| General information | | DisProt: | DP00253 | | Name: | Myristoylated alanine-rich C-kinase substrate | | Synonym(s): | MARCS_MOUSE
MARCKS
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P26645 | | UniGene: | Mm.477725 | | SwissProt: | MARCS_MOUSE | | TrEMBL: | | | NCBI (GI): | 126752 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 309 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MGAQFSKTAA KGEATAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA EPGAKEELQA - 60
NGSAPAADKE EPASGSAATP AAAEKDEAAA ATEPGAGAAD KEAAEAEPAE PSSPAAEAEG - 120
ASASSTSSPK AEDGAAPSPS SETPKKKKKR FSFKKSFKLS GFSFKKSKKE SGEGAEAEGA - 180
TAEGAKDEAA AAAGGEGAAA PGEQAGGAGA EGAAGGEPRE AEAAEPEQPE QPEQPAAEEP - 240
QAEEQSEAAG EKAEEPAPGA TAGDASSAAG PEQEAPAATD EAAASAAPAA SPEPQPECSP - 300
EAPPAPTAE
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| Functional narrative |
Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
Subcellular location: Cytoplasm › cytoskeleton Probable. Membrane; Lipid-anchor. By similarity.
Tissue specificity: Brain, spleen, less in kidney and heart, and very low levels in liver.
Induction by lipopolysaccharides (LPS).
Post-translational modification : Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Sequence similarities: Belongs to the MARCKS family.
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UniProt
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 309 | | Length: | 309 | | Region sequence: |
MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQA
NGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEG
ASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGA
TAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEP
QAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSP
EAPPAPTAE | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | | | Functional subclasses: | Phosphorylation
Substrate/ligand binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; CaCl2 0.5 mM; NaCl 0.1 M; protein 1 uM; Tris-HCl (buffer (pH 7.5)) 20 mM)
| References:
- Matsubara M, Yamauchi E, Hayashi N, Taniguchi H. "MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin." FEBS Lett. 1998; 421(3): 203-7. PubMed: 9468306
- Tapp H, Al-Naggar IM, Yarmola EG, Harrison A, Shaw G, Edison AS, Bubb MR. "MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions." J Biol Chem. 2005; 280(11): 9946-56. PubMed: 15640140
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 1 - 309 | | Length: | 309 | | Region sequence: |
MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQA
NGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEG
ASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGA
TAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEP
QAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSP
EAPPAPTAE | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | | | Functional subclasses: | Phosphorylation
Substrate/ligand binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; CaCl2 0.5 mM; calmodulin 1 uM; NaCl 0.1 M; protein 1 uM; Tris-HCl (buffer (pH 7.5)) 20 mM)
| References:
- Matsubara M, Yamauchi E, Hayashi N, Taniguchi H. "MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin." FEBS Lett. 1998; 421(3): 203-7. PubMed: 9468306
- Tapp H, Al-Naggar IM, Yarmola EG, Harrison A, Shaw G, Edison AS, Bubb MR. "MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions." J Biol Chem. 2005; 280(11): 9946-56. PubMed: 15640140
| Comments:This protein was found to be disordered while in a complex with calmodulin.
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| References |
- Arbuzova A, Schmitz AA, Vergères G. "Cross-talk unfolded: MARCKS proteins." Biochem J. 2002; 362(Pt 1): 1-12. PubMed: 11829734
- Seykora JT, Ravetch JV, Aderem A. "Cloning and molecular characterization of the murine macrophage "68-kDa" protein kinase C substrate and its regulation by bacterial lipopolysaccharide." Proc Natl Acad Sci U S A. 1991; 88(6): 2505-9. PubMed: 2006186
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