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ACC2_CAEEL
ID   ACC2_CAEEL              Reviewed;         445 AA.
AC   Q18812;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Acetylcholine-gated chloride channel subunit acc-2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=acc-2 {ECO:0000312|WormBase:C53D6.3};
GN   ORFNames=C53D6.3 {ECO:0000312|WormBase:C53D6.3};
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, SUBUNIT, AND SUBCELLULAR LOCATION.
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   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: Acetylcholine-gated chloride channel subunit. Currents in
CC       channels are triggered in response to acetylcholine. Channel properties
CC       may be modulated by the formation of homomeric and heteromeric
CC       channels. {ECO:0000269|PubMed:15579462}.
CC   -!- SUBUNIT: Homopentamer (in vitro). May interact with either acc-3 or
CC       acc-4; the interactions do not result in significant heteropentameric
CC       ion channel activity. {ECO:0000269|PubMed:15579462}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15579462};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in RIA, RIG, PHA and AIZ glutamatergic
CC       neurons, URX and RIH cholinergic neurons, and in male-specific MCM
CC       neurons. {ECO:0000269|PubMed:26705699}.
CC   -!- DISRUPTION PHENOTYPE: Grossly normal movement.
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; BX284604; CAA94228.1; -; Genomic_DNA.
DR   PIR; T20190; T20190.
DR   RefSeq; NP_501567.1; NM_069166.1.
DR   AlphaFoldDB; Q18812; -.
DR   SMR; Q18812; -.
DR   STRING; 6239.C53D6.3; -.
DR   PaxDb; Q18812; -.
DR   EnsemblMetazoa; C53D6.3.1; C53D6.3.1; WBGene00008280.
DR   GeneID; 183758; -.
DR   KEGG; cel:CELE_C53D6.3; -.
DR   UCSC; C53D6.3; c. elegans.
DR   CTD; 183758; -.
DR   WormBase; C53D6.3; CE05488; WBGene00008280; acc-2.
DR   eggNOG; KOG3644; Eukaryota.
DR   HOGENOM; CLU_010920_1_3_1; -.
DR   InParanoid; Q18812; -.
DR   OMA; IYITETW; -.
DR   OrthoDB; 534697at2759; -.
DR   PhylomeDB; Q18812; -.
DR   Reactome; R-CEL-977443; GABA receptor activation.
DR   PRO; PR:Q18812; -.
DR   Proteomes; UP000001940; Chromosome IV.
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: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   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
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.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..445
FT                   /note="Acetylcholine-gated chloride channel subunit acc-2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5004186831"
FT   TOPO_DOM        27..258
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..445
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        59
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        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        177..191
FT                   /evidence="ECO:0000250|UniProtKB:P02712"
SQ   SEQUENCE   445 AA;  51686 MW;  3F60AE853A50F4FC CRC64;
     MIFTLLSTLP VLIITTELDY SELVHSAELV SSSSYIHHKT NKKPDNCTRD TDIIDRLLNG
     TGYNKFRIPQ EEGMTVVVEI WIQAITSIDE LTNDFDMDIY ITETWLDPAL NFQTMTPCKG
     NLSLNHQVLD RLWTPNSCFI NSKVAQIHNS PFRSVFLMLF PNGTVMVNYR VRVKGPCSLD
     LSNFPLDLQK CSLIYESFNY NRQEVEMRWS DAEHPVFNLS KIMLPDFDLF EIQTERRQEP
     YPAGMWDELH VTIIFERRFI WYFMQAYLPT YLTIFISWIS FSLGSRAIPA RTMLGVNSLL
     AIVFSFGNIM RNLPRVSYIK GIDVWMLVSM TFIFCSLLEL AIVGFMVRDE TVAKKKQQKK
     ISGNISREES PHGIISERRF MFPPGCSESS KSLSSCTSGW TPERIDSISS VMFPFSFFVF
     NIIYWFYYIH RKEIIKQNLI NRVDG
 
 
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