RAPSN_MOUSE
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 03-AUG-2022, entry version 189.
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; 10.
DR IntAct; P12672; 1.
DR MINT; P12672; -.
DR STRING; 10090.ENSMUSP00000054150; -.
DR iPTMnet; P12672; -.
DR PhosphoSitePlus; P12672; -.
DR PaxDb; P12672; -.
DR PRIDE; P12672; -.
DR ProteomicsDB; 254985; -.
DR Antibodypedia; 13774; 175 antibodies from 34 providers.
DR DNASU; 19400; -.
DR Ensembl; ENSMUST00000050323; ENSMUSP00000054150; ENSMUSG00000002104.
DR GeneID; 19400; -.
DR KEGG; mmu:19400; -.
DR UCSC; uc008kud.2; mouse.
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; 1245397at2759; -.
DR PhylomeDB; P12672; -.
DR TreeFam; TF328344; -.
DR BioGRID-ORCS; 19400; 0 hits in 72 CRISPR screens.
DR PRO; PR:P12672; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P12672; protein.
DR Bgee; ENSMUSG00000002104; Expressed in muscle tissue and 75 other tissues.
DR ExpressionAtlas; P12672; baseline and differential.
DR Genevisible; P12672; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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:0043495; F:protein-membrane adaptor activity; IEA:InterPro.
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: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:0007271; P:synaptic transmission, cholinergic; ISO:MGI.
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; 7.
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; 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
