PBO6_CAEEL
ID PBO6_CAEEL Reviewed; 422 AA.
AC Q19351; G4S6G6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 5.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Proton-gated ion channel subunit pbo-6 {ECO:0000303|PubMed:18191228};
DE AltName: Full=PBoc defective protein pbo-6 {ECO:0000303|PubMed:18191228};
DE Flags: Precursor;
GN Name=pbo-6 {ECO:0000312|EMBL:CCD66918.1, ECO:0000312|WormBase:F11C7.1};
GN Synonyms=lgc-3 {ECO:0000312|EMBL:CCD66918.1, ECO:0000312|WormBase:F11C7.1};
GN ORFNames=F11C7.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:18191228};
RX PubMed=18191228; DOI=10.1016/j.cell.2007.10.058;
RA Beg A.A., Ernstrom G.G., Nix P., Davis M.W., Jorgensen E.M.;
RT "Protons act as a transmitter for muscle contraction in C. elegans.";
RL Cell 132:149-160(2008).
RN [2] {ECO:0000312|EMBL:CCD66918.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD66918.1};
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).
CC -!- FUNCTION: Forms a proton-gated ion channel with pbo-5 that is activated
CC by acidification of the posterior coelomic space, leading to posterior
CC body wall muscle contraction (pBoc) during the defecation cycle. Not
CC necessary for stimulation of posterior body contraction (pBoc). Does
CC not bind neurotransmitters such as acetylcholine, gamma-aminobutyric
CC acid, glycine, serotonin, glutamate or choline.
CC {ECO:0000269|PubMed:18191228}.
CC -!- SUBUNIT: The functional channel is a hetero-oligomer of pbo-5 and pbo-
CC 6. {ECO:0000269|PubMed:18191228}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18191228}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:18191228}.
CC -!- TISSUE SPECIFICITY: Expressed in the posterior body muscles.
CC {ECO:0000269|PubMed:18191228}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mutants exhibit normal
CC posterior body contractions. {ECO:0000269|PubMed:18191228}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000255}.
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DR EMBL; FO080804; CCD66918.1; -; Genomic_DNA.
DR EMBL; FO080802; CCD66918.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001294833.1; NM_001307904.1.
DR AlphaFoldDB; Q19351; -.
DR SMR; Q19351; -.
DR STRING; 6239.F11C7.1; -.
DR PaxDb; Q19351; -.
DR EnsemblMetazoa; F11C7.1.1; F11C7.1.1; WBGene00017375.
DR GeneID; 24104421; -.
DR KEGG; cel:CELE_F11C7.1; -.
DR UCSC; F11C7.1; c. elegans.
DR CTD; 24104421; -.
DR WormBase; F11C7.1; CE42343; WBGene00017375; pbo-6.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_2_1_1; -.
DR InParanoid; Q19351; -.
DR OMA; ARKEYEH; -.
DR OrthoDB; 1666203at2759; -.
DR PhylomeDB; Q19351; -.
DR Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR PRO; PR:Q19351; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017375; Expressed in larva and 2 other tissues.
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:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IDA:WormBase.
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; -; 1.
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 PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
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 Disulfide bond; Ion channel; Ion transport; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..422
FT /note="Proton-gated ion channel subunit pbo-6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424149"
FT TOPO_DOM 21..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000250|UniProtKB:P02712"
SQ SEQUENCE 422 AA; 48982 MW; BA042F0E33FE5700 CRC64;
MQCSFLTIFI FITTVTVGVA EFSEQYQGSS SRLTRHLLEK HNKCSPPDGR VDISHNIELV
HIIGINELNQ NMQVLVYIVQ QWTDASLSWK VEEFRGIKHT WLPEHSIWIP DIIVFNTLEH
KMLLEAVRSP IKVSYTGEVT YAYPAIYTVL CQIGIATFPF DDQVCKIRFA SWAYDEDKIL
LNASHKPLLK NYSPNEEWAL QDVDMARKEY EHEETVVSEI IYYIKVARKP FYYLISLVVP
SYIICVLSIA GLFARFSTKH ERQERFTLGV TAILSMAVLS LVVTEKVPHS SENVPLLIVY
MHFIIVMVTI ATILTSTVMR VHAKGFRTHF LSPPNWIRKV LLIARKHANF FQQHGKVYMD
IHTTAEQWGE VSRRMDYLLA SVFIIIISTP TLYLFYMCFQ MDHATAERVL LENAKRRDQL
YY
