478294}.
CC -!- SUBUNIT: Component of a non-voltage-gated amiloride-sensitive cation
CC channel complex (also called the degenerin channel complex) composed of
CC at least the mec-2, mec-4, mec-6 and mec-10 subunits; the complex
CC mediates mechanotransduction in touch cells (PubMed:12478294).
CC Interacts with mec-6 and mec-4 (PubMed:12478294).
CC {ECO:0000269|PubMed:12478294}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U26736; AAA87552.1; -; Genomic_DNA.
DR EMBL; U26735; AAA87551.1; -; mRNA.
DR EMBL; BX284606; CCD83468.1; -; Genomic_DNA.
DR PIR; S60260; S60260.
DR RefSeq; NP_741797.1; NM_171691.3.
DR AlphaFoldDB; Q27433; -.
DR SMR; Q27433; -.
DR BioGRID; 45759; 5.
DR DIP; DIP-61307N; -.
DR IntAct; Q27433; 1.
DR STRING; 6239.F14D12.4a; -.
DR TCDB; 1.A.6.2.2; the epithelial na(+) channel (enac) family.
DR SwissPalm; Q27433; -.
DR PaxDb; Q27433; -.
DR EnsemblMetazoa; F14D12.4a.1; F14D12.4a.1; WBGene00003166.
DR GeneID; 180826; -.
DR UCSC; F14D12.4a; c. elegans.
DR CTD; 180826; -.
DR WormBase; F14D12.4a; CE04393; WBGene00003166; mec-2.
DR eggNOG; KOG2621; Eukaryota.
DR InParanoid; Q27433; -.
DR OrthoDB; 1062075at2759; -.
DR PhylomeDB; Q27433; -.
DR PRO; PR:Q27433; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003166; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q27433; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0032589; C:neuron projection membrane; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IDA:WormBase.
DR GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IGI:UniProtKB.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:WormBase.
DR GO; GO:1905789; P:positive regulation of detection of mechanical stimulus involved in sensory perception of touch; IGI:UniProtKB.
DR GO; GO:1905792; P:positive regulation of mechanosensory behavior; IGI:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:WormBase.
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; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR10264; PTHR10264; 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 Ion channel; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..481
FT /note="Mechanosensory protein 2"
FT /id="PRO_0000094038"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 51900 MW; 37D2894AD39E040A CRC64;
MSATMSSARN SVVSLSSNGS VKVETRLVSN ERSSSIQQEG AMLPSSSSKD DDLLSTSSDE
VENMATRTLQ QLEESTSIIS ANSDDDSVKK EKQAEKDVEK GNGKEEKANI QNEFGVCGWI
LTILSYLLIF FTLPISACMC IKVVQEYERA VIFRLGRLMP GGAKGPGIFF IVPCIDTYRK
VDLRVLSFEV PPQEILSKDS VTVAVDAVVY FRISNATISV TNVEDAARST KLLAQTTLRN
ILGTKTLAEM LSDREAISHQ MQTTLDEATE PWGVKVERVE VKDVRLPVQL QRAMAAEAEA
AREARAKVIV AEGEQKASRA LKEAAEVIAE SPSALQLRYL QTLNSISAEK NSTIIFPFPI
DLLSAFLQRT PPKVEEPPSL PKKIRSCCLY KYPDWVQGMV GSEGGGGHGH SHGGGGGGLG
SSQGAFHPSQ AGSGPSTTTT SGRPLLRSMR EAQFHSAAPP ISAPNQSQTS VSQLDPALLI
R