RAPSN_CHICK
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 03-AUG-2022, entry version 144.
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}.
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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; O42393; -.
DR PRIDE; O42393; -.
DR GeneID; 395986; -.
DR KEGG; gga:395986; -.
DR CTD; 5913; -.
DR VEuPathDB; HostDB:geneid_395986; -.
DR eggNOG; KOG1941; Eukaryota.
DR InParanoid; O42393; -.
DR OrthoDB; 1245397at2759; -.
DR PhylomeDB; O42393; -.
DR PRO; PR:O42393; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.40.10; -; 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; IPR041617; TPR_MalT.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; SSF48452; SSF48452; 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
