Reviewed,
UniProtKB/Swiss-Prot P68138 (ACTS_BOVIN)
Last modified
November 24, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Actin, alpha skeletal muscle Alternative name(s): Alpha-actin-1 | ||||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
| Subunit structure | Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Interacts with TTID By similarity. |
| Subcellular location | |
| Miscellaneous | In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. |
| Sequence similarities | Belongs to the actin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Muscle protein |
| PTM | Acetylation Methylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | muscle thin filament assembly Inferred from sequence or structural similarity. Source: UniProtKB skeletal muscle fiber developmentInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | actin filament Inferred from sequence or structural similarity. Source: UniProtKB stress fiberInferred from sequence or structural similarity. Source: UniProtKB striated muscle thin filamentInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 2 | 2 | Removed in mature form | PRO_0000000842 | |||||
| Chain | 3 – 377 | 375 | Actin, alpha skeletal muscle | PRO_0000000843 | |||||
Amino acid modifications | |||||||||
| Modified residue | 3 | 1 | N-acetylaspartate | ||||||
| Modified residue | 55 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 63 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 70 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 75 | 1 | Tele-methylhistidine | ||||||
| Modified residue | 93 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 193 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 242 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 328 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 330 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 349 | 1 | A → R in AAA82873. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The nucleotide sequence, structure, and preliminary studies on the transcriptional regulation of the bovine alpha skeletal actin gene." Davey H.W., Kelly J.K., Wildeman A.G. DNA Cell Biol. 14:609-618(1995) [PubMed: 7626220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum. |
| [3] | "The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation." Vandekerckhove J., Weber K. Differentiation 14:123-133(1979) [PubMed: 499690] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-377. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U02285 Genomic DNA. Translation: AAA82873.1. BC102376 mRNA. Translation: AAI02377.1. | |
| IPI | IPI00697648. |
| RefSeq | NP_776650.1. |
| UniGene | Bt.88733 |
3D structure databases | |
| SMR | P68138. Positions 6-373. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P68138. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000006534; ENSBTAP00000006534; ENSBTAG00000004965; Bos taurus. [Genome view] |
| GeneID | 281592. |
| KEGG | bta:281592. |
Organism-specific databases | |
| CTD | 281592. |
Phylogenomic databases | |
| HOVERGEN | P68138. |
| OMA | FVGMESA |
Family and domain databases | |
| InterPro | IPR004000. Actin-like. IPR004001. Actin_CS. [Graphical view] |
| PANTHER | PTHR11937. Actin_like. 1 hit. |
| Pfam | PF00022. Actin. 1 hit. [Graphical view] |
| PRINTS | PR00190. ACTIN. |
| SMART | SM00268. ACTIN. 1 hit. [Graphical view] |
| PROSITE | PS00406. ACTINS_1. 1 hit. PS00432. ACTINS_2. 1 hit. PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACTS_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P68138 Secondary accession number(s): P02568, P99020, Q3ZCG3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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