| Tag |
Content |
LipidDB ID |
LipidDB-10090-00816 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
4.6 |
Molecular Weight |
20165.43 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
MARCKS-related protein |
Protein Synonyms/Alias |
Brain protein F52; MARCKS-like protein 1; Macrophage myristoylated alanine-rich C kinase substrate; Mac-MARCKS; MacMARCKS; |
Gene Name |
Marcksl1 |
Gene Synonyms/Alias |
Mlp; Mrp; |
Created Date |
01-DEC-1992 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGSQSSKAP | [1] | N-Myristoylation |
|
Organism |
Mus musculus (Mouse) |
NCBI Taxa ID |
10090 |
Reference |
[1] Bähr G, Diederich A, Vergères G, Winterhalter M. Interaction of the effectordomain of MARCKS and MARCKS-related protein with lipid membranes revealed byelectric potential measurements. Biochemistry. 1998 Nov 17;37(46):16252-61.[ PMID:9819217]
|
Functional Description |
Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May also affect cancer cell migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems. |
Sequence Annotation |
Region: 87 110 Effector domain involved in lipid-binding. Region: 87 100 Calmodulin-binding (PSD). Modified residue: 22 22 Phosphoserine. Modified residue: 36 36 Phosphoserine. Modified residue: 48 48 Phosphoserine. Modified residue: 71 71 Phosphoserine. Modified residue: 85 85 Phosphothreonine. Modified residue: 93 93 Phosphoserine; by PKC. Modified residue: 101 101 Phosphoserine; by PKC. Modified residue: 104 104 Phosphoserine; by PKC. Modified residue: 120 120 Phosphoserine; by MAPK8. Modified residue: 135 135 Phosphoserine. Modified residue: 148 148 Phosphothreonine; by MAPK8. Modified residue: 151 151 Phosphoserine. Modified residue: 162 162 Phosphoserine. Modified residue: 165 165 Phosphoserine. Modified residue: 170 170 Phosphothreonine. Modified residue: 183 183 Phosphothreonine; by MAPK8. Modified residue: 192 192 Phosphothreonine.
|
Protein Length |
200 AA. |
Protein Sequence (Canonical) |
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVRSNGDL TPKGEGESPP VNGTDEAAGA 60
TGDAIEPAPP SQEAEAKGEV APKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS 120
PTEEEQEQGE MSACSDEGTA QEGKAAATPE SQEPQAKGAE ASAASKEGDT EEEAGPQAAE 180
PSTPSGPESG PTPASAEQNE 200
|
FASTA (Canonical) |
>LipidDB-10090-00816|P28667
MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVRSNGDLTPKGEGESPPVNGTDEAAGA
TGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASS
PTEEEQEQGEMSACSDEGTAQEGKAAATPESQEPQAKGAEASAASKEGDTEEEAGPQAAE
PSTPSGPESGPTPASAEQNE
|
Gene Ontology |
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl GO:0005886; C:plasma membrane; IEA:UniProtKB-KW GO:0008284; P:positive regulation of cell proliferation; IDA:MGI |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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