ID   RAPSN_MOUSE             Reviewed;         412 AA.
AC   P12672; Q2M2N6;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   24-JAN-2024, entry version 196.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=2737281; DOI=10.1016/0014-5793(89)80629-5;
RA   Froehner S.C.;
RT   "Expression of RNA transcripts for the postsynaptic 43 kDa protein in
RT   innervated and denervated rat skeletal muscle.";
RL   FEBS Lett. 249:229-233(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=3170600; DOI=10.1016/s0021-9258(19)37631-8;
RA   Frail D.E., McLaughlin L.L., Mudd J., Merlie J.P.;
RT   "Identification of the mouse muscle 43,000-dalton acetylcholine receptor-
RT   associated protein (RAPsyn) by cDNA cloning.";
RL   J. Biol. Chem. 263:15602-15607(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- 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   -!- PTM: Ubiquitinated by the BCR(KLHL8) complex, leading to its
CC       degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RAPsyn family. {ECO:0000305}.
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DR   EMBL; X15788; CAA33789.1; -; mRNA.
DR   EMBL; J03962; AAA40030.1; -; mRNA.
DR   EMBL; AL672241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466519; EDL27517.1; -; Genomic_DNA.
DR   EMBL; BC111863; AAI11864.1; -; mRNA.
DR   CCDS; CCDS16422.1; -.
DR   PIR; A31995; A31995.
DR   RefSeq; NP_033049.2; NM_009023.3.
DR   AlphaFoldDB; P12672; -.
DR   SMR; P12672; -.
DR   BioGRID; 202585; 12.
DR   IntAct; P12672; 2.
DR   MINT; P12672; -.
DR   STRING; 10090.ENSMUSP00000054150; -.
DR   iPTMnet; P12672; -.
DR   PhosphoSitePlus; P12672; -.
DR   PaxDb; 10090-ENSMUSP00000054150; -.
DR   ProteomicsDB; 254985; -.
DR   Antibodypedia; 13774; 201 antibodies from 34 providers.
DR   DNASU; 19400; -.
DR   Ensembl; ENSMUST00000050323.6; ENSMUSP00000054150.6; ENSMUSG00000002104.12.
DR   GeneID; 19400; -.
DR   KEGG; mmu:19400; -.
DR   UCSC; uc008kud.2; mouse.
DR   AGR; MGI:99422; -.
DR   CTD; 5913; -.
DR   MGI; MGI:99422; Rapsn.
DR   VEuPathDB; HostDB:ENSMUSG00000002104; -.
DR   eggNOG; KOG1941; Eukaryota.
DR   GeneTree; ENSGT00390000016785; -.
DR   InParanoid; P12672; -.
DR   OMA; ALRCSHI; -.
DR   OrthoDB; 893642at2759; -.
DR   PhylomeDB; P12672; -.
DR   TreeFam; TF328344; -.
DR   BioGRID-ORCS; 19400; 0 hits in 77 CRISPR screens.
DR   PRO; PR:P12672; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P12672; Protein.
DR   Bgee; ENSMUSG00000002104; Expressed in muscle tissue and 77 other cell types or tissues.
DR   ExpressionAtlas; P12672; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0033130; F:acetylcholine receptor binding; IPI:MGI.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:MGI.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IEA:InterPro.
DR   GO; GO:0098879; F:structural constituent of postsynaptic specialization; IDA:SynGO.
DR   GO; GO:1903540; P:establishment of protein localization to postsynaptic membrane; ISO:MGI.
DR   GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:2000673; P:positive regulation of motor neuron apoptotic process; IMP:MGI.
DR   GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; ISO:MGI.
DR   GO; GO:1901626; P:regulation of postsynaptic membrane organization; ISO:MGI.
DR   GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IDA:MGI.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:MGI.
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; 7.
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.
DR   Genevisible; P12672; MM.
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; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..412
FT                   /note="43 kDa receptor-associated protein of the synapse"
FT                   /id="PRO_0000167592"
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   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        344..345
FT                   /note="EL -> DV (in Ref. 1; CAA33789)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   412 AA;  46393 MW;  EB5C656229AB0D15 CRC64;
     MGQDQTKQQI EKGLQLYQSN QTEKALQVWM KVLEKGSDLV GRFRVLGCLV TAHSEMGRYK
     EMLKFAVVQI DTARGLEDAD FLLESYLNLA RSNEKLCEFH KTISYCKTCL GLPGTRAGAQ
     LGGQVSLSMG NAFLGLSLFQ KALESFEKAL RYAHNNDDTM LECRVCCSLG SFYAQVKDYE
     KALFFPCKAA ELVNDYGKGW SLKYRAMSQY HMAVAYRLLG HLGSAMECCE ESMKIALQHG
     DRPLQALCLL CFADIHRSRG DLETAFPRYD SAMSIMTEIG NRLGQVHVLL GVAKCWMARK
     VQDKALDAIE KAQDLAEEVG NKLSQLKLHC LSESIYRSKG LQRELRTHVV RFHECVEETE
     LYCGLCGESI GERNSRLQAL PCSHIFHLRC LQNNGTRSCP NCRRSSMKPG FV
//