Actin, alpha skeletal muscle precursor

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P68134 (ACTS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Actin, alpha skeletal muscle

Alternative name(s):
Alpha-actin-1

Gene names

Name:	Acta1
Synonyms:	Acta

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Interacts (via its C-terminus) with USP25; the interaction occurs for all USP25 isoforms but is strongest for isoform USP25m in muscle differentiating cells By similarity. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X By similarity.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced 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
Molecular function	Muscle protein
PTM	Acetylation Methylation Oxidation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell growth Inferred from electronic annotation. Source: Compara response to extracellular stimulus Inferred from electronic annotation. Source: Compara response to lithium ion Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara skeletal muscle fiber adaptation Inferred from electronic annotation. Source: Compara skeletal muscle fiber development Inferred from direct assay PubMed 2731651. Source: UniProtKB skeletal muscle thin filament assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	actin filament Inferred from sequence or structural similarity. Source: UniProtKB stress fiber Inferred from sequence or structural similarity. Source: UniProtKB striated muscle thin filament Traceable author statement PubMed 2731651. 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

Removed in mature form By similarity

PRO_0000000846

Chain

3 – 377

375

Actin, alpha skeletal muscle

PRO_0000000847

Amino acid modifications

Modified residue

N-acetylaspartate By similarity

Modified residue

Methionine sulfoxide By similarity

Modified residue

Phosphotyrosine Ref.5

Modified residue

N6-malonyllysine By similarity

Modified residue

Tele-methylhistidine By similarity

Modified residue

Phosphotyrosine Ref.4 Ref.5

Modified residue

242

Phosphotyrosine Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P68134 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DF2A3A046346A179
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FASTA

377

42,051

        10         20         30         40         50         60 
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA 

        70         80         90        100        110        120 
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK 

       130        140        150        160        170        180 
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL 

       190        200        210        220        230        240 
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK 

       250        260        270        280        290        300 
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 

       310        320        330        340        350        360 
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT 

       370 
KQEYDEAGPS IVHRKCF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of cDNA clones from mouse skeletal muscle actin mRNA." Leader D.P., Gall I., Campbell P.C., Frischauf A.-M. DNA 5:235-238(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The complete sequence of the mouse skeletal alpha-actin gene reveals several conserved and inverted repeat sequences outside of the protein-coding region." Hu M.C.-T., Sharp S.B., Davidson N. Mol. Cell. Biol. 6:15-25(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[4]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-93, MASS SPECTROMETRY. Tissue: Mast cell.
[5]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55; TYR-93 AND TYR-242, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12866 mRNA. Translation: AAA37164.1. M12347 Genomic DNA. Translation: AAA37141.1. BC014877 mRNA. Translation: AAH14877.1.
IPI	IPI00110827.
PIR	A24904.
RefSeq	NP_001258970.1. NM_001272041.1. NP_033736.1. NM_009606.3.
UniGene	Mm.214950.
3D structure databases
ProteinModelPortal	P68134.
ModBase	Search...
Protein-protein interaction databases
IntAct	P68134. 21 interactions.
PTM databases
PhosphoSite	P68134.
Proteomic databases
PRIDE	P68134.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034453; ENSMUSP00000034453; ENSMUSG00000031972.
GeneID	11459.
KEGG	mmu:11459.
Organism-specific databases
CTD	58.
MGI	MGI:87902. Acta1.
Phylogenomic databases
GeneTree	ENSGT00690000101919.
HOGENOM	HOG000233340.
HOVERGEN	HBG003771.
InParanoid	P68134.
KO	K10354.
OMA	FEEEMAT.
OrthoDB	EOG4W9J40.
Gene expression databases
Bgee	P68134.
CleanEx	MM_ACTA1.
Genevestigator	P68134.
GermOnline	ENSMUSG00000031972. Mus musculus.
Family and domain databases
InterPro	IPR004000. Actin-related. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. PTHR11937. 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...
Other
NextBio	278780.
SOURCE	Search...

Entry information

Entry name

ACTS_MOUSE

Accession

Primary (citable) accession number: P68134
Secondary accession number(s): P02568, P99020

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents