MRP_BOVIN
ID MRP_BOVIN Reviewed; 198 AA.
AC Q0VBZ9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=MARCKS-related protein;
DE AltName: Full=MARCKS-like protein 1;
GN Name=MARCKSL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Controls cell movement by regulating actin cytoskeleton
CC homeostasis and filopodium and lamellipodium formation. When
CC unphosphorylated, induces cell migration. When phosphorylated by MAPK8,
CC induces actin bundles formation and stabilization, thereby reducing
CC actin plasticity, hence restricting cell movement, including neuronal
CC migration. May be involved in coupling the protein kinase C and
CC calmodulin signal transduction systems. {ECO:0000250|UniProtKB:P28667,
CC ECO:0000250|UniProtKB:P49006}.
CC -!- SUBUNIT: Binds to filamentous actin (F-actin), but not to monomeric G-
CC actin, independently of its phosphorylation status. Interacts with
CC calmodulin. {ECO:0000250|UniProtKB:P28667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P28667}. Cell membrane
CC {ECO:0000250|UniProtKB:P28667}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P28667}. Note=Associates with the membrane via
CC the insertion of the N-terminal N-myristoyl chain and the partial
CC insertion of the effector domain. Association of the effector domain
CC with membranes may be regulated by Ca(2+)/calmodulin. Colocalizes with
CC F-actin at the leading edge of migrating cells.
CC {ECO:0000250|UniProtKB:P28667, ECO:0000250|UniProtKB:P49006}.
CC -!- PTM: Phosphorylated. Phosphorylation at Ser-120 and Thr-182 is non-
CC redundantly catalyzed by MAPK8 in vivo. Phosphorylation at Thr-148 is
CC preferentially catalyzed by MAPK8 in vivo, but this modification can
CC also be catalyzed by other kinases in the absence of MAPK8. May be
CC phosphorylated by protein kinase C, which disrupts the interaction with
CC calmodulin. {ECO:0000250|UniProtKB:P28667}.
CC -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
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DR EMBL; BC120310; AAI20311.1; -; mRNA.
DR EMBL; BC120422; AAI20423.1; -; mRNA.
DR RefSeq; NP_001069640.1; NM_001076172.1.
DR AlphaFoldDB; Q0VBZ9; -.
DR STRING; 9913.ENSBTAP00000054436; -.
DR PeptideAtlas; Q0VBZ9; -.
DR PRIDE; Q0VBZ9; -.
DR Ensembl; ENSBTAT00000066345; ENSBTAP00000054896; ENSBTAG00000046862.
DR GeneID; 539555; -.
DR KEGG; bta:539555; -.
DR CTD; 65108; -.
DR VEuPathDB; HostDB:ENSBTAG00000046862; -.
DR VGNC; VGNC:31245; MARCKSL1.
DR eggNOG; ENOG502RYXK; Eukaryota.
DR GeneTree; ENSGT00730000111349; -.
DR InParanoid; Q0VBZ9; -.
DR OMA; CSTNETE; -.
DR OrthoDB; 1511774at2759; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000046862; Expressed in floor plate of diencephalon and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Actin-binding; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49006"
FT CHAIN 2..198
FT /note="MARCKS-related protein"
FT /id="PRO_0000283705"
FT REGION 1..198
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 41
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 132
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 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28667"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P49006"
SQ SEQUENCE 198 AA; 19825 MW; 7661B711DC0B0F44 CRC64;
MGSQSSKAPR GDVTAEEAAG ASPAKVNGQE NGHVKSNGDL SPKGEGESPP VNGTEEAAGA
TGDAIEPAPP SQGAEAKGEV PPKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS
PTEEEQEQGE ISACGEEGTA QEGKAAATPE SQEPQAKGAE ASAAAKGGDT EEAGPQAAEP
STPSGPESDP APASEQNE
