| IED ID | IndEnz0002005044 |
| Enzyme Type ID | protease005044 |
| Protein Name |
Actin, alpha skeletal muscle Alpha-actin-1 Cleaved into: Actin, alpha skeletal muscle, intermediate form |
| Gene Name | ACTA1 ACTA |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF |
| Enzyme Length | 377 |
| Uniprot Accession Number | P68133 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Cross-link (2); Initiator methionine (1); Modified residue (6); Natural variant (84); Region (2) |
| Keywords | 3D-structure;ATP-binding;Acetylation;Cytoplasm;Cytoskeleton;Disease variant;Isopeptide bond;Methylation;Muscle protein;Nemaline myopathy;Nucleotide-binding;Oxidation;Reference proteome |
| Interact With | Q6XD76; Q9UQM7; Q0VD86; Q6ZQX7-4; Q96PV4; Q9H7C4; P17024 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. |
| Modified Residue | MOD_RES 2; /note=N-acetylcysteine; in intermediate form; /evidence=ECO:0000250|UniProtKB:P62737; MOD_RES 46; /note=Methionine (R)-sulfoxide; /evidence=ECO:0000250|UniProtKB:P68134; MOD_RES 49; /note=Methionine (R)-sulfoxide; /evidence=ECO:0000250|UniProtKB:P68134; MOD_RES 63; /note=N6-malonyllysine; /evidence=ECO:0000269|PubMed:21908771; MOD_RES 75; /note=Tele-methylhistidine; /evidence=ECO:0000269|PubMed:30626964; MOD_RES 86; /note=N6-methyllysine; /evidence=ECO:0000269|PubMed:23673617 |
| Post Translational Modification | PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. {ECO:0000250|UniProtKB:P68134}.; PTM: Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000269|PubMed:23673617}.; PTM: Methylated at His-75 by SETD3. {ECO:0000269|PubMed:30626964}.; PTM: (Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-52 of one monomer and Glu-272 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148). {ECO:0000305|PubMed:19015515, ECO:0000305|PubMed:26228148}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 7RNS; 7RNU; 7RNV; |
| Mapped Pubmed ID | 10747208; 10854330; 11702052; 12048248; 12210873; 12721663; 14684598; 15072110; 15660133; 15679046; 16945536; 17065230; 17266347; 17620599; 18063690; 18157088; 18461503; 18976909; 19002257; 19150851; 19383239; 19389844; 19562689; 19634497; 19635823; 19819966; 19934221; 19948975; 20100475; 20179953; 20201926; 20332100; 20378355; 20388088; 20391533; 20452215; 20630939; 20686692; 20716950; 20718862; 20809254; 20826790; 21079800; 21080425; 21108927; 21340023; 21514153; 21691712; 21824169; 21874239; 21912905; 21931536; 21975552; 21994736; 22031939; 22081313; 22209233; 23042265; 23071671; 23176180; 23247112; 23376163; 23414517; 23420843; 23656990; 23831272; 2395459; 24255178; 24313005; 24502978; 24576301; 24725412; 25182138; 25746564; 25747004; 25895516; 25913210; 26172852; 26295568; 26493222; 27074222; 27112274; 28337446; 28341124; 28416349; 28712119; 28780987; 30354303; 30517146; 30732915; 30937621; 32222963; 32414151; 32751693; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,051 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |