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MEC10_CAEBR
ID   MEC10_CAEBR             Reviewed;         724 AA.
AC   Q60NC0; A8Y2V5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Degenerin mec-10;
DE   AltName: Full=Mechanosensory abnormality protein 10;
GN   Name=mec-10 {ECO:0000250|UniProtKB:P34886}; ORFNames=CBG22775;
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 [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: Amiloride-sensitive sodium channel subunit required for
CC       mechanosensory transduction (touch sensitivity). Negatively regulates
CC       the turning step of male mating behavior.
CC       {ECO:0000250|UniProtKB:P34886}.
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:P34886}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P34886};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P34886}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. {ECO:0000305}.
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DR   EMBL; HE601156; CAP39289.1; -; Genomic_DNA.
DR   RefSeq; XP_002645519.1; XM_002645473.1.
DR   AlphaFoldDB; Q60NC0; -.
DR   STRING; 6238.CBG22775; -.
DR   EnsemblMetazoa; CBG22775.1; CBG22775.1; WBGene00041260.
DR   GeneID; 8587518; -.
DR   KEGG; cbr:CBG_22775; -.
DR   CTD; 8587518; -.
DR   WormBase; CBG22775; CBP24993; WBGene00041260; Cbr-mec-10.
DR   eggNOG; KOG4294; Eukaryota.
DR   HOGENOM; CLU_017673_0_0_1; -.
DR   InParanoid; Q60NC0; -.
DR   OMA; MSQAKHN; -.
DR   OrthoDB; 686369at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0044298; C:cell body membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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; 1.
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   Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Sensory transduction; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..724
FT                   /note="Degenerin mec-10"
FT                   /id="PRO_0000294930"
FT   TOPO_DOM        1..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..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   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
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"
SQ   SEQUENCE   724 AA;  82166 MW;  19B7F9142076C457 CRC64;
     MNRGPPNPRM FKFQPNPKVK NRFQDEADLR SLRSFKTDFS NYLASDTNFL NVAEIMTSYA
     YGESNNANEK EIQCDLLTEN GGIEIDPTRL SYRERIRWHL QQFCYKTSSH GIPMLGQAPN
     SLYRAVWVFL LLICAIQFIN QAVAVIQKYQ KMDKITDIQL KFDTAPFPAI TLCNLNPYKD
     SVIRSHDSIS KILGVFKSVM KKAGDSSAEA SDDGVEYDMD GITIQAKRRK RGAGEKGTFE
     PANSACECDE EDGSNECEEK STEKPSSDND MCICAFDRQT NDAWPCHRRE QWTNTTCQAC
     DEHYLCSKKA KKGTKRSEIK KEPCICESKG LFCIKHEHAA LVLNLWEYFG DTEEFSDIST
     EEREALGFGN MTDEVAIVTK AKENIIFAMS ASEEQRILMS QAKHNLIHKC SFNGKPCDID
     KDFELVADPT FGNCFVFNHD REIFKSSVRA GPQYGLRVML FVNASDYLPT SEAVGIRLTI
     HDKDDFPFPD TFGYSAPTGY ISSFGMRMKK MSRLPAPYGD CVEDGTTSNY IYKGYAYSTE
     GCYRTCFQEL IIDRCGCSDP RFPSIGGVQP CQVFNKNHRE CLEKHTHQIG EIHGSFKCRC
     QQPCNQTIYT TSYSEAIWPS QALNISLGHC EKEAEECNEE YKENAAMLEV FYEALNFEVL
     AESEAYGIVK MMADFGGHLG LWSGVSVMTC CEFVCLVLEL LYMAVTHHIT QERIRRRENA
     ANEF
 
 
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