RAPSN_TETCF
ID RAPSN_TETCF Reviewed; 412 AA.
AC P09108;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
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 Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=3476945; DOI=10.1073/pnas.84.17.6302;
RA Frail D.E., Mudd J., Shah V., Carr C., Cohen J.B., Merlie J.P.;
RT "cDNAs for the postsynaptic 43-kDa protein of Torpedo electric organ encode
RT two proteins with different carboxyl termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6302-6306(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3077352; DOI=10.1242/dev.104.4.557;
RA Baldwin T.J., Theriot J.A., Yoshihara C.M., Burden S.J.;
RT "Regulation of transcript encoding the 43K subsynaptic protein during
RT development and after denervation.";
RL Development 104:557-564(1988).
RN [3]
RP PROTEIN SEQUENCE OF 8-412.
RX PubMed=3427060; DOI=10.1021/bi00396a034;
RA Carr C., McCourt D., Cohen J.B.;
RT "The 43-kilodalton protein of Torpedo nicotinic postsynaptic membranes:
RT purification and determination of primary structure.";
RL Biochemistry 26:7090-7102(1987).
RN [4]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=3417776; DOI=10.1083/jcb.107.3.1113;
RA Musil L.S., Carr C., Cohen J.B., Merlie J.P.;
RT "Acetylcholine receptor-associated 43K protein contains covalently bound
RT myristate.";
RL J. Cell Biol. 107:1113-1121(1988).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P09108-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P09108-2; Sequence=VSP_005534;
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; J02952; AAA49282.1; -; mRNA.
DR EMBL; J02953; AAA49283.1; -; mRNA.
DR PIR; A28009; A28009.
DR AlphaFoldDB; P09108; -.
DR SMR; P09108; -.
DR MINT; P09108; -.
DR iPTMnet; P09108; -.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033130; F:acetylcholine receptor binding; IEA:InterPro.
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:0007268; P:chemical synaptic transmission; IEA:InterPro.
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; IPR019734; TPR_repeat.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF10579; Rapsyn_N; 1.
DR Pfam; PF13176; TPR_7; 2.
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; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Phosphoprotein; Postsynaptic cell membrane; Repeat; Synapse; TPR repeat;
KW Zinc; 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_0000167594"
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:0000269|PubMed:3417776"
FT VAR_SEQ 390..412
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:3476945"
FT /id="VSP_005534"
FT CONFLICT 362
FT /note="Y -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="Y -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 46453 MW; C0BAE696ADFB2DFA CRC64;
MGQDQTKQQI EKGLQLYQAN ETGKALEIWQ QVVERSTELP GRFRALGCLI TAHSEMGKYE
DMLRFAVAQS EAARQMGDPE RVTEAYLNLA RGHEKLCEFS EAVAYCRTCL GAEGGPLRLQ
FNGQVCLSMG NAFLGLSAFQ KALECFEKAL RYAHGNDDKM LECRVCCSLG AFYVQLKDYE
KALFFPCKSA ELVADYGRGW SLKYKAMSRY HMAAAYRKLG RMDDAMECCE ESMKIALQHQ
DRPLQALCLL CFADIHRHRS DIGKALPRYE SSLNIMTEIG NRLGQAHVLL NIAKCWMTEK
KLDKTLGVVQ KAEELADAVG NKLVLLKAHC LYETIYREMG SDQLLRDHVV KFHECMEDME
LYCGLCGESI GDQNSQLQAL PCSHLFHLKC LQTNGNRGCP NCKRSSVKPG YV
