ID MACS_RAT STANDARD; PRT; 308 AA. AC P30009; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE (MARCKS). GN MACS. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RX MEDLINE=91201362; PubMed=1707878; RA Erusalimsky J.D., Brooks S.F., Herget T., Morris C., Rozengurt E.; RT "Molecular cloning and characterization of the acidic 80-kDa protein RT kinase C substrate from rat brain. Identification as a glycoprotein."; RL J. Biol. Chem. 266:7073-7080(1991). RN [2] RP PHOSPHORYLATION SITES. RC TISSUE=BRAIN; RX MEDLINE=93135774; PubMed=8422248; RA Heemskerk F.M., Chen H.C., Huang F.L.; RT "Protein kinase C phosphorylates Ser-152, Ser-156 and Ser-163 but not RT Ser-160 of MARCKS in rat brain."; RL Biochem. Biophys. Res. Commun. 190:236-241(1993). CC -!- FUNCTION: MARCKS IS THE MOST PROMINENT CELLULAR SUBSTRATE FOR CC PROTEIN KINASE C. THIS PROTEIN BINDS CALMODULIN, ACTIN, AND CC SYNAPSIN. MARCKS IS A FILAMENTOUS (F) ACTIN CROSS-LINKING PROTEIN. CC -!- PTM: PHOSPHORYLATION BY PKC DISPLACES MARCKS FROM THE MEMBRANE. IT CC ALSO INHIBITS THE F-ACTIN CROSS-LINKING ACTIVITY. CC -!- SIMILARITY: BELONGS TO THE MARCKS 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; M59859; -; NOT_ANNOTATED_CDS. DR PIR; A39773; A39773. DR INTERPRO; IPR002101; -. DR PFAM; PF02063; MARCKS; 1. DR PRINTS; PR00963; MARCKS. DR PROSITE; PS00826; MARCKS_1; 1. DR PROSITE; PS00827; MARCKS_2; 1. KW Phosphorylation; Myristate; Calmodulin-binding; Actin-binding; KW Membrane. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 144 168 CALMODULIN-BINDING (PSD). FT MOD_RES 151 151 PHOSPHORYLATION (BY PKC). FT MOD_RES 155 155 PHOSPHORYLATION (BY PKC). FT MOD_RES 162 162 PHOSPHORYLATION (BY PKC). SQ SEQUENCE 308 AA; 29663 MW; 59B50228BB1B75D2 CRC64; GAQFSKTAAK GEAAAERPGE AAVASSPSKA NGQENGHVKV NGDASPAAAE PGAKEELQAN GSAPAADKEE PASGGAATPA AADKDEAAAA PEPGAATADK EAAEAEPAEP GSPSAETEGA SASSTSSPKA EDGAAPSPSS ETPKKKKKRF SFKKSFKLSG FSFKKSKKEA GEGAEAEGAT ADGAKDEAAA AAGGDAAAAP GEQAGGAGAE GAEGGESREA EAAEPEQPEQ PEQPAAEEPR AEEPSEAVGE KAEEPAPGAT ADDAPSAAGP EQEAPAATDE PAASAAPSAS PEPQPECSPE APPAPVAE //