ID   RIC3_CAEBR              Reviewed;         385 AA.
AC   Q60ZR7; A8XRI9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Resistance to inhibitors of cholinesterase protein 3;
GN   Name=ric-3; ORFNames=CBG17683;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Required for maturation and cell surface expression of
CC       acetylcholine receptors. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the deg-3/des-2 acetylcholine receptor.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ric-3 family. {ECO:0000305}.
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DR   EMBL; HE600976; CAP35263.1; -; Genomic_DNA.
DR   RefSeq; XP_002634339.1; XM_002634293.1.
DR   AlphaFoldDB; Q60ZR7; -.
DR   SMR; Q60ZR7; -.
DR   STRING; 6238.CBG17683; -.
DR   EnsemblMetazoa; CBG17683.1; CBG17683.1; WBGene00037247.
DR   GeneID; 8576334; -.
DR   KEGG; cbr:CBG_17683; -.
DR   CTD; 8576334; -.
DR   WormBase; CBG17683; CBP10623; WBGene00037247; Cbr-ric-3.
DR   eggNOG; KOG4808; Eukaryota.
DR   HOGENOM; CLU_732029_0_0_1; -.
DR   InParanoid; Q60ZR7; -.
DR   OMA; IMYRIFL; -.
DR   OrthoDB; 1448427at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
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; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IEA:EnsemblMetazoa.
DR   GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR   GO; GO:0006937; P:regulation of muscle contraction; IEA:EnsemblMetazoa.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   InterPro; IPR026160; Ric3.
DR   InterPro; IPR032763; RIC3_N.
DR   PANTHER; PTHR21723; PTHR21723; 2.
DR   Pfam; PF15361; RIC3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..385
FT                   /note="Resistance to inhibitors of cholinesterase protein
FT                   3"
FT                   /id="PRO_0000302734"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          32..152
FT                   /note="Sufficient for function in acetylcholine receptor
FT                   folding"
FT                   /evidence="ECO:0000250"
FT   REGION          72..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..307
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   385 AA;  44182 MW;  22259E184AA233DB CRC64;
     MPKLTDRNRD RDREKKKRRR RDDSYDDYEE EGGISGWKLG LVVGVIVVCF AMLYPTLFHP
     MLMGFLGRSS QPAPSINQQR PPIHPAMGGG GGQRHPGGYP SRPDVHPAMR MAQAQAEGQS
     GGSKGMFTWM LPIYTIGVVL FLLYTLFKSK GKKAKRKKRN YFDSEDDSED SEMETKYGGK
     FGKKKLKGLQ ERLRQTEDAM SKILEQLESV QAGANPVDLD AADKLALELE EDKSAKEAVG
     LTETNEQYIK DLEVALKEFQ SLSKAYDKEK MKKLKRKDSS SEEEEEEEEE EEEEEEELSE
     LSEVEEEEEE KPVKKGKKVV DQKKPAKKAI LRQKSTSEEE EETRIADKKA EEEEEEGIDI
     DFEIREHAER NKKDKNLRRR RPKKT