ID MACS_MOUSE STANDARD; PRT; 308 AA. AC P26645; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 01-JUL-1993 (Rel. 26, Last annotation update) DE MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE (MARCKS). GN MACS. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=MACROPHAGE; RX MEDLINE=91172836; PubMed=2006186; RA Seykora J.T., Ravetch J.V., Aderem A.; RT "Cloning and molecular characterization of the murine macrophage '68- RT kDa' protein kinase C substrate and its regulation by bacterial RT lipopolysaccharide."; RL Proc. Natl. Acad. Sci. U.S.A. 88:2505-2509(1991). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=FIBROBLAST; RX MEDLINE=91330872; PubMed=1868832; RA Brooks S.F., Herget T., Erusalimsky J.D., Rozengurt E.; RT "Protein kinase C activation potently down-regulates the expression of RT its major substrate, 80K, in Swiss 3T3 cells."; RL EMBO J. 10:2497-2505(1991). RN [3] RP PARTIAL SEQUENCE. RC STRAIN=SWISS; TISSUE=FIBROBLAST; RX MEDLINE=90346162; PubMed=2384168; RA Brooks S.F., Erusalimsky J.D., Totty N.F., Rozengurt E.; RT "Purification and internal amino acid sequence of the 80 kDa protein RT kinase C substrate from Swiss 3T3 fibroblasts. Homology with RT substrates from brain."; RL FEBS Lett. 268:291-295(1990). 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 -!- TISSUE SPECIFICITY: BRAIN, SPLEEN, LESS IN KIDNEY AND HEART, AND CC VERY LOW LEVELS IN LIVER. CC -!- INDUCTION: BY LIPOPOLYSACCHARIDE. 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; M60474; AAA39491.1; -. DR PIR; A39169; A39169. DR PIR; S16519; S16519. DR MGD; MGI:96907; Macs. 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) (BY SIMILARITY). FT MOD_RES 155 155 PHOSPHORYLATION (BY PKC) (BY SIMILARITY). FT MOD_RES 159 159 PHOSPHORYLATION (BY PKC) (BY SIMILARITY). FT MOD_RES 162 162 PHOSPHORYLATION (BY PKC) (BY SIMILARITY). FT CONFLICT 95 97 AGA -> TGT (IN REF. 2). SQ SEQUENCE 308 AA; 29530 MW; FB5313B913701C5C CRC64; GAQFSKTAAK GEATAERPGE AAVASSPSKA NGQENGHVKV NGDASPAAAE PGAKEELQAN GSAPAADKEE PASGSAATPA AAEKDEAAAA TEPGAGAADK EAAEAEPAEP SSPAAEAEGA SASSTSSPKA EDGAAPSPSS ETPKKKKKRF SFKKSFKLSG FSFKKSKKES GEGAEAEGAT AEGAKDEAAA AAGGEGAAAP GEQAGGAGAE GAAGGEPREA EAAEPEQPEQ PEQPAAEEPQ AEEQSEAAGE KAEEPAPGAT AGDASSAAGP EQEAPAATDE AAASAAPAAS PEPQPECSPE APPAPTAE //