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ACC4_CAEEL
ID   ACC4_CAEEL              Reviewed;         408 AA.
AC   Q9U358;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Acetylcholine-gated ion channel acc-4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=acc-4 {ECO:0000303|PubMed:15579462, ECO:0000312|WormBase:T27E9.9};
GN   ORFNames=T27E9.9 {ECO:0000312|WormBase:T27E9.9};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX   PubMed=15579462; DOI=10.1074/jbc.m412644200;
RA   Putrenko I., Zakikhani M., Dent J.A.;
RT   "A family of acetylcholine-gated chloride channel subunits in
RT   Caenorhabditis elegans.";
RL   J. Biol. Chem. 280:6392-6398(2005).
RN   [2] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=26705699; DOI=10.7554/elife.12432;
RA   Pereira L., Kratsios P., Serrano-Saiz E., Sheftel H., Mayo A.E., Hall D.H.,
RA   White J.G., LeBoeuf B., Garcia L.R., Alon U., Hobert O.;
RT   "A cellular and regulatory map of the cholinergic nervous system of C.
RT   elegans.";
RL   Elife 4:12432-12477(2015).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27782882; DOI=10.7554/elife.21734;
RA   Takayanagi-Kiya S., Zhou K., Jin Y.;
RT   "Release-dependent feedback inhibition by a presynaptically localized
RT   ligand-gated anion channel.";
RL   Elife 5:21734-21749(2016).
CC   -!- FUNCTION: Probable acetylcholine-gated chloride channel subunit
CC       (PubMed:15579462). Does not have ion channel activity alone as a
CC       homopentamer, but forms a functional heteropentameric ion channel with
CC       acc-1 (PubMed:15579462). May function with lgc-46 to regulate synaptic
CC       transmission and synaptic vesicle release in response to acetylcholine
CC       in cholinergic motor neurons (PubMed:27782882).
CC       {ECO:0000269|PubMed:15579462, ECO:0000269|PubMed:27782882}.
CC   -!- SUBUNIT: Does not form a functional homopentameric ion channel. Forms a
CC       functional heteropentameric ion channel composed of acc-1 and acc-4.
CC       May interact with acc-2; the interaction does not result in significant
CC       heteropentameric ion channel activity. {ECO:0000269|PubMed:15579462}.
CC   -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC       {ECO:0000269|PubMed:27782882}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:27782882}.
CC   -!- TISSUE SPECIFICITY: Expressed in all cholinergic motor neurons except
CC       for ASJ and RIB neurons. Also expressed in AVF neurons.
CC       {ECO:0000269|PubMed:26705699}.
CC   -!- DISRUPTION PHENOTYPE: Grossly normal movement. In addition, in response
CC       to induced acetylcholine release, there is prolonged and slow decay of
CC       excitory postsynaptic currents which results in increased release of
CC       synaptic vesicles during that late phase of synaptic vesicle release in
CC       cholinergic motor neurons. Knockout in an lgc-46 gain of function
CC       mutant background suppresses the slow locomotion defect in the single
CC       lgc-46 gain of function mutant. Knockout together with gain of function
CC       mutations in lgc-46 and acr-2 suppresses the convulsion defects in the
CC       double lgc-46 and acr-2 double gain of function mutant.
CC       {ECO:0000269|PubMed:27782882}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       {ECO:0000305}.
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DR   EMBL; BX284603; CAB04879.2; -; Genomic_DNA.
DR   PIR; E88613; E88613.
DR   PIR; T25376; T25376.
DR   RefSeq; NP_499789.1; NM_067388.4.
DR   AlphaFoldDB; Q9U358; -.
DR   SMR; Q9U358; -.
DR   STRING; 6239.T27E9.9; -.
DR   PaxDb; Q9U358; -.
DR   EnsemblMetazoa; T27E9.9.1; T27E9.9.1; WBGene00012099.
DR   EnsemblMetazoa; T27E9.9.2; T27E9.9.2; WBGene00012099.
DR   GeneID; 176778; -.
DR   UCSC; T27E9.9; c. elegans.
DR   CTD; 176778; -.
DR   WormBase; T27E9.9; CE24020; WBGene00012099; acc-4.
DR   eggNOG; KOG3644; Eukaryota.
DR   HOGENOM; CLU_010920_1_3_1; -.
DR   InParanoid; Q9U358; -.
DR   OMA; FYESFTH; -.
DR   OrthoDB; 625651at2759; -.
DR   PhylomeDB; Q9U358; -.
DR   Reactome; R-CEL-977443; GABA receptor activation.
DR   PRO; PR:Q9U358; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00012099; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0034707; C:chloride channel complex; 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:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
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:1902476; P:chloride transmembrane transport; 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; -; 1.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
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   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Chloride; Chloride channel; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW   Membrane; Reference proteome; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..408
FT                   /note="Acetylcholine-gated ion channel acc-4"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5004333882"
FT   TOPO_DOM        18..262
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..325
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        347..380
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        402..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        178..192
FT                   /evidence="ECO:0000250|UniProtKB:P02712"
SQ   SEQUENCE   408 AA;  46218 MW;  F2D7348DE2319081 CRC64;
     MRLIILVISI LISNAGSLLR SLEDDSNECM FNCPKRARNV SVPHTEKTCM GDDAIIAQIL
     DGYNKLDLPG GGHVVVSIEI WVQEVSKIIE ITSEFELDIY VTERWTDPSL AYSHLNPCKS
     NMSVDGATIL NKIWNPHACF VNSKLANIHE SPFKNIFLQI YSNGSIWHNY RIKLTGPCSS
     TLRTFPIDQQ RCMLFYESFT HNTDQVKMEW ITTVPPITIL KGNITLPDYV LVDFSSSSEL
     RLYPPGIFNE LIATFTFQRL YGFYILQVYV PAYISVFISW VSFTLGAEQI PSRTTVGVNS
     LLALTFQFGA VVNNLPKTSD VKAIDVWILS SMAFIFASLI ELAVVGYLSR DGQHGSIKCR
     CSWLCMNCKD WTALKIDQMS SIVFPVSFLA FNIWYWFIFL GKLLVRTI
 
 
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