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TMC1_CAEEL
ID   TMC1_CAEEL              Reviewed;        1285 AA.
AC   D3KZG3; G4S885;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Transmembrane channel-like protein 1;
GN   Name=tmc-1; ORFNames=T13G4.3;
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 [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   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23364694; DOI=10.1038/nature11845;
RA   Chatzigeorgiou M., Bang S., Hwang S.W., Schafer W.R.;
RT   "tmc-1 encodes a sodium-sensitive channel required for salt chemosensation
RT   in C. elegans.";
RL   Nature 494:95-99(2013).
CC   -!- FUNCTION: Sodium-sensor ion channel that acts specifically in salt
CC       taste chemosensation. Required for salt-evoked neuronal activity and
CC       behavioral avoidance of high concentrations of NaCl.
CC       {ECO:0000269|PubMed:23364694}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23364694};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:23364694}.
CC   -!- TISSUE SPECIFICITY: Expressed in the ASH polymodal avoidance neurons.
CC       Also expressed in other sensory neurons, including the ADF, ASE, ADL,
CC       AQR, PQR, URX and PHA cells. {ECO:0000269|PubMed:23364694}.
CC   -!- DISRUPTION PHENOTYPE: No apparent defect in nose touch avoidance but
CC       mutants show strong defects in the avoidance of NaCl concentrations
CC       above 100 mM. Responses to other soluble repellents as well as to
CC       hyperosmolarity are indistinguishable from wild-type animals.
CC       {ECO:0000269|PubMed:23364694}.
CC   -!- SIMILARITY: Belongs to the TMC family. {ECO:0000305}.
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DR   EMBL; FO080889; CCD67541.1; -; Genomic_DNA.
DR   EMBL; FO080360; CCD67541.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_508221.3; NM_075820.5.
DR   AlphaFoldDB; D3KZG3; -.
DR   STRING; 6239.T13G4.3; -.
DR   TCDB; 1.A.17.4.7; the calcium-dependent chloride channel (ca-clc) family.
DR   EPD; D3KZG3; -.
DR   PaxDb; D3KZG3; -.
DR   EnsemblMetazoa; T13G4.3.1; T13G4.3.1; WBGene00020490.
DR   EnsemblMetazoa; T13G4.3.2; T13G4.3.2; WBGene00020490.
DR   GeneID; 188483; -.
DR   KEGG; cel:CELE_T13G4.3; -.
DR   CTD; 188483; -.
DR   WormBase; T13G4.3; CE37147; WBGene00020490; tmc-1.
DR   eggNOG; ENOG502QQGX; Eukaryota.
DR   GeneTree; ENSGT01050000244942; -.
DR   HOGENOM; CLU_278527_0_0_1; -.
DR   InParanoid; D3KZG3; -.
DR   OMA; RYLYQES; -.
DR   OrthoDB; 124678at2759; -.
DR   PhylomeDB; D3KZG3; -.
DR   PRO; PR:D3KZG3; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00020490; Expressed in larva and 3 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR   GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR   GO; GO:0005216; F:ion channel activity; IDA:UniProtKB.
DR   GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR   GO; GO:0005272; F:sodium channel activity; IMP:CACAO.
DR   GO; GO:0050906; P:detection of stimulus involved in sensory perception; IMP:UniProtKB.
DR   GO; GO:0034220; P:ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0007606; P:sensory perception of chemical stimulus; IMP:UniProtKB.
DR   InterPro; IPR038900; TMC.
DR   InterPro; IPR012496; TMC_dom.
DR   PANTHER; PTHR23302; PTHR23302; 1.
DR   Pfam; PF07810; TMC; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Ion channel; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1285
FT                   /note="Transmembrane channel-like protein 1"
FT                   /id="PRO_0000421989"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        676..696
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        739..759
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        787..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        852..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          940..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1114..1133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1169..1186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1285 AA;  147129 MW;  BC5A3332464D6D36 CRC64;
     MQEAARRASL RKEHTPTNEK FGDLSKQDSL GERASSKLTL DDELYDILYA FGETDAFINK
     GDKQRETDED GNPLTRQALL ERIRQKKEVI GKLRCQAWSM TRKRRTLKLA QKYLEQHESK
     VSRSHLYMEE MRKRARLMKR SFSNFKTYLI PWESKIKRIE SHFGSVVSSY FTFLRWIVFV
     NIMITLIALV FVVLPETLAD SVANEGRFNR TKTRKQIPAN ERVHADELAV VWHYDGYLRY
     SPLFYGYYSD DPFLGNKIKY ALPLAYFMVT LTIFAYSFFA ILRKMAANAR MSKLSGSKAE
     QYIFNWKLFT GWDYTIGNSE TASNTVMAVV IKLRESIADI KKDAHGKFRL LQFSLRVFAN
     IIICAMLGFS IYCIIFAVQK SQVQDDGNLF TKNQVPSVVS TITHVFPMIF DLIGKMENYH
     PRTALRAHLG RVLILYTVNY ITLIFALFEK MTALRDRVNS TSTSSSHRTK RQQGGWNPNM
     QRPPPYASRA EVRQMSDFLA ANTRRFQTVS QRTTRSVTTP FTVAPQFGPF NVNNPNAVFH
     NGTHSTSFES QILGPKALPI FTPPPRKYPG FTPGNVGQQF GGPDFPRNQV YTKSTPLPRV
     RTKPPWVYTT THPPLVQNRA MTTTMSKSAK KGNSKNLDDD ILLSNETIQM SEAALRRNHD
     GHNNDICWET IIGQEIVKLV TMDLIFTILS ILVIDLFRGL WIKYCSSWWC WDIETTFPEY
     GEFKVAENVL HIINNQGMIW LGLFFAPLLP AINNIKLIIL MYIRGWAVMT CNVPAREIFR
     ASRSSNFYLG ILLIWLLLCT LPVGFVIASM SPSRSCGPFA RYQHFYTVVT REIEKRVDQT
     VLSYIRHIAS PGVVIPIILF LILIIYFLFS LVRGLREANT DLQAQLVHER TEEKKKIFEL
     AGGKKNKFEK DRDKKRSNDY IPLIEQRRRE PWRQYHEMEA DHALASDSSE ESDINEDEDD
     ERQPLTAYPL RAIETPPETL QVTAFHPSLG SLIENREMED EESASGDQLP MIHKSVSFQG
     PSHMQMRQSI STESCSQISR SAIQVATPEE IRALLRPYLE AKYGIPYQHG IKSFPIDVHT
     PPNNTPSRRS SKYNSFVSLY EHTRDDHKNF VASTIKETDE DPGKSDKKQT SSKDVAPDFM
     PWPSADEARA LREKMKSKTP LMLTKTTVEE KPKGGKSSES EFRPPVPIHR KYNIQTTEEE
     NEEEETDSAP ESSKKRFRIS VSPTKTIAPA SASRAQHKIV SQASSSSSIP HGRQPDPNKK
     ASLVLPPLRA PRVQFDEDDS PRQID
 
 
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