MEC4_CAEEL
ID MEC4_CAEEL Reviewed; 768 AA.
AC P24612;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Degenerin mec-4;
DE AltName: Full=Mechanosensory abnormality protein 4;
GN Name=mec-4 {ECO:0000312|WormBase:T01C8.7};
GN Synonyms=mec-13 {ECO:0000312|WormBase:T01C8.7};
GN ORFNames=T01C8.7 {ECO:0000312|WormBase:T01C8.7};
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
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=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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 271-768, AND MUTAGENESIS OF ALA-713.
RC STRAIN=Bristol N2;
RX PubMed=1672038; DOI=10.1038/349588a0;
RA Driscoll M., Chalfie M.;
RT "The mec-4 gene is a member of a family of Caenorhabditis elegans genes
RT that can mutate to induce neuronal degeneration.";
RL Nature 349:588-593(1991).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE DEGENERIN CHANNEL COMPLEX, INTERACTION WITH
RP MEC-2; MEC-6 AND MEC-10, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-230.
RX PubMed=17611271; DOI=10.1523/jneurosci.1405-07.2007;
RA Liu T., Kim K., Li C., Barr M.M.;
RT "FMRFamide-like neuropeptides and mechanosensory touch receptor neurons
RT regulate male sexual turning behavior in Caenorhabditis elegans.";
RL J. Neurosci. 27:7174-7182(2007).
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:8655580, PubMed:12478294). Negatively regulates
CC the turning step of male mating behavior (PubMed:17611271).
CC {ECO:0000269|PubMed:12478294, ECO:0000269|PubMed:17611271,
CC ECO:0000269|PubMed:8655580}.
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-6 and mec-10 (PubMed:12478294).
CC {ECO:0000269|PubMed:12478294}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:12478294}. Note=Co-localizes with mec-6 in touch
CC neuron axons. {ECO:0000269|PubMed:12478294}.
CC -!- TISSUE SPECIFICITY: Expressed in AVM, ALM, PVM and PLM touch neurons.
CC {ECO:0000269|PubMed:12478294, ECO:0000269|PubMed:8655580}.
CC -!- MISCELLANEOUS: Mutations in mec-4 results in the degeneration of a
CC small set of neurons which typically swell to several times their
CC normal diameter before they disappear, presumably due to lysis.
CC {ECO:0000269|PubMed:1672038}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. {ECO:0000305}.
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DR EMBL; U53669; AAC47265.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD68838.1; -; Genomic_DNA.
DR EMBL; X58982; CAA41731.1; -; Genomic_DNA.
DR PIR; T29859; T29859.
DR RefSeq; NP_510712.2; NM_078311.5.
DR PDB; 2K2B; NMR; -; A=1-103.
DR PDB; 5TTT; NMR; -; A=1-103.
DR PDBsum; 2K2B; -.
DR PDBsum; 5TTT; -.
DR AlphaFoldDB; P24612; -.
DR BMRB; P24612; -.
DR SMR; P24612; -.
DR BioGRID; 46611; 8.
DR STRING; 6239.T01C8.7.1; -.
DR TCDB; 1.A.6.2.2; the epithelial na(+) channel (enac) family.
DR PaxDb; P24612; -.
DR EnsemblMetazoa; T01C8.7.1; T01C8.7.1; WBGene00003168.
DR GeneID; 181728; -.
DR KEGG; cel:CELE_T01C8.7; -.
DR UCSC; T01C8.7; c. elegans.
DR CTD; 181728; -.
DR WormBase; T01C8.7; CE39109; WBGene00003168; mec-4.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00970000196327; -.
DR HOGENOM; CLU_017673_0_0_1; -.
DR InParanoid; P24612; -.
DR OMA; KYNRNEK; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; P24612; -.
DR EvolutionaryTrace; P24612; -.
DR PRO; PR:P24612; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003168; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0032589; C:neuron projection membrane; IDA:WormBase.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:WormBase.
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:0061096; P:negative regulation of turning behavior involved in mating; 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 GO; GO:0035725; P:sodium ion transmembrane transport; IDA:WormBase.
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 1: Evidence at protein level;
KW 3D-structure; Cell projection; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Neurodegeneration; Potassium; Potassium transport;
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_0000181287"
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 184..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
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 MUTAGEN 230
FT /note="G->E: In e1339; abnormal repetitive turning behavior
FT during male mating."
FT /evidence="ECO:0000269|PubMed:17611271"
FT MUTAGEN 713
FT /note="A->G,S,C: No degeneration."
FT /evidence="ECO:0000269|PubMed:1672038"
FT MUTAGEN 713
FT /note="A->R,D,F,L,P,T,V: Degeneration."
FT /evidence="ECO:0000269|PubMed:1672038"
FT HELIX 2..8
FT /evidence="ECO:0007829|PDB:2K2B"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:2K2B"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:2K2B"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:2K2B"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5TTT"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2K2B"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2K2B"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2K2B"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:2K2B"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2K2B"
SQ SEQUENCE 768 AA; 87194 MW; 8899D0FCCB7F62C6 CRC64;
MSWMQNLKNY QHLRDPSEYM SQVYGDPLAY LQETTKFVTE REYYEDFGYG ECFNSTESEV
QCELITGEFD PKLLPYDKRL AWHFKEFCYK TSAHGIPMIG EAPNVYYRAV WVVLFLGCMI
MLYLNAQSVL DKYNRNEKIV DIQLKFDTAP FPAITLCNLN PYKASLATSV DLVKRTLSAF
DGAMGKAGGN KDHEEEREVV TEPPTTPAPT TKPARRRGKR DLSGAFFEPG FARCLCGSQG
SSEQEDKDEE KEEELLETTT KKVFNINDAD EEWDGMEEYD NEHYENYDVE ATTGMNMMEE
CQSERTKFDE PTGFDDRCIC AFDRSTHDAW PCFLNGTWET TECDTCNEHA FCTKDNKTAK
GHRSPCICAP SRFCVAYNGK TPPIEIWTYL QGGTPTEDPN FLEAMGFQGM TDEVAIVTKA
KENIMFAMAT LSMQDRERLS TTKRELVHKC SFNGKACDIE ADFLTHIDPA FGSCFTFNHN
RTVNLTSIRA GPMYGLRMLV YVNASDYMPT TEATGVRLTI HDKEDFPFPD TFGYSAPTGY
VSSFGLRLRK MSRLPAPYGD CVPDGKTSDY IYSNYEYSVE GCYRSCFQQL VLKECRCGDP
RFPVPENARH CDAADPIARK CLDARMNDLG GLHGSFRCRC QQPCRQSIYS VTYSPAKWPS
LSLQIQLGSC NGTAVECNKH YKENGAMVEV FYEQLNFEML TESEAYGFVN LLADFGGQLG
LWCGISFLTC CEFVFLFLET AYMSAEHNYS LYKKKKAEKA KKIASGSF
