ID   RAPSN_CAEEL             Reviewed;         596 AA.
AC   Q09485;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=43 kDa receptor-associated protein of the synapse homolog;
DE            Short=RAPsyn;
GN   Name=rpy-1; ORFNames=C18H9.7;
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   UBIQUITINATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=19158078; DOI=10.1074/jbc.m808230200;
RA   Nam S., Min K., Hwang H., Lee H.O., Lee J.H., Yoon J., Lee H., Park S.,
RA   Lee J.;
RT   "Control of rapsyn stability by the CUL-3-containing E3 ligase complex.";
RL   J. Biol. Chem. 284:8195-8206(2009).
CC   -!- FUNCTION: Postsynaptic protein required for clustering of nicotinic
CC       acetylcholine receptors (nAChRs) at the neuromuscular junction.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q09485; Q20759: CELE_F54C9.11; NbExp=3; IntAct=EBI-315739, EBI-312110;
CC   -!- TISSUE SPECIFICITY: Expressed in muscles and neurons.
CC       {ECO:0000269|PubMed:19158078}.
CC   -!- PTM: Ubiquitinated by the BCR(kel-8) complex in the absence of unc-29,
CC       leading to its degradation. {ECO:0000269|PubMed:19158078}.
CC   -!- DISRUPTION PHENOTYPE: Mutants are resistant to levamisole, an agonist
CC       of nAChRs. {ECO:0000269|PubMed:19158078}.
CC   -!- SIMILARITY: Belongs to the RAPsyn family. {ECO:0000305}.
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DR   EMBL; FO080625; CCD65265.1; -; Genomic_DNA.
DR   PIR; F88188; F88188.
DR   RefSeq; NP_495365.2; NM_062964.5.
DR   AlphaFoldDB; Q09485; -.
DR   SMR; Q09485; -.
DR   BioGRID; 39443; 51.
DR   DIP; DIP-25948N; -.
DR   IntAct; Q09485; 44.
DR   STRING; 6239.C18H9.7; -.
DR   PaxDb; Q09485; -.
DR   EnsemblMetazoa; C18H9.7.1; C18H9.7.1; WBGene00004507.
DR   EnsemblMetazoa; C18H9.7.2; C18H9.7.2; WBGene00004507.
DR   GeneID; 174105; -.
DR   UCSC; C18H9.7; c. elegans.
DR   CTD; 174105; -.
DR   WormBase; C18H9.7; CE51338; WBGene00004507; rpy-1.
DR   eggNOG; KOG1941; Eukaryota.
DR   GeneTree; ENSGT00390000016785; -.
DR   HOGENOM; CLU_030911_0_0_1; -.
DR   InParanoid; Q09485; -.
DR   OMA; ALRCSHI; -.
DR   OrthoDB; 398693at2759; -.
DR   PhylomeDB; Q09485; -.
DR   SignaLink; Q09485; -.
DR   PRO; PR:Q09485; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004507; Expressed in larva and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0033130; F:acetylcholine receptor binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IEA:InterPro.
DR   GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 3.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001237; Postsynaptic.
DR   InterPro; IPR019568; Rapsyn_myristoylation/link_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF10579; Rapsyn_N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   PRINTS; PR00217; POSTSYNAPTIC.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Repeat; TPR repeat; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..596
FT                   /note="43 kDa receptor-associated protein of the synapse
FT                   homolog"
FT                   /id="PRO_0000424031"
FT   REPEAT          6..39
FT                   /note="TPR 1"
FT   REPEAT          43..76
FT                   /note="TPR 2"
FT   REPEAT          83..116
FT                   /note="TPR 3"
FT   REPEAT          121..154
FT                   /note="TPR 4"
FT   REPEAT          161..194
FT                   /note="TPR 5"
FT   ZN_FING         374..418
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          535..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  65523 MW;  9601E092326E2ACB CRC64;
     MGQRQAKQHM QAGVKLYHQR HYAQAINKWR QSLNRLNNAE DRFITLGYLA QALCDQGEYE
     GMLSYALSQM QLATDQNDSA MKCEAFLNLA KAYERLADFT KALQYGKASL EHPSMDPRTP
     GYAHLTIALA HLGMSQFQQC LESFESAMNV ANETSDRLLE LQICVGLGSL FTLLRDITKA
     LIFLRNALAI VQSVTVDDVH AKYRCLILYH LSVALRMKGS LVDAKEACDE ASQLAVEMGN
     RAIHARCMCS LADIYRELGE SEAKETITKS WARYEDAYRV MRGANDKMGE VLVLSSMAKS
     ASESRSHYTG QCECQAIQLN KKCIEIANQI GCKHVVLKCH LRLAELYSQL NDDDSEETAR
     RAASRLTQEM QLFCNFCGQR YGLKDESLQA LRCSHIFHEK CLHTYLLQRT DQTCPKCRCR
     AVLSDNISIR SSIASTIDVQ SPSTSFAPPG GVATPLVSAA AELGDITPQA TLTRRSQQDK
     ILRGAEKDID RVDRSLARLK SQQSAAANAC SAVAVPSPEV PSTTASCASE PILTASTTSQ
     SHTHSNANHK PPPPPRKPCC SQAALPPSSI VALPPAMPLA EDGPLVITHT PTVTDV