CUP4_CAEEL
ID CUP4_CAEEL Reviewed; 433 AA.
AC P34271; Q6IZD3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Acetylcholine receptor-like protein cup-4;
DE AltName: Full=Coelomocyte uptake defective protein 4;
DE Flags: Precursor;
GN Name=cup-4; ORFNames=C02C2.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF VAL-272.
RX PubMed=15936276; DOI=10.1016/j.cub.2005.04.057;
RA Patton A., Knuth S., Schaheen B., Dang H., Greenwald I., Fares H.;
RT "Endocytosis function of a ligand-gated ion channel homolog in
RT Caenorhabditis elegans.";
RL Curr. Biol. 15:1045-1050(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11560892; DOI=10.1093/genetics/159.1.133;
RA Fares H., Greenwald I.;
RT "Genetic analysis of endocytosis in Caenorhabditis elegans: coelomocyte
RT uptake defective mutants.";
RL Genetics 159:133-145(2001).
CC -!- FUNCTION: Thought to regulate endocytosis in coelomocytes through
CC modulation of phospholipase C activity. Possible acetylcholine
CC receptor. {ECO:0000269|PubMed:11560892, ECO:0000269|PubMed:15936276}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:15936276}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15936276}.
CC -!- TISSUE SPECIFICITY: Expressed in coelomocytes.
CC {ECO:0000269|PubMed:15936276}.
CC -!- DISRUPTION PHENOTYPE: Worms display a lack of uptake of GFP from the
CC pseudocoelom into coelomocytes, suggesting a decrease or absence of
CC endocytosis in coelomocytes. Mutants also display a slightly dumpy
CC appearance with a low penetrance defect in distal tip cell leader
CC function, indicating defects in coelomocyte function.
CC {ECO:0000269|PubMed:11560892}.
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; AY611497; AAT42012.1; -; mRNA.
DR EMBL; FO080276; CCD62529.1; -; Genomic_DNA.
DR PIR; S44741; S44741.
DR RefSeq; NP_498710.2; NM_066309.5.
DR AlphaFoldDB; P34271; -.
DR SMR; P34271; -.
DR STRING; 6239.C02C2.3; -.
DR EPD; P34271; -.
DR PaxDb; P34271; -.
DR PeptideAtlas; P34271; -.
DR EnsemblMetazoa; C02C2.3.1; C02C2.3.1; WBGene00000845.
DR GeneID; 176104; -.
DR KEGG; cel:CELE_C02C2.3; -.
DR UCSC; C02C2.3; c. elegans.
DR CTD; 176104; -.
DR WormBase; C02C2.3; CE30416; WBGene00000845; cup-4.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_633456_0_0_1; -.
DR InParanoid; P34271; -.
DR OMA; VWQPKIK; -.
DR OrthoDB; 1028699at2759; -.
DR PhylomeDB; P34271; -.
DR Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-CEL-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR PRO; PR:P34271; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000845; Expressed in larva and 3 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
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:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015464; F:acetylcholine receptor activity; NAS:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; TAS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
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:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:WormBase.
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:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0061771; P:response to caloric restriction; IDA:UniProtKB.
DR GO; GO:1901562; P:response to paraquat; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR SUPFAM; SSF63712; SSF63712; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Disulfide bond; Endocytosis; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..433
FT /note="Acetylcholine receptor-like protein cup-4"
FT /id="PRO_0000000404"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..192
FT /evidence="ECO:0000250"
FT MUTAGEN 272
FT /note="V->D: In ar494; coelomocyte endocytosis defect."
FT /evidence="ECO:0000269|PubMed:15936276"
SQ SEQUENCE 433 AA; 49771 MW; F56A3D4E13AC9F5D CRC64;
MKIIIFVCFI LIFYLPIQKK HVNSQQQGID SDDGDAESFF NKSYSEHQSA LEQKIFRGYN
PKNRPMKNAS FPTIVDVHWH IIHVSINQRE QTMTVHGHIY MRWFDEFLVW DPKDFNNIQY
ARVKKWQVWQ PKIKVSNSAS GLGSAFDFST SAHVIIQMMG KDRAKVEMYP TFSIKVGCAF
DFTDYPYDLN KCAINLFSTS TMADVQLQNL YAIPPTLSFG WEEQKMKRII SDFKIQNVSS
SALYYTNGNI TSSAPITGFD LGSTWSMLAV TVSFVRHSPL FEAAVVTPCI VVASLISMTF
FIDSLSSTFL LMMLHFYVQL IFLHDLVEKL PLSVSEIPFC IKLIGILMYT NGLTLVLHSS
LLCGSYYKCP VPQQLNKIFV IEEYIPNTFK EKVQIKKEES NKSWRDLMKL IRPIIGFVLI
ILLICMFFVC LLL
