RIC3_CAEEL
ID RIC3_CAEEL Reviewed; 378 AA.
AC Q22472;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Resistance to inhibitors of cholinesterase protein 3;
GN Name=ric-3; Synonyms=des-5; ORFNames=T14A8.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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 [2]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11867529; DOI=10.1093/emboj/21.5.1012;
RA Halevi S., McKay J., Palfreyman M., Yassin L., Eshel M., Jorgensen E.,
RA Treinin M.;
RT "The C. elegans ric-3 gene is required for maturation of nicotinic
RT acetylcholine receptors.";
RL EMBO J. 21:1012-1020(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH DEG-3.
RX PubMed=15932871; DOI=10.1074/jbc.m504369200;
RA Ben-Ami H.C., Yassin L., Farah H., Michaeli A., Eshel M., Treinin M.;
RT "RIC-3 affects properties and quantity of nicotinic acetylcholine receptors
RT via a mechanism that does not require the coiled-coil domains.";
RL J. Biol. Chem. 280:28053-28060(2005).
RN [4]
RP FUNCTION.
RX PubMed=16466809; DOI=10.1016/j.jneumeth.2005.11.016;
RA Gottschalk A., Schafer W.R.;
RT "Visualization of integral and peripheral cell surface proteins in live
RT Caenorhabditis elegans.";
RL J. Neurosci. Methods 154:68-79(2006).
CC -!- FUNCTION: Required for maturation and cell surface expression of
CC acetylcholine receptors. {ECO:0000269|PubMed:11867529,
CC ECO:0000269|PubMed:15932871, ECO:0000269|PubMed:16466809}.
CC -!- SUBUNIT: Interacts with the deg-3/des-2 acetylcholine receptor.
CC {ECO:0000269|PubMed:15932871}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:11867529}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:11867529}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal muscles, body wall muscles
CC and in most neurons. {ECO:0000269|PubMed:11867529}.
CC -!- SIMILARITY: Belongs to the ric-3 family. {ECO:0000305}.
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DR EMBL; FO080379; CCD63313.1; -; Genomic_DNA.
DR PIR; T16872; T16872.
DR RefSeq; NP_501299.1; NM_068898.4.
DR AlphaFoldDB; Q22472; -.
DR SMR; Q22472; -.
DR BioGRID; 42687; 4.
DR IntAct; Q22472; 1.
DR STRING; 6239.T14A8.1; -.
DR iPTMnet; Q22472; -.
DR EPD; Q22472; -.
DR PaxDb; Q22472; -.
DR PeptideAtlas; Q22472; -.
DR PRIDE; Q22472; -.
DR EnsemblMetazoa; T14A8.1.1; T14A8.1.1; WBGene00004363.
DR GeneID; 177570; -.
DR KEGG; cel:CELE_T14A8.1; -.
DR UCSC; T14A8.1; c. elegans.
DR CTD; 37384; -.
DR WormBase; T14A8.1; CE27448; WBGene00004363; ric-3.
DR eggNOG; KOG4808; Eukaryota.
DR GeneTree; ENSGT00440000034107; -.
DR HOGENOM; CLU_732029_0_0_1; -.
DR InParanoid; Q22472; -.
DR OMA; IMYRIFL; -.
DR OrthoDB; 1448427at2759; -.
DR PRO; PR:Q22472; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004363; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:WormBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IDA:WormBase.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:WormBase.
DR GO; GO:0006937; P:regulation of muscle contraction; IGI:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR DisProt; DP00613; -.
DR InterPro; IPR026160; Ric3.
DR InterPro; IPR032763; RIC3_N.
DR PANTHER; PTHR21723; PTHR21723; 2.
DR Pfam; PF15361; RIC3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="Resistance to inhibitors of cholinesterase protein
FT 3"
FT /id="PRO_0000302735"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..152
FT /note="Sufficient for function in acetylcholine receptor
FT folding"
FT REGION 74..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..212
FT /evidence="ECO:0000255"
FT COMPBIAS 220..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 43112 MW; 7C4D25038C35C453 CRC64;
MPKTERRRDR DRDRDRERRN RRKRDDSYDD YDEEGGISGW KLGLVFGVIV VCFAMLYPTL
FHPMLMGFLG RSPPSSPSIN QQRPPIHPAM GGGSGQRHPG GGADVHPAMR MAQAQAESQS
GGSKGMFTWM LPVYTIGVVL FLLYTLFKSK GKKSKRKKRN YFDSEDDDDE SESETKYGGK
FGKKKLEGLQ KRLRETESAM SKILEQLESV QAGANPVDLD AADKRSEQLE EDPSVKEAVG
LTETNEQYIK DLEVALKEFQ SLSKEYDKAK MKKLKRKDSS SDEDEEDEEE NSSELSEIEE
EEEEVKPVKK SKSSSQSVGK RKNRPKSTSE EEDEGEEESR KVAEDAEEEG IDIDSEIREH
AEKEKKDKNV RRRRPKKT
