Reviewed, UniProtKB/Swiss-Prot P68134 (ACTS_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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	Cytoplasm › cytoskeleton.
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
Gene Ontology (GO)
Biological process	muscle thin filament assembly Inferred from sequence or structural similarity. Source: UniProtKB skeletal muscle fiber development Inferred from direct assay. 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. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred 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 By similarity		PRO_0000000846
	Chain	3 – 377	375	Actin, alpha skeletal muscle		PRO_0000000847
Amino acid modifications
	Modified residue	3	1	N-acetylaspartate By similarity
	Modified residue	55	1	Phosphotyrosine Ref.5 Ref.6
	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 Ref.6 Ref.4
	Modified residue	193	1	N6-acetyllysine By similarity
	Modified residue	242	1	Phosphotyrosine Ref.6
	Modified residue	328	1	N6-acetyllysine By similarity
	Modified residue	330	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P68134-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: DF2A3A046346A179	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

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: 3013550] [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: 3023820] [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: 15489334] [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: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-93, MASS SPECTROMETRY. Tissue: Mast cell.
[5]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, MASS SPECTROMETRY.
[6]	"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: 18034455] [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
EMBLGenBankDDBJ	M12866 mRNA. Translation: AAA37164.1. M12347 Genomic DNA. Translation: AAA37141.1. BC014877 mRNA. Translation: AAH14877.1.
IPI	IPI00110827.
PIR	A24904.
RefSeq	NP_033736.1.
UniGene	Mm.214950
3D structure databases
SMR	P68134. Positions 6-373.
ModBase	Search...
Protein-protein interaction databases
STRING	P68134.
PTM databases
PhosphoSite	P68134.
Proteomic databases
PRIDE	P68134.
Genome annotation databases
Ensembl	ENSMUST00000034453; ENSMUSP00000034453; ENSMUSG00000031972; Mus musculus. [Genome view]
GeneID	11459.
KEGG	mmu:11459.
UCSC	uc009nwr.1. mouse.
Organism-specific databases
CTD	11459.
MGI	MGI:87902. Acta1.
Phylogenomic databases
HOGENOM	P68134.
HOVERGEN	P68134.
OMA	FVGMESA
Gene expression databases
ArrayExpress	P68134.
Bgee	P68134.
CleanEx	MM_ACTA1.
Genevestigator	P68134.
GermOnline	ENSMUSG00000031972. Mus musculus.
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...
Other Resources
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:	November 24, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)