MRP_RABIT
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 03-AUG-2022, entry version 100.
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}.
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DR EMBL; S43921; AAB23156.1; -; mRNA.
DR PIR; A43341; A43341.
DR RefSeq; NP_001075787.1; NM_001082318.1.
DR AlphaFoldDB; P35566; -.
DR STRING; 9986.ENSOCUP00000007731; -.
DR iPTMnet; P35566; -.
DR PRIDE; P35566; -.
DR GeneID; 100009158; -.
DR KEGG; ocu:100009158; -.
DR CTD; 65108; -.
DR eggNOG; ENOG502RYXK; Eukaryota.
DR InParanoid; P35566; -.
DR OrthoDB; 1511774at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR InterPro; IPR002101; MARCKS.
DR PANTHER; PTHR14353; PTHR14353; 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 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
