MEC4_CAEBR
ID MEC4_CAEBR Reviewed; 768 AA.
AC Q17298; A8XNT4; Q613Q9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Degenerin mec-4;
DE AltName: Full=Mechanosensory protein 4;
GN Name=mec-4; ORFNames=CBG16250;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8655580; DOI=10.1083/jcb.133.5.1071;
RA Lai C.C., Hong K., Kinnell M., Chalfie M., Driscoll M.;
RT "Sequence and transmembrane topology of MEC-4, an ion channel subunit
RT required for mechanotransduction in Caenorhabditis elegans.";
RL J. Cell Biol. 133:1071-1081(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Probable sodium channel subunit. May be needed for
CC mechanosensory transduction (touch sensitivity). Negatively regulates
CC the turning step of male mating behavior.
CC {ECO:0000250|UniProtKB:P24612}.
CC -!- SUBUNIT: The channel is probably composed of at least the mec-2, mec-4,
CC mec-6 and mec-10 subunits. {ECO:0000250|UniProtKB:P24612}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. {ECO:0000305}.
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DR EMBL; U53670; AAC47264.1; -; Genomic_DNA.
DR EMBL; HE600961; CAP34173.3; -; Genomic_DNA.
DR AlphaFoldDB; Q17298; -.
DR SMR; Q17298; -.
DR STRING; 6238.CBG16250; -.
DR EnsemblMetazoa; CBG16250.1; CBG16250.1; WBGene00036254.
DR WormBase; CBG16250; CBP37569; WBGene00036254; Cbr-mec-4.
DR eggNOG; KOG4294; Eukaryota.
DR HOGENOM; CLU_017673_0_0_1; -.
DR InParanoid; Q17298; -.
DR OMA; KYNRNEK; -.
DR OrthoDB; 686369at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032589; C:neuron projection membrane; IEA:EnsemblMetazoa.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IEA:EnsemblMetazoa.
DR GO; GO:0007638; P:mechanosensory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0061096; P:negative regulation of turning behavior involved in mating; IEA:EnsemblMetazoa.
DR GO; GO:1905789; P:positive regulation of detection of mechanical stimulus involved in sensory perception of touch; IEA:EnsemblMetazoa.
DR GO; GO:1905792; P:positive regulation of mechanosensory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR004726; Deg-1.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 2.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00867; deg-1; 1.
DR PROSITE; PS01206; ASC; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Neurodegeneration;
KW Reference proteome; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..768
FT /note="Degenerin mec-4"
FT /id="PRO_0000181286"
FT TOPO_DOM 1..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..718
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 187..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 424
FT /note="N -> NI (in Ref. 1; AAC47264)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="R -> G (in Ref. 1; AAC47264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 768 AA; 87127 MW; B6F85FD90F2B26C3 CRC64;
MSWMQNLKNY QHLRDPSEYM SQVYGDPLAY LQENTKFVTE REYYEDFGYG ECFNSSESEV
QCELITGEFD PKLLPYDKRL AWHFKEFCYK TSAHGIPMIG EAPNVYYRAV WVMLFLGCMI
MLYLNAQSVL DKYNRNEKIV DIQLKFDTAP FPAITLCNLN PYKASLATSV DLVKRTLSAF
DGAMGKAGGN KEHDGEKEVI TEAPTTPAPT TKPSRRRGKR DLSGAFFEPG FARCLCGSQG
SSEQEDKDDE KEEEMHETTT RKPFNINDAD EEWDGMEEYD NNEHYENYDV EATTGMNMME
ECQSERTKFD EPTGFDDRCI CAFDRSTHDA WPCFLNGTWE TTECDTCNEH AFCTKDNKTA
KGHRSPCICA PSKFCVAYNG KTPPIEIWTY LQGGTPTEDP NFLEAMGFQG MTDEVAIVTK
AKENMFAMAT LSMQDRERLS TTKRELVHKC SFNGKACDIE ADFLTHIDPV FGSCFTFNHN
RTVNLTSIRA GPMYGLRMLV YVNASDYMPT TEATGVRLTI HDKEDFPFPD TFGYSAPTGY
VSSFGLRLRK MSRLPAPYGD CVPDGKTSDY IYSNYEYSVE GCYRSCFQQL VLKECRCGDP
RFPVPEGARH CDAADPVARR CLDARMNDLG GLHGSFRCRC QQPCRQSIYS VTYSPAKWPS
LSLQIQLGSC NGTAVECNKH YKENGAMVEV FYEQLNFEML TESEAYGFVN LLADFGGQLG
LWCGISFLTC CEFVFLFLET AYMSAEHNYS LYKKKKAEKA KKVASGSF
