Reviewed,
UniProtKB/Swiss-Prot P60708 (ACTB_HORSE)
Last modified
December 15, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Actin, cytoplasmic 1 Alternative name(s): Beta-actin Cleaved into the following chain: 1- Recommended name: Actin, cytoplasmic 1, N-terminally processed | ||
| Gene names |
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| Organism | Equus caballus (Horse) | ||
| Taxonomic identifier | 9796 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus |
Protein attributes
| Sequence length | 375 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript 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. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD By similarity. |
| Subcellular location | Cytoplasm › cytoskeleton. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs By similarity. |
| 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 |
| PTM | Acetylation Methylation Phosphoprotein |
| Gene Ontology (GO) | |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 375 | 375 | Actin, cytoplasmic 1 | PRO_0000367072 | |||||
| Initiator methionine | 1 | 1 | Removed; alternate By similarity | ||||||
| Chain | 2 – 375 | 374 | Actin, cytoplasmic 1, N-terminally processed | PRO_0000000769 | |||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine; in Actin, cytoplasmic 1; alternate By similarity | ||||||
| Modified residue | 2 | 1 | N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed By similarity | ||||||
| Modified residue | 53 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 73 | 1 | Tele-methylhistidine By similarity | ||||||
| Modified residue | 91 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 166 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 169 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 198 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 218 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 294 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 318 | 1 | Phosphothreonine By similarity | ||||||
Sequences
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References
| [1] | "Equine beta actin." Swiderski C.E., Horohov D.W. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF035774 mRNA. Translation: AAB88212.1. | |
| RefSeq | NP_001075307.1. |
| UniGene | Eca.15483 |
3D structure databases | |
| SMR | P60708. Positions 4-371. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P60708. |
Genome annotation databases | |
| Ensembl | ENSECAT00000019685; ENSECAP00000016124; ENSECAG00000018600; Equus caballus. [Genome view] |
| GeneID | 100033878. |
| KEGG | ecb:100033878. |
Phylogenomic databases | |
| HOVERGEN | P60708. |
| InParanoid | P60708. |
| OrthoDB | EOG944P4G. |
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 | ACTB_HORSE | ||||||||
| Accession | Primary (citable) accession number: P60708 Secondary accession number(s): P02570 Q64316 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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