ID RAPS_TORCA STANDARD; PRT; 411 AA. AC P09108; DT 01-MAR-1989 (Rel. 10, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 43 KDA RECEPTOR-ASSOCIATED PROTEIN OF THE SYNAPSE (RAPSYN) DE (ACETYLCHOLINE RECEPTOR-ASSOCIATED 43 KDA PROTEIN) (43 KDA DE POSTSYNAPTIC PROTEIN). GN RAPSN. OS Torpedo californica (Pacific electric ray). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea; OC Torpediniformes; Torpedinoidei; Torpedinidae; Torpedo. OX NCBI_TaxID=7787; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87317641; PubMed=3476945; 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 RT encode two proteins with different carboxyl termini."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6302-6306(1987). RN [2] RP SEQUENCE OF 8-412. RX MEDLINE=88107644; PubMed=3427060; RA Carr C., McCourt D., Cohen J.B.; RT "The 43-kilodalton protein of Torpedo nicotinic postsynaptic RT membranes: purification and determination of primary structure."; RL Biochemistry 26:7090-7102(1987). RN [3] RP MYRISTOYLATION. RX MEDLINE=88331095; PubMed=3417776; RA Musil L.S., Carr C., Cohen J.B., Merlie J.P.; RT "Acetylcholine receptor-associated 43K protein contains covalently RT bound myristate."; RL J. Cell Biol. 107:1113-1121(1988). CC -!- FUNCTION: THOUGHT TO PLAY SOME ROLE IN ANCHORING OR STABILIZING CC THE NICOTINIC ACETYLCHOLINE RECEPTOR AT SYNAPTIC SITES. IT MAY CC LINK THE RECEPTOR TO THE UNDERLYING POSTSYNAPTIC CYTOSKELETON, CC POSSIBLY BY DIRECT ASSOCIATION WITH ACTIN OR SPECTRIN. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC SURFACE OF POSTSYNAPTIC CC MEMBRANES. CC -!- ALTERNATIVE PRODUCTS: THERE ARE AT LEAST TWO DISTINCT PROTEINS CC EXPRESSED, WHICH DIFFER IN THEIR C-TERMINUS. CC -!- DOMAIN: A CYSTEINE-RICH REGION HOMOLOGOUS TO PART OF THE CC REGULATORY DOMAIN OF PROTEIN KINASE C MAY BE IMPORTANT IN CC INTERACTIONS OF THIS PROTEIN WITH THE LIPID BILAYER. CC -!- SIMILARITY: BELONGS TO THE RAPSYN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J02952; AAA49282.1; -. DR EMBL; J02953; AAA49283.1; -. DR PIR; A28009; A28009. DR INTERPRO; IPR001237; -. DR INTERPRO; IPR001841; -. DR PFAM; PF00097; zf-C3HC4; 1. DR PRINTS; PR00217; POSTSYNAPTIC. DR PROSITE; PS00405; 43_KD_POSTSYNAPTIC; 1. KW Synapse; Postsynaptic membrane; Cytoskeleton; Phosphorylation; KW Myristate; Alternative splicing. FT INIT_MET 0 0 FT LIPID 1 1 MYRISTATE. FT MOD_RES 195 195 PHOSPHORYLATION (POTENTIAL). FT MOD_RES 404 404 PHOSPHORYLATION (POTENTIAL). FT DOMAIN 362 398 INVOLVED IN MEMBRANE ASSOCIATION FT (POTENTIAL). FT VARSPLIC 389 411 MISSING (IN SHORT ISOFORM). FT CONFLICT 361 361 Y -> T (IN REF. 2). FT CONFLICT 393 393 N -> D (IN REF. 2). FT CONFLICT 410 410 Y -> T (IN REF. 2). SQ SEQUENCE 411 AA; 46321 MW; 4D26262679FC9B4D CRC64; GQDQTKQQIE KGLQLYQANE TGKALEIWQQ VVERSTELPG RFRALGCLIT AHSEMGKYED MLRFAVAQSE AARQMGDPER VTEAYLNLAR GHEKLCEFSE AVAYCRTCLG AEGGPLRLQF NGQVCLSMGN AFLGLSAFQK ALECFEKALR YAHGNDDKML ECRVCCSLGA FYVQLKDYEK ALFFPCKSAE LVADYGRGWS LKYKAMSRYH MAAAYRKLGR MDDAMECCEE SMKIALQHQD RPLQALCLLC FADIHRHRSD IGKALPRYES SLNIMTEIGN RLGQAHVLLN IAKCWMTEKK LDKTLGVVQK AEELADAVGN KLVLLKAHCL YETIYREMGS DQLLRDHVVK FHECMEDMEL YCGLCGESIG DQNSQLQALP CSHLFHLKCL QTNGNRGCPN CKRSSVKPGY V //