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ACH1_CAEBR
ID   ACH1_CAEBR              Reviewed;         499 AA.
AC   A8WQK3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Acetylcholine receptor subunit alpha-type acr-16 {ECO:0000250|UniProtKB:P48180};
DE   Flags: Precursor;
GN   Name=acr-16 {ECO:0000312|EMBL:CAP22761.2}; ORFNames=CBG01491;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP22761.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP22761.2};
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: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane. A
CC       subunit of the levamisole-insensitive nicotinic receptor (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:P48180}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P48180}. Cell membrane
CC       {ECO:0000250|UniProtKB:P48180}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P48180}. Note=The cam-1 protein is required for
CC       correct localization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000305}.
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DR   EMBL; HE601420; CAP22761.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8WQK3; -.
DR   SMR; A8WQK3; -.
DR   STRING; 6238.CBG01491; -.
DR   EnsemblMetazoa; CBG01491.1; CBG01491.1; WBGene00024720.
DR   WormBase; CBG01491; CBP35005; WBGene00024720; Cbr-acr-16.
DR   eggNOG; KOG3646; Eukaryota.
DR   HOGENOM; CLU_018074_0_3_1; -.
DR   InParanoid; A8WQK3; -.
DR   OMA; AWLQMSW; -.
DR   OrthoDB; 845098at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:EnsemblMetazoa.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.20.58.390; -; 2.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..499
FT                   /note="Acetylcholine receptor subunit alpha-type acr-16"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000365627"
FT   TOPO_DOM        20..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..473
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        474..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        495..499
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        147..161
FT                   /evidence="ECO:0000250|UniProtKB:P02708"
FT   DISULFID        211..212
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250|UniProtKB:P02708"
SQ   SEQUENCE   499 AA;  57264 MW;  C06C515D8B1DDED6 CRC64;
     MSSVCALLLS CALFLVAHGS LQERRLYEDL MRNYNNLERP VANHSEPVTV HLKVALQQII
     DVDEKNQVVY VNAWLDYTWK DYNLVWDQAE YGNITDVRFP AGKIWKPDVL LYNSVDTNFD
     STYQTNMIVY SSGLVHWVPP GIFKISCKID IQWFPFDEQK CFFKFGSWTY DGYKLDLQPA
     TGGFDISEYL PNGEWALPLT TVERNEKFYD CCPEPYPDVH FYLHMRRRTL YYGFNLIMPC
     ILTTLMTLLG FTLPPDAGEK ITLQITVLLS ICFFLSIVSE MSPPTSEAVP LLGIFFTCCM
     IVVTASTVFT VYVLNLHYRT PETHDMGPWT RNLLLYWIPW ILRMKRPGHN LTYASLPSLF
     ASKPNRHSES LIRNIKDNEH SLSRANSFDA DCRLNQYIMT QSVSNGLTSM GSIPSTMISS
     TNGALTDVSQ QATLLILHRI YHELKIVTKR MIEGDKEEQA SNNWKFAAMV VDRLCLYVFT
     IFIIASTIGI FWSAPYLVA
 
 
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