MRP_RAT
ID MRP_RAT Reviewed; 199 AA.
AC Q9EPH2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=MARCKS-related protein;
DE AltName: Full=Brain protein F52;
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jess U., El Far O., Betz H.;
RT "Rat Mac-MARCKS protein.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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-183 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; AJ301677; CAC18528.1; -; mRNA.
DR EMBL; BC081789; AAH81789.1; -; mRNA.
DR RefSeq; NP_110489.1; NM_030862.2.
DR AlphaFoldDB; Q9EPH2; -.
DR BioGRID; 249517; 1.
DR STRING; 10116.ENSRNOP00000012663; -.
DR iPTMnet; Q9EPH2; -.
DR PhosphoSitePlus; Q9EPH2; -.
DR PaxDb; Q9EPH2; -.
DR PRIDE; Q9EPH2; -.
DR Ensembl; ENSRNOT00000012663; ENSRNOP00000012663; ENSRNOG00000009113.
DR Ensembl; ENSRNOT00000111046; ENSRNOP00000087964; ENSRNOG00000066033.
DR GeneID; 81520; -.
DR KEGG; rno:81520; -.
DR CTD; 65108; -.
DR RGD; 621197; Marcksl1.
DR eggNOG; ENOG502RYXK; Eukaryota.
DR GeneTree; ENSGT00730000111349; -.
DR HOGENOM; CLU_073091_1_0_1; -.
DR InParanoid; Q9EPH2; -.
DR OMA; ANCQENG; -.
DR OrthoDB; 1511774at2759; -.
DR PhylomeDB; Q9EPH2; -.
DR TreeFam; TF332815; -.
DR PRO; PR:Q9EPH2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009113; Expressed in ovary and 18 other tissues.
DR Genevisible; Q9EPH2; RN.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IDA:SynGO.
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:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
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..199
FT /note="MARCKS-related protein"
FT /id="PRO_0000157155"
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 114..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..199
FT /note="Polar residues"
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 132
FT /note="Phosphoserine"
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 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28667"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49006"
FT MOD_RES 183
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 199 AA; 19847 MW; 5107095D4ACD6298 CRC64;
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVKSNGDL TPKGEGESPP VNGADEAAGA
TGDAIEPAPP SQEAEAKGEV APKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS
PTEEEQEQGE ISACSDEGTA QEGKAAATPE SQEPQAKGAE ASAVSKGGDA EEEAGPQAAE
PSTPSGPESG PASASAENE
