PBO5_CAEEL
ID PBO5_CAEEL Reviewed; 509 AA.
AC G5ECT0; G5ECR4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Proton-gated ion channel subunit pbo-5 {ECO:0000303|PubMed:18191228};
DE AltName: Full=PBoc defective protein pbo-5 {ECO:0000303|PubMed:18191228};
DE Flags: Precursor;
GN Name=pbo-5 {ECO:0000312|EMBL:CAH19091.1, ECO:0000312|WormBase:Y44A6E.1b};
GN Synonyms=lgc-2 {ECO:0000312|EMBL:CAH19091.1}; ORFNames=Y44A6E.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] (ISOFORM A), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PRO-186; HIS-189; THR-309; LEU-321; PRO-330 AND MET-347.
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:CAH19091.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAH19091.1};
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).
RN [3]
RP FUNCTION.
RX PubMed=25849533; DOI=10.1371/journal.pone.0124515;
RA Sheng M., Hosseinzadeh A., Muralidharan S.V., Gaur R., Selstam E., Tuck S.;
RT "Aberrant fat metabolism in Caenorhabditis elegans mutants with defects in
RT the defecation motor program.";
RL PLoS ONE 10:E0124515-E0124515(2015).
CC -!- FUNCTION: Forms a proton-gated ion channel with pbo-6 that is activated
CC by acidification of the posterior coelomic space, leading to posterior
CC body wall muscle contraction (pBoc) during the defecation cycle
CC (PubMed:18191228). Probably by regulating the defecation motor program,
CC required for fatty acid uptake by intestinal cells (PubMed:25849533).
CC Does not bind neurotransmitters such as acetylcholine, gamma-
CC aminobutyric acid, glycine, serotonin, glutamate or choline
CC (PubMed:18191228). {ECO:0000269|PubMed:18191228,
CC ECO:0000269|PubMed:25849533}.
CC -!- SUBUNIT: The functional channel is a heterooligomer of pbo-5 and pbo-6.
CC May self-associate to form homooligomers with negligible ion channel
CC activity. {ECO:0000269|PubMed:18191228}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18191228}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:18191228}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=G5ECT0-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:18191228, ECO:0000269|PubMed:9851916};
CC IsoId=G5ECT0-2; Sequence=VSP_053336;
CC -!- TISSUE SPECIFICITY: Expressed in the posterior body muscles. Also
CC detected in the RIFL, RIFR and RIS head neurons.
CC {ECO:0000269|PubMed:18191228}.
CC -!- DISRUPTION PHENOTYPE: Loss of posterior body wall muscle contractions
CC (pBoc). {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; AL033511; CAH19091.1; -; Genomic_DNA.
DR EMBL; AL033515; CAH19091.1; JOINED; Genomic_DNA.
DR EMBL; Z81512; CAH19091.1; JOINED; Genomic_DNA.
DR EMBL; AL033511; CAA22072.2; -; Genomic_DNA.
DR EMBL; AL033515; CAA22072.2; JOINED; Genomic_DNA.
DR EMBL; Z81512; CAA22072.2; JOINED; Genomic_DNA.
DR RefSeq; NP_001024239.1; NM_001029068.3. [G5ECT0-2]
DR RefSeq; NP_001024240.1; NM_001029069.4. [G5ECT0-1]
DR AlphaFoldDB; G5ECT0; -.
DR SMR; G5ECT0; -.
DR STRING; 6239.Y44A6E.1b; -.
DR EPD; G5ECT0; -.
DR PaxDb; G5ECT0; -.
DR PeptideAtlas; G5ECT0; -.
DR EnsemblMetazoa; Y44A6E.1a.1; Y44A6E.1a.1; WBGene00012857. [G5ECT0-2]
DR EnsemblMetazoa; Y44A6E.1b.1; Y44A6E.1b.1; WBGene00012857. [G5ECT0-1]
DR GeneID; 189903; -.
DR KEGG; cel:CELE_Y44A6E.1; -.
DR CTD; 189903; -.
DR WormBase; Y44A6E.1a; CE32021; WBGene00012857; pbo-5. [G5ECT0-2]
DR WormBase; Y44A6E.1b; CE37284; WBGene00012857; pbo-5. [G5ECT0-1]
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000173136; -.
DR HOGENOM; CLU_518985_0_0_1; -.
DR InParanoid; G5ECT0; -.
DR OMA; IMCAISV; -.
DR OrthoDB; 1290238at2759; -.
DR PhylomeDB; G5ECT0; -.
DR Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR PRO; PR:G5ECT0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012857; Expressed in larva and 3 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:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0010877; P:lipid transport involved in lipid storage; IMP:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:1904731; P:positive regulation of intestinal lipid absorption; IMP:UniProtKB.
DR GO; GO:0045989; P:positive regulation of striated muscle contraction; IMP:WormBase.
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 Alternative splicing; Disulfide bond; Ion channel; Ion transport; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..509
FT /note="Proton-gated ion channel subunit pbo-5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424148"
FT TOPO_DOM 22..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 193..207
FT /evidence="ECO:0000250|UniProtKB:P02712"
FT VAR_SEQ 155..159
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:18191228"
FT /id="VSP_053336"
FT MUTAGEN 186
FT /note="P->L: In sa242; defective in posterior body wall
FT contraction (pBoc)."
FT /evidence="ECO:0000269|PubMed:18191228"
FT MUTAGEN 189
FT /note="H->Q: In ox9; defective in posterior body wall
FT contraction (pBoc)."
FT /evidence="ECO:0000269|PubMed:18191228"
FT MUTAGEN 309
FT /note="T->I: In ox38; defective in posterior body wall
FT contraction (pBoc)."
FT /evidence="ECO:0000269|PubMed:18191228"
FT MUTAGEN 321
FT /note="L->F: In ox7dm; defective in posterior body wall
FT contraction (pBoc)."
FT /evidence="ECO:0000269|PubMed:18191228"
FT MUTAGEN 330
FT /note="P->L: In ox34; defective in posterior body wall
FT contraction (pBoc)."
FT /evidence="ECO:0000269|PubMed:18191228"
FT MUTAGEN 347
FT /note="M->T: In sa297; defective in posterior body wall
FT contraction (pBoc)."
FT /evidence="ECO:0000269|PubMed:18191228"
SQ SEQUENCE 509 AA; 58441 MW; 3D7A3C3960B96D10 CRC64;
MTRLSILQHL LTFLILSKIN ATSTTESYFD SSEEAPNVLL NHLNNESEGE ELTQINDTQP
AFVPGSSKRL TEYLLSRHNL NAPPDGLLYV EYELELVHIL GIDELKQTMT VLIYVDEHWV
DPSLTWDPAL FGGITKTWIP LDKIWVPDII VFNMVKSNRL AHEDLLSAVR APARIHYNGT
IVASHPAVHT VSCEINIRHF PLDDQRCAIE IASWAYGQEK IRLHAHTDHS LEHYKRNEEW
HLLNLNVSEE KYEHEGVEVS EVKFEISLKR RPLFYMVTLT FPSYIMCAIS VVGLFARFST
TGEREERFTL GVTAILTMAV LSLVVSEKVP HSSTHVPLLV AYFLFNMVIV SIAAMTTGIV
MKVHRLGRYG DEPSDFWMRC FLLKPVFRTS NRRKYRMNPE EPTQVILVSE AKNGEVLTKK
STELNGTVVK EIMLSSRLEA LEEYIRKMVN RCETIKWELD EIDAAENIEL VRRRSTNGYV
RISERLDILF MFLFLSTVTI PVAVLFYLT
