ID MRP_RABIT Reviewed; 199 AA. AC P35566; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 109. DE RecName: Full=MARCKS-related protein; DE AltName: Full=MARCKS-like protein 1; DE AltName: Full=Macrophage myristoylated alanine-rich C kinase substrate; DE Short=Mac-MARCKS; DE Short=MacMARCKS; GN Name=MARCKSL1; Synonyms=MLP, MRP; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION RP WITH CALMODULIN, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION, AND RP MYRISTOYLATION AT GLY-2. RC TISSUE=Macrophage; RX PubMed=1516135; DOI=10.1016/0092-8674(92)90312-z; RA Li J., Aderem A.; RT "MacMARCKS, a novel member of the MARCKS family of protein kinase C RT substrates."; RL Cell 70:791-801(1992). CC -!- FUNCTION: Controls cell movement by regulating actin cytoskeleton CC homeostasis and filopodium and lamellipodium formation (By similarity). CC When unphosphorylated, induces cell migration (By similarity). When CC phosphorylated by MAPK8, induces actin bundles formation and CC stabilization, thereby reducing actin plasticity, hence restricting CC cell movement, including neuronal migration (By similarity). May be CC involved in coupling the protein kinase C and calmodulin signal CC transduction systems (Probable). {ECO:0000250|UniProtKB:P28667, CC ECO:0000305|PubMed:1516135}. CC -!- SUBUNIT: Binds to filamentous actin (F-actin), but not to monomeric G- CC actin, independently of its phosphorylation status (By similarity). CC Interacts with calmodulin (PubMed:1516135). CC {ECO:0000250|UniProtKB:P28667, ECO:0000269|PubMed:1516135}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P28667}. Cell membrane CC {ECO:0000305|PubMed:1516135}; Lipid-anchor CC {ECO:0000305|PubMed:1516135}. Note=Associates with the membrane via the CC insertion of the N-terminal N-myristoyl chain and the partial insertion CC of the effector domain. Association of the effector domain with CC membranes may be regulated by Ca(2+)/calmodulin. Colocalizes with F- CC actin at the leading edge of migrating cells. CC {ECO:0000250|UniProtKB:P28667, ECO:0000250|UniProtKB:P49006}. CC -!- INDUCTION: Up-regulated in alveolar macrophages in response to CC bacterial lipopolysaccharide (LPS). {ECO:0000269|PubMed:1516135}. CC -!- PTM: Phosphorylated (PubMed:1516135). Phosphorylation at Ser-120 and CC Thr-182 is non-redundantly catalyzed by MAPK8 in vivo (By similarity). CC Phosphorylation at Thr-148 is preferentially catalyzed by MAPK8 in CC vivo, but this modification can also be catalyzed by other kinases in CC the absence of MAPK8 (By similarity). May be phosphorylated by protein CC kinase C, which disrupts the interaction with calmodulin CC (PubMed:1516135). {ECO:0000250|UniProtKB:P28667, CC ECO:0000269|PubMed:1516135}. CC -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S43921; AAB23156.1; -; mRNA. DR PIR; A43341; A43341. DR RefSeq; NP_001075787.1; NM_001082318.1. DR AlphaFoldDB; P35566; -. DR FunCoup; P35566; 122. DR STRING; 9986.ENSOCUP00000007731; -. DR iPTMnet; P35566; -. DR PaxDb; 9986-ENSOCUP00000007731; -. DR GeneID; 100009158; -. DR KEGG; ocu:100009158; -. DR CTD; 65108; -. DR eggNOG; ENOG502RYXK; Eukaryota. DR InParanoid; P35566; -. DR OrthoDB; 9948538at2759; -. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter. DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro. DR GO; GO:0007015; P:actin filament organization; IEA:TreeGrafter. DR GO; GO:0007417; P:central nervous system development; IEA:TreeGrafter. DR InterPro; IPR002101; MARCKS. DR PANTHER; PTHR14353:SF8; MARCKS-RELATED PROTEIN; 1. DR PANTHER; PTHR14353; MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE MARCKS; 1. DR Pfam; PF02063; MARCKS; 2. 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; Cell membrane; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Lipoprotein; Membrane; Myristate; KW Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000305|PubMed:1516135" FT CHAIN 2..199 FT /note="MARCKS-related protein" FT /id="PRO_0000157154" FT REGION 1..199 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 87..110 FT /note="Effector domain involved in lipid-binding and FT calmodulin-binding" FT /evidence="ECO:0000250|UniProtKB:P28667" FT COMPBIAS 16..26 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..64 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 76..85 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 86..98 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 156..167 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 181..199 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 14 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28667" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 85 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 93 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 101 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 104 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28667" FT MOD_RES 120 FT /note="Phosphoserine; by MAPK8" FT /evidence="ECO:0000250|UniProtKB:P28667" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28667" FT MOD_RES 148 FT /note="Phosphothreonine; by MAPK8" FT /evidence="ECO:0000250|UniProtKB:P28667" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49006" FT MOD_RES 170 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P28667" FT MOD_RES 182 FT /note="Phosphothreonine; by MAPK8" FT /evidence="ECO:0000250|UniProtKB:P28667" FT MOD_RES 191 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P28667" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:1516135" SQ SEQUENCE 199 AA; 19766 MW; D8C40706EF86CDE5 CRC64; MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVKSNGDL TPKGEGESPP VNGTDEAAGA TGDAIEPAPP SQGAEAKGDA PPKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS PTEEEQEQGE IGACSEEGTA PEGKAAATPE SQEPQAKGAE AGAACKGGDT EEEAGPPAEP STPSGPESGP TPAGAEQNE //