ID   MARCS_CHICK             Reviewed;         281 AA.
AC   P16527;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Myristoylated alanine-rich C-kinase substrate;
DE            Short=MARCKS;
GN   Name=MARCKS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MYRISTOYLATION AT GLY-2, AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   PubMed=2608063; DOI=10.1210/mend-3-11-1903;
RA   Graff J.M., Stumpo D.J., Blackshear P.J.;
RT   "Molecular cloning, sequence, and expression of a cDNA encoding the chicken
RT   myristoylated alanine-rich C kinase substrate (MARCKS).";
RL   Mol. Endocrinol. 3:1903-1906(1989).
CC   -!- FUNCTION: MARCKS is the most prominent cellular substrate for protein
CC       kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is
CC       a filamentous (F) actin cross-linking protein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
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DR   EMBL; M31650; AAA48946.1; -; mRNA.
DR   PIR; A41400; A41400.
DR   RefSeq; NP_990811.1; NM_205480.1.
DR   AlphaFoldDB; P16527; -.
DR   BMRB; P16527; -.
DR   BioGRID; 676720; 1.
DR   iPTMnet; P16527; -.
DR   GeneID; 396473; -.
DR   KEGG; gga:396473; -.
DR   CTD; 4082; -.
DR   VEuPathDB; HostDB:geneid_396473; -.
DR   InParanoid; P16527; -.
DR   OrthoDB; 1628566at2759; -.
DR   PRO; PR:P16527; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   InterPro; IPR002101; MARCKS.
DR   PANTHER; PTHR14353; PTHR14353; 1.
DR   Pfam; PF02063; MARCKS; 1.
DR   PRINTS; PR00963; MARCKS.
DR   PROSITE; PS00826; MARCKS_1; 1.
DR   PROSITE; PS00827; MARCKS_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Lipoprotein; Membrane; Myristate;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..281
FT                   /note="Myristoylated alanine-rich C-kinase substrate"
FT                   /id="PRO_0000157151"
FT   REGION          1..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..141
FT                   /note="Calmodulin-binding (PSD)"
FT   COMPBIAS        69..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:2608063"
SQ   SEQUENCE   281 AA;  27728 MW;  CCAF4875E9FD176E CRC64;
     MGAQFSKTAA KGEAAAEKPG EAVAASPSKA NGQENGHVKV NGDASPAAAE AGKEEVQANG
     SAPAEETGKE EAASSEPASE KEAAEAESTE PASPAEGEAS PKTEEGATPS SSSETPKKKK
     KRFSFKKSFK LSGFSFKKNK KEAGEGAESE GGAAAAAEGG KEEAAAAAPE AAGGEEGKAA
     AEEASAAAAG SREAAKEEAG DSQEAKSDEA APEKATGEEA PAAEEQQQQQ QQEKAAEEAG
     AAATSEAGSG EQEAAPAEEP AAARQEAPSE SSPEGPAEPA E