P68137 (ACTS_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Actin, alpha skeletal muscle Alternative name(s): Alpha-actin-1 | ||||
| Gene names |
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| Organism | Sus scrofa (Pig) [Complete proteome] | ||||
| Taxonomic identifier | 9823 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
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. Interacts (via its C-terminus) with USP25 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 | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | skeletal muscle fiber development Inferred from sequence or structural similarity. Source: UniProtKB skeletal muscle thin filament assemblyInferred 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 |
| 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 By similarity | PRO_0000000848 | |||||
| Chain | 3 – 377 | 375 | Actin, alpha skeletal muscle | PRO_0000000849 | |||||
Amino acid modifications | |||||||||
| Modified residue | 3 | 1 | N-acetylaspartate By similarity | ||||||
| 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 By similarity | ||||||
| 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 | ||||||
Sequences
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References
| [1] | "Structure and regulation of the porcine skeletal alpha-actin-encoding gene." Reecy J.M., Bidwell C.A., Briley G.P., Grant A.L. Gene 180:23-28(1996) [PubMed: 8973342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U16368 Genomic DNA. Translation: AAC48692.1. |
| PIR | JC5301. |
| RefSeq | NP_001161267.1. NM_001167795.1. |
| UniGene | Ssc.37707. |
3D structure databases | |
| ProteinModelPortal | P68137. |
| SMR | P68137. Positions 6-377. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P68137. |
Proteomic databases | |
| PRIDE | P68137. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSSSCT00000011156; ENSSSCP00000010867; ENSSSCG00000010190. |
| GeneID | 100154254. |
| KEGG | ssc:100154254. |
Organism-specific databases | |
| CTD | 58. |
Phylogenomic databases | |
| GeneTree | ENSGT00590000082732. |
| HOVERGEN | HBG003771. |
| OMA | IXMESAG. |
| OrthoDB | EOG4W9J40. |
Family and domain databases | |
| InterPro | IPR004000. Actin-like. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view] |
| KO | K10354. |
| 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_PIG | ||||||||
| Accession | Primary (citable) accession number: P68137 Secondary accession number(s): P02568, P99020 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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