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MEC6_CAEEL
ID   MEC6_CAEEL              Reviewed;         377 AA.
AC   O01811; Q8T7S8;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Mechanosensory abnormality protein 6;
GN   Name=mec-6 {ECO:0000312|WormBase:W02D3.3};
GN   ORFNames=W02D3.3 {ECO:0000312|WormBase:W02D3.3};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, IDENTIFICATION IN THE DEGENERIN CHANNEL COMPLEX, INTERACTION
RP   WITH MEC-2; MEC-4 AND MEC-10, GLYCOSYLATION, AND MUTAGENESIS OF GLY-235.
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).
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.
RX   PubMed=12385749; DOI=10.1016/s0925-4773(02)00293-9;
RA   Zhang Y., Chalfie M.;
RT   "MTD-1, a touch-cell-specific membrane protein with a subtle effect on
RT   touch sensitivity.";
RL   Mech. Dev. 119:3-7(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). Interacts with degenerin channel
CC       proteins and stabilizes the channel (PubMed:12478294). Plays a role in
CC       mechanosensory transduction (touch sensitivity) (PubMed:12478294,
CC       PubMed:12385749). {ECO:0000269|PubMed:12385749,
CC       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-2, mec-4 and mec-10 (PubMed:12478294).
CC       {ECO:0000269|PubMed:12478294}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12478294};
CC       Single-pass membrane protein {ECO:0000269|PubMed:12478294}. Cell
CC       projection, axon {ECO:0000269|PubMed:12478294}. Note=Co-localizes with
CC       mec-4 in puncta along the axons of touch cell receptor neurons and in
CC       muscles. {ECO:0000269|PubMed:12478294}.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons including the six touch
CC       receptors, ventral cord motor neurons, HSN, PVD, PVC, IL1, and several
CC       neurons near the nerve ring, in the anal ganglion and in the male tail
CC       sensory rays, in muscles including the body wall, vulval, intestinal,
CC       anal depressor and sphincter muscles, and in the excretory canal.
CC       {ECO:0000269|PubMed:12478294}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:12478294}.
CC   -!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}.
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DR   EMBL; AF295927; AAL83724.1; -; mRNA.
DR   EMBL; BX284601; CCD68986.1; -; Genomic_DNA.
DR   PIR; T15204; T15204.
DR   RefSeq; NP_491925.2; NM_059524.5.
DR   AlphaFoldDB; O01811; -.
DR   SMR; O01811; -.
DR   BioGRID; 37837; 4.
DR   STRING; 6239.W02D3.3; -.
DR   TCDB; 1.A.6.2.2; the epithelial na(+) channel (enac) family.
DR   EPD; O01811; -.
DR   PaxDb; O01811; -.
DR   PeptideAtlas; O01811; -.
DR   EnsemblMetazoa; W02D3.3.1; W02D3.3.1; WBGene00003170.
DR   EnsemblMetazoa; W02D3.3.2; W02D3.3.2; WBGene00003170.
DR   EnsemblMetazoa; W02D3.3.3; W02D3.3.3; WBGene00003170.
DR   GeneID; 172389; -.
DR   UCSC; W02D3.3; c. elegans.
DR   CTD; 172389; -.
DR   WormBase; W02D3.3; CE31080; WBGene00003170; mec-6.
DR   eggNOG; ENOG502S6UP; Eukaryota.
DR   GeneTree; ENSGT00390000008932; -.
DR   HOGENOM; CLU_049839_1_0_1; -.
DR   InParanoid; O01811; -.
DR   OMA; YEMMLLT; -.
DR   OrthoDB; 888266at2759; -.
DR   PhylomeDB; O01811; -.
DR   Reactome; R-CEL-2142688; Synthesis of 5-eicosatetraenoic acids.
DR   Reactome; R-CEL-9754706; Atorvastatin ADME.
DR   PRO; PR:O01811; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003170; Expressed in embryo and 3 other tissues.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004064; F:arylesterase activity; IEA:InterPro.
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; IMP:UniProtKB.
DR   GO; GO:0007638; P:mechanosensory behavior; IMP:UniProtKB.
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; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase.
DR   Pfam; PF01731; Arylesterase; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Hydrolase;
KW   Ion channel; Ion transport; Membrane; Neurodegeneration; Potassium;
KW   Potassium transport; Reference proteome; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..377
FT                   /note="Mechanosensory abnormality protein 6"
FT                   /id="PRO_0000142347"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..377
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..369
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         235
FT                   /note="G->R: In u3; does not affect the expression levels.
FT                   Abolishes amiloride-sensitive current. Completely blocks
FT                   mec-4(d)-induced degenerations, and abolishes the punctate
FT                   expression of mec-4 in vivo."
FT                   /evidence="ECO:0000269|PubMed:12478294"
SQ   SEQUENCE   377 AA;  42491 MW;  B8DEBFE45474DAE6 CRC64;
     MGLQSAAAHF INRFIIWITI FMVACFLLRL LVVLDLNKRV YNHTPGPCRV LTDNYKGTAG
     MTYVESQKRV YITLGYGRAH DLKTKTGIAF YKTNRTDGRS QQEMYDLIEM TINWNGYEYK
     KEFIPTGIDS YSSSNGRVLL YVINAHPNHQ CIHFFQIVES SKLNHRKAIC DPSFSSLQDI
     AVVGPDRLFV TNMAAFGRGW AQILEFSLQT GQGAVYYYDG SKLSTAASSL IAPTGIGYDA
     KRRILYVGSM IRESIFAYKV AKDTTLELLY EMMLLTSPIG VFVESKTGDI WIAAHPVIHE
     SAWHYTHPEN QNIHSPSQIL RIRIQEEGNS WVTTEPYAND GATISASSSV VFTDEQMLIG
     SSFGRLLHCD LTHSYIT
 
 
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