ID RAPSN_CHICK Reviewed; 412 AA. AC O42393; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 149. DE RecName: Full=43 kDa receptor-associated protein of the synapse; DE Short=RAPsyn; DE AltName: Full=43 kDa postsynaptic protein; DE AltName: Full=Acetylcholine receptor-associated 43 kDa protein; GN Name=RAPSN; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C; RX PubMed=9185539; DOI=10.1523/jneurosci.17-13-05016.1997; RA Burns A.L., Benson D., Howard M.J., Margiotta J.F.; RT "Chick ciliary ganglion neurons contain transcripts coding for RT acetylcholine receptor-associated protein at synapses (rapsyn)."; RL J. Neurosci. 17:5016-5026(1997). CC -!- FUNCTION: Postsynaptic protein required for clustering of nicotinic CC acetylcholine receptors (nAChRs) at the neuromuscular junction. It may CC link the receptor to the underlying postsynaptic cytoskeleton, possibly CC by direct association with actin or spectrin (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Postsynaptic cell membrane; Peripheral membrane CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic CC surface of postsynaptic membranes. CC -!- TISSUE SPECIFICITY: Expressed in muscle fibers and in neurons. CC -!- DOMAIN: A cysteine-rich region homologous to part of the regulatory CC domain of protein kinase C may be important in interactions of this CC protein with the lipid bilayer. CC -!- SIMILARITY: Belongs to the RAPsyn family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF000138; AAB63149.1; -; mRNA. DR RefSeq; NP_990428.1; NM_205097.1. DR AlphaFoldDB; O42393; -. DR SMR; O42393; -. DR STRING; 9031.ENSGALP00000013132; -. DR PaxDb; 9031-ENSGALP00000013132; -. DR GeneID; 395986; -. DR KEGG; gga:395986; -. DR CTD; 5913; -. DR VEuPathDB; HostDB:geneid_395986; -. DR eggNOG; KOG1941; Eukaryota. DR InParanoid; O42393; -. DR PhylomeDB; O42393; -. DR PRO; PR:O42393; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. 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 CDD; cd16478; RING-H2_Rapsyn; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001237; Postsynaptic. DR InterPro; IPR018293; Postsynaptic_CS. DR InterPro; IPR019568; Rapsyn_myristoylation/link_N. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46574; 43 KDA RECEPTOR-ASSOCIATED PROTEIN OF THE SYNAPSE; 1. DR PANTHER; PTHR46574:SF1; 43 KDA RECEPTOR-ASSOCIATED PROTEIN OF THE SYNAPSE; 1. DR Pfam; PF10579; Rapsyn_N; 1. DR Pfam; PF17874; TPR_MalT; 1. DR Pfam; PF13639; zf-RING_2; 1. DR PRINTS; PR00217; POSTSYNAPTIC. DR SMART; SM00184; RING; 1. DR SMART; SM00028; TPR; 6. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS00405; 43_KD_POSTSYNAPTIC; 1. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 2: Evidence at transcript level; KW Cell membrane; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; KW Metal-binding; Myristate; Phosphoprotein; Postsynaptic cell membrane; KW Reference proteome; Repeat; Synapse; TPR repeat; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..412 FT /note="43 kDa receptor-associated protein of the synapse" FT /id="PRO_0000167593" FT REPEAT 6..39 FT /note="TPR 1" FT REPEAT 83..116 FT /note="TPR 2" FT REPEAT 123..156 FT /note="TPR 3" FT REPEAT 163..196 FT /note="TPR 4" FT REPEAT 206..239 FT /note="TPR 5" FT REPEAT 246..279 FT /note="TPR 6" FT REPEAT 286..319 FT /note="TPR 7" FT ZN_FING 363..403 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT MOD_RES 196 FT /note="Phosphotyrosine" FT /evidence="ECO:0000255" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250" SQ SEQUENCE 412 AA; 46808 MW; 0882BB9F924202EE CRC64; MGQDQTKQQI EKGLHLYQSN QTEKALQVWM RVLEKSADPA GRFRVLGCLI TAHAEMGRYK DMLKFAVVQI DTARELEDPN YLTEGYLNLA RSNEKLCEFQ KTISYCKTCL NMQGTTVSLQ LNGQVSLSMG NAFLGLSIFQ KALECFEKAL RYAHNNDDKM LECRVCCSLG NFYAQIKDYE KALFFPCKAA ELVNDYGAGW SLKYRAMSQY HMAVAYRKLG RLADAMDCCE ESMKIALQHG DRPLQALCLL CFADIHLSRR DVQTAFPRYD SAMSIMTEIG NRLGQIQVLL GVAKCWMIQK ELDKALESIE KAQELAEGLG NKLGLLKLHC LCERIYRTKG LQQELRDHVV KFHECVEEME LYCGMCGESI GEKNNQLQAL PCSHFFHLKC LQTNGTRGCP NCRRLSVKPG YV //