ID MACS_BOVIN STANDARD; PRT; 331 AA. AC P12624; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE (MARCKS) (ACAMP-81). GN MACS. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89282412; PubMed=2734111; RA Stumpo D.J., Graff J.M., Albert K.A., Greengard P., Blackshear P.J.; RT "Nucleotide sequence of a cDNA for the bovine myristoylated alanine- RT rich C kinase substrate (MARCKS)."; RL Nucleic Acids Res. 17:3987-3988(1989). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=89264553; PubMed=2726763; RA Stumpo D.J., Graff J.M., Albert K.A., Greengard P., Blackshear P.J.; RT "Molecular cloning, characterization, and expression of a cDNA RT encoding the '80- to 87-kDa' myristoylated alanine-rich C kinase RT substrate: a major cellular substrate for protein kinase C."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4012-4016(1989). RN [3] RP PARTIAL SEQUENCE. RX MEDLINE=92171958; PubMed=1540183; RA Mizutani A., Tokumitsu H., Hidaka H.; RT "Acidic calmodulin binding protein, ACAMP-81, is MARCKS protein RT interacting with synapsin I."; RL Biochem. Biophys. Res. Commun. 182:1395-1401(1992). RN [4] RP PHOSPHORYLATION SITES. RX MEDLINE=89308594; PubMed=2473066; RA Graff J.M., Stumpo D.J., Blackshear P.J.; RT "Characterization of the phosphorylation sites in the chicken and RT bovine myristoylated alanine-rich C kinase substrate protein, a RT prominent cellular substrate for protein kinase C."; RL J. Biol. Chem. 264:11912-11919(1989). RN [5] RP PHOSPHORYLATION SITES, AND REVISIONS. RC TISSUE=BRAIN; RX MEDLINE=94308052; PubMed=8034575; RA Taniguchi H., Manenti S., Suzuki M., Titani K.; RT "Myristoylated alanine-rich C kinase substrate (MARCKS), a major RT protein kinase C substrate, is an in vivo substrate of proline- RT directed protein kinase(s). A mass spectroscopic analysis of the post- RT translational modifications."; RL J. Biol. Chem. 269:18299-18302(1994). RN [6] RP REVERSIBLE ASSOCIATION WITH THE MEMBRANE. RX MEDLINE=91238951; PubMed=2034276; RA Thelen M., Rosen A., Nairn A.C., Aderem A.; RT "Regulation by phosphorylation of reversible association of a RT myristoylated protein kinase C substrate with the plasma membrane."; RL Nature 351:320-322(1991). RN [7] RP ACTIN-FILAMENT CROSS-LINKING. RX MEDLINE=92220195; PubMed=1560845; RA Hartwig J.H., Thelen M., Rosen A., Janmey P.A., Nairn A.C., Aderem A.; RT "MARCKS is an actin filament crosslinking protein regulated by protein RT kinase C and calcium-calmodulin."; RL Nature 356:618-622(1992). 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 -!- CAUTION: REF.1 AND REF.2 SEQUENCES DIFFER FROM THAT SHOWN IN CC POSITIONS 140 TO 150 DUE TO A FRAMESHIFT. 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; M24638; AAA30635.1; ALT_FRAME. DR PIR; A32904; A32904. DR PIR; PS0338; PS0338. DR PIR; S08341; S08341. 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 FT LIPID 1 1 MYRISTATE. FT DOMAIN 150 174 CALMODULIN-BINDING (PSD). FT MOD_RES 26 26 PHOSPHORYLATION. FT MOD_RES 45 45 PHOSPHORYLATION. FT MOD_RES 80 80 PHOSPHORYLATION. FT MOD_RES 99 99 PHOSPHORYLATION. FT MOD_RES 116 116 PHOSPHORYLATION. FT MOD_RES 133 133 PHOSPHORYLATION. FT MOD_RES 157 157 PHOSPHORYLATION (BY PKC). FT MOD_RES 161 161 PHOSPHORYLATION (BY PKC). FT MOD_RES 165 165 PHOSPHORYLATION (BY PKC). FT MOD_RES 168 168 PHOSPHORYLATION (BY PKC). SQ SEQUENCE 331 AA; 31450 MW; 0F77BF117EDB35CA CRC64; GAQFSKTAAK GEATAERPGE AAVASSPSKA NGQENGHVKV NGDASPAAAE PGAKEELQAN GSAPAADKEE PAAAGSGAAS PAAAEKDEPA AAAPDAGASP VEKEAPVEGG AAEPGSPTAA EGEAASAASS SSSPKAEDGA TPSPSNETPK KKKKRFSFKK SFKLSGFSFK KNKKEAGEGG EAEGAAGASA EGGKDEASGG AAAAAGEAGA APGEPTAAPG EEAAAGEEGA AGGDPQEAKP EEAAVAPEKP PASEEAKAVE EPSKAEEKAE EAGVSAAGCE APSAAGPGCP RAGGAPREEA APPRASSACS APSQEAQPEC SPEAPPAEAA E //