P28667 · MRP_MOUSE
- ProteinMARCKS-related protein
- GeneMarcksl1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids200 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the control of cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation (PubMed:22751924).
When unphosphorylated, induces cell migration (PubMed:22751924).
When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration (PubMed:22751924).
May be involved in coupling the protein kinase C and calmodulin signal transduction systems (Probable)
When unphosphorylated, induces cell migration (PubMed:22751924).
When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration (PubMed:22751924).
May be involved in coupling the protein kinase C and calmodulin signal transduction systems (Probable)
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | plasma membrane | |
Cellular Component | presynaptic cytosol | |
Cellular Component | presynaptic membrane | |
Cellular Component | synaptic vesicle | |
Molecular Function | actin filament binding | |
Molecular Function | calmodulin binding | |
Biological Process | actin filament organization | |
Biological Process | cell population proliferation | |
Biological Process | central nervous system development | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | regulation of presynaptic cytosolic calcium ion concentration |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameMARCKS-related protein
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP28667
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Note: Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain (Probable). Association of the effector domain with membranes may be regulated by Ca2+/calmodulin (By similarity).
Colocalizes with F-actin at the leading edge of migrating cells (PubMed:22751924).
Colocalizes with F-actin at the leading edge of migrating cells (PubMed:22751924).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 120 | Complete loss of MAPK-mediated phosphorylation; when associated with A-148 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-148 and A-183. | ||||
Sequence: S → A | ||||||
Mutagenesis | 120 | Induction of F-actin-bundling; when associated with D-148 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-148 and D-183. | ||||
Sequence: S → D | ||||||
Mutagenesis | 148 | Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-183. | ||||
Sequence: T → A | ||||||
Mutagenesis | 148 | Induction of F-actin-bundling; when associated with D-120 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-183. | ||||
Sequence: T → D | ||||||
Mutagenesis | 183 | Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-148. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-148. | ||||
Sequence: T → A | ||||||
Mutagenesis | 183 | Induction of F-actin-bundling; when associated with D-120 and D-148. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-148. | ||||
Sequence: T → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 7 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000157153 | 2-200 | MARCKS-related protein | |||
Sequence: GSQSSKAPRGDVTAEEAAGASPAKANGQENGHVRSNGDLTPKGEGESPPVNGTDEAAGATGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEMSACSDEGTAQEGKAAATPESQEPQAKGAEASAASKEGDTEEEAGPQAAEPSTPSGPESGPTPASAEQNE | ||||||
Modified residue | 14 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 48 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 71 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 85 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 93 | Phosphoserine; by PKC | ||||
Sequence: S | ||||||
Modified residue | 101 | Phosphoserine; by PKC | ||||
Sequence: S | ||||||
Modified residue | 104 | Phosphoserine; by PKC | ||||
Sequence: S | ||||||
Modified residue | 119 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 120 | Phosphoserine; by MAPK8 | ||||
Sequence: S | ||||||
Modified residue | 132 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 135 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 148 | Phosphothreonine; by MAPK8 | ||||
Sequence: T | ||||||
Modified residue | 151 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 162 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 165 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 170 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 183 | Phosphothreonine; by MAPK8 | ||||
Sequence: T | ||||||
Modified residue | 192 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated (PubMed:1618855, PubMed:22751924).
Phosphorylation at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo (PubMed:22751924).
Phosphorylation at Thr-148 is preferentially catalyzed by MAPK8 in vivo, but this modification can also be catalyzed by other kinases in the absence of MAPK8 (PubMed:22751924).
May be phosphorylated by protein kinase C, which disrupts the interaction with calmodulin (PubMed:1618855).
Phosphorylation at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo (PubMed:22751924).
Phosphorylation at Thr-148 is preferentially catalyzed by MAPK8 in vivo, but this modification can also be catalyzed by other kinases in the absence of MAPK8 (PubMed:22751924).
May be phosphorylated by protein kinase C, which disrupts the interaction with calmodulin (PubMed:1618855).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at high levels in brain cortex and hippocampus, including dentate gyrus, anterior olfactory nucleus, primary olfactory cortex, entorhinal cortex, medial preoptic area and dorsomedial hypothalamic nucleus (at protein level) (PubMed:1864362, PubMed:22751924, PubMed:8406449, PubMed:9598313).
Expressed in neuronal cells (at protein level) (PubMed:22751924).
Detected in the retina (PubMed:9598313).
Strongly expressed in testis and uterus; expressed at lower levels in cerebellum, cerebrum, adipose tissue, spleen, kidney, thyroid, liver, lung, skeletal muscle and heart (PubMed:8406449).
Detected in T-cells and B-cells (PubMed:8406449).
Expressed in neuronal cells (at protein level) (PubMed:22751924).
Detected in the retina (PubMed:9598313).
Strongly expressed in testis and uterus; expressed at lower levels in cerebellum, cerebrum, adipose tissue, spleen, kidney, thyroid, liver, lung, skeletal muscle and heart (PubMed:8406449).
Detected in T-cells and B-cells (PubMed:8406449).
Induction
Up-regulated in peritoneal macrophages in response to bacterial lipopolysaccharide (LPS).
Developmental stage
Expressed in the developing neural tube as early as 8.5 dpc. Remains most highly expressed in the developing brain and spinal cord during later development at least until 14.5 dpc. Also detected in the lung, adrenal gland, gut and kidney, particularly the kidney cortex. Undetectable in the liver.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-200 | Disordered | ||||
Sequence: MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVRSNGDLTPKGEGESPPVNGTDEAAGATGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEMSACSDEGTAQEGKAAATPESQEPQAKGAEASAASKEGDTEEEAGPQAAEPSTPSGPESGPTPASAEQNE | ||||||
Region | 87-110 | Effector domain involved in lipid-binding and calmodulin-binding | ||||
Sequence: KKKKKFSFKKPFKLSGLSFKRNRK | ||||||
Compositional bias | 114-135 | Polar residues | ||||
Sequence: GDSSASSPTEEEQEQGEMSACS | ||||||
Compositional bias | 182-200 | Polar residues | ||||
Sequence: STPSGPESGPTPASAEQNE |
Sequence similarities
Belongs to the MARCKS family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length200
- Mass (Da)20,165
- Last updated2007-01-23 v2
- ChecksumAA50A0E2029921AF
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 114-135 | Polar residues | ||||
Sequence: GDSSASSPTEEEQEQGEMSACS | ||||||
Sequence conflict | 134 | in Ref. 5; AAH06757 | ||||
Sequence: C → S | ||||||
Compositional bias | 182-200 | Polar residues | ||||
Sequence: STPSGPESGPTPASAEQNE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X61399 EMBL· GenBank· DDBJ | CAA43671.1 EMBL· GenBank· DDBJ | mRNA | ||
S65597 EMBL· GenBank· DDBJ | AAP13962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK079390 EMBL· GenBank· DDBJ | BAC37630.1 EMBL· GenBank· DDBJ | mRNA | ||
AK083913 EMBL· GenBank· DDBJ | BAC39058.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152990 EMBL· GenBank· DDBJ | BAE31636.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169355 EMBL· GenBank· DDBJ | BAE41104.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006757 EMBL· GenBank· DDBJ | AAH06757.1 EMBL· GenBank· DDBJ | mRNA |