MEC10_CAEEL
ID MEC10_CAEEL Reviewed; 724 AA.
AC P34886; P37087;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Degenerin mec-10;
DE AltName: Full=Mechanosensory abnormality protein 10;
GN Name=mec-10 {ECO:0000312|WormBase:F16F9.5};
GN ORFNames=F16F9.5 {ECO:0000312|WormBase:F16F9.5};
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, SUBUNIT, AND MUTAGENESIS OF SER-105
RP AND ALA-673.
RC STRAIN=Bristol N2;
RX PubMed=7509039; DOI=10.1038/367467a0;
RA Huang M., Chalfie M.;
RT "Gene interactions affecting mechanosensory transduction in Caenorhabditis
RT elegans.";
RL Nature 367:467-470(1994).
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, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11875573; DOI=10.1038/4151039a;
RA Goodman M.B., Ernstrom G.G., Chelur D.S., O'Hagan R., Yao C.A., Chalfie M.;
RT "MEC-2 regulates C. elegans DEG/ENaC channels needed for
RT mechanosensation.";
RL Nature 415:1039-1042(2002).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE DEGENERIN CHANNEL COMPLEX, AND INTERACTION
RP WITH MEC-4 AND MEC-6.
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 ALA-673.
RX PubMed=17261841; DOI=10.1085/jgp.200609672;
RA Brown A.L., Fernandez-Illescas S.M., Liao Z., Goodman M.B.;
RT "Gain-of-function mutations in the MEC-4 DEG/ENaC sensory
RT mechanotransduction channel alter gating and drug blockade.";
RL J. Gen. Physiol. 129:161-173(2007).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF SER-105.
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:11875573, PubMed:17261841, PubMed:7509039,
CC PubMed:12478294). Negatively regulates the turning step of male mating
CC behavior (PubMed:17611271). {ECO:0000269|PubMed:11875573,
CC ECO:0000269|PubMed:12478294, ECO:0000269|PubMed:17261841,
CC ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:7509039}.
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:7509039,
CC PubMed:11875573, PubMed:12478294). Interacts with mec-4 and mec-6
CC (PubMed:12478294). {ECO:0000269|PubMed:11875573,
CC ECO:0000269|PubMed:12478294, ECO:0000269|PubMed:7509039}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11875573};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11875573}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) 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; L25312; AAA17404.1; -; mRNA.
DR EMBL; BX284606; CCD69038.1; -; Genomic_DNA.
DR PIR; T25700; T25700.
DR RefSeq; NP_509438.1; NM_077037.4.
DR AlphaFoldDB; P34886; -.
DR SMR; P34886; -.
DR BioGRID; 46022; 3.
DR STRING; 6239.F16F9.5; -.
DR TCDB; 1.A.6.2.2; the epithelial na(+) channel (enac) family.
DR PaxDb; P34886; -.
DR EnsemblMetazoa; F16F9.5.1; F16F9.5.1; WBGene00003174.
DR GeneID; 181101; -.
DR KEGG; cel:CELE_F16F9.5; -.
DR UCSC; F16F9.5; c. elegans.
DR CTD; 181101; -.
DR WormBase; F16F9.5; CE09444; WBGene00003174; mec-10.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00970000196327; -.
DR HOGENOM; CLU_017673_0_0_1; -.
DR InParanoid; P34886; -.
DR OMA; MSQAKHN; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; P34886; -.
DR PRO; PR:P34886; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003174; Expressed in larva and 1 other tissue.
DR GO; GO:0044298; C:cell body membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; 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 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; 1.
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 Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Sensory transduction;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..724
FT /note="Degenerin mec-10"
FT /id="PRO_0000181288"
FT TOPO_DOM 1..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 105
FT /note="S->F: In e1515; loss of mechanosensory transduction
FT between touch cells. Abnormal repetitive turning behavior
FT during male mating."
FT /evidence="ECO:0000269|PubMed:17611271,
FT ECO:0000269|PubMed:7509039"
FT MUTAGEN 673
FT /note="A->C: Slight increase in channel current."
FT /evidence="ECO:0000269|PubMed:17261841,
FT ECO:0000269|PubMed:7509039"
FT MUTAGEN 673
FT /note="A->D: Increased channel current."
FT /evidence="ECO:0000269|PubMed:17261841,
FT ECO:0000269|PubMed:7509039"
FT MUTAGEN 673
FT /note="A->V: Causes degeneration of the PLM mechanosensory
FT neuron and increases channel current."
FT /evidence="ECO:0000269|PubMed:17261841,
FT ECO:0000269|PubMed:7509039"
SQ SEQUENCE 724 AA; 82382 MW; 196819763C2CBA57 CRC64;
MNRNPRMSKF QPNPRSRSRF QDETDLRSLR SFKTDFSNYL ASDTNFLNVA EIMTSYAYGE
SNNAHEKEIQ CDLLTENGGI EIDPTRLSYR ERIRWHLQQF CYKTSSHGIP MLGQAPNSLY
RAAWVFLLLI CAIQFINQAV AVIQKYQKMD KITDIQLKFD TAPFPAITLC NLNPYKDSVI
RSHDSISKIL GVFKSVMKKA GDSSSEALEE EEETEYDMNG ITIQAKRKKR GAGEKGTFEP
ANSACECDEE DGSNECEERS TEKPSGDNDM CICAFDRQTN DAWPCHRKEQ WTNTTCQTCD
EHYLCSKKAK KGTKRSELKK EPCICESKGL FCIKHEHAAM VLNLWEYFGD SEDFSEISTE
EREALGFGNM TDEVAIVTKA KENIIFAMSA LSEEQRILMS QAKHNLIHKC SFNGKPCDID
QDFELVADPT FGNCFVFNHD REIFKSSVRA GPQYGLRVML FVNASDYLPT SEAVGIRLTI
HDKDDFPFPD TFGYSAPTGY ISSFGMRMKK MSRLPAPYGD CVEDGATSNY IYKGYAYSTE
GCYRTCFQEL IIDRCGCSDP RFPSIGGVQP CQVFNKNHRE CLEKHTHQIG EIHGSFKCRC
QQPCNQTIYT TSYSEAIWPS QALNISLGQC EKEAEECNEE YKENAAMLEV FYEALNFEVL
SESEAYGIVK MMADFGGHLG LWSGVSVMTC CEFVCLAFEL IYMAIAHHIN QQRIRRRENA
ANEY