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Protein

Actin, alpha skeletal muscle

Gene

Acta1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Gene namesi
Name:Acta1
Synonyms:Acta
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:87902. Acta1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000846
Chaini3 – 377375Actin, alpha skeletal musclePRO_0000000847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartateBy similarity
Modified residuei46 – 461Methionine (R)-sulfoxide1 Publication
Modified residuei49 – 491Methionine (R)-sulfoxide1 Publication
Modified residuei63 – 631N6-malonyllysineBy similarity
Modified residuei86 – 861N6-methyllysineBy similarity

Post-translational modificationi

Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization.1 Publication
Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation

Proteomic databases

EPDiP68134.
MaxQBiP68134.
PaxDbiP68134.
PeptideAtlasiP68134.
PRIDEiP68134.

PTM databases

iPTMnetiP68134.
PhosphoSiteiP68134.
SwissPalmiP68134.

Expressioni

Gene expression databases

BgeeiP68134.
CleanExiMM_ACTA1.
GenevisibleiP68134. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi197943. 8 interactions.
IntActiP68134. 24 interactions.
MINTiMINT-149880.
STRINGi10090.ENSMUSP00000034453.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145Combined sources
Beta strandi16 – 238Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 345Combined sources
Helixi57 – 626Combined sources
Turni63 – 664Combined sources
Beta strandi72 – 743Combined sources
Helixi81 – 9313Combined sources
Helixi100 – 1023Combined sources
Beta strandi105 – 1095Combined sources
Helixi115 – 12713Combined sources
Beta strandi132 – 1387Combined sources
Helixi139 – 1468Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi162 – 1687Combined sources
Helixi174 – 1763Combined sources
Beta strandi178 – 1814Combined sources
Helixi184 – 19714Combined sources
Helixi205 – 21814Combined sources
Helixi225 – 2295Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi249 – 2535Combined sources
Helixi255 – 26410Combined sources
Helixi266 – 2694Combined sources
Helixi276 – 28510Combined sources
Helixi289 – 2913Combined sources
Helixi292 – 2965Combined sources
Beta strandi299 – 3035Combined sources
Helixi304 – 3063Combined sources
Helixi311 – 32212Combined sources
Helixi337 – 3393Combined sources
Helixi340 – 35011Combined sources
Helixi352 – 3543Combined sources
Turni355 – 3573Combined sources
Beta strandi358 – 3603Combined sources
Helixi361 – 3677Combined sources
Helixi368 – 3703Combined sources
Helixi371 – 3755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B1UX-ray2.00B2-377[»]
ProteinModelPortaliP68134.
SMRiP68134. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68134.
KOiK10354.
OMAiMGSANKT.
OrthoDBiEOG72RMZ1.
PhylomeDBiP68134.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P68134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG
60 70 80 90 100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP
110 120 130 140 150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT
160 170 180 190 200
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY
210 220 230 240 250
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI
260 270 280 290 300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
310 320 330 340 350
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS
360 370
LSTFQQMWIT KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):42,051
Last modified:July 21, 1986 - v1
Checksum:iDF2A3A046346A179
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12866 mRNA. Translation: AAA37164.1.
M12347 Genomic DNA. Translation: AAA37141.1.
BC014877 mRNA. Translation: AAH14877.1.
CCDSiCCDS22764.1.
PIRiA24904.
RefSeqiNP_001258970.1. NM_001272041.1.
NP_033736.1. NM_009606.3.
UniGeneiMm.214950.

Genome annotation databases

EnsembliENSMUST00000034453; ENSMUSP00000034453; ENSMUSG00000031972.
GeneIDi11459.
KEGGimmu:11459.
UCSCiuc009nwr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12866 mRNA. Translation: AAA37164.1.
M12347 Genomic DNA. Translation: AAA37141.1.
BC014877 mRNA. Translation: AAH14877.1.
CCDSiCCDS22764.1.
PIRiA24904.
RefSeqiNP_001258970.1. NM_001272041.1.
NP_033736.1. NM_009606.3.
UniGeneiMm.214950.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B1UX-ray2.00B2-377[»]
ProteinModelPortaliP68134.
SMRiP68134. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197943. 8 interactions.
IntActiP68134. 24 interactions.
MINTiMINT-149880.
STRINGi10090.ENSMUSP00000034453.

PTM databases

iPTMnetiP68134.
PhosphoSiteiP68134.
SwissPalmiP68134.

Proteomic databases

EPDiP68134.
MaxQBiP68134.
PaxDbiP68134.
PeptideAtlasiP68134.
PRIDEiP68134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034453; ENSMUSP00000034453; ENSMUSG00000031972.
GeneIDi11459.
KEGGimmu:11459.
UCSCiuc009nwr.2. mouse.

Organism-specific databases

CTDi58.
MGIiMGI:87902. Acta1.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68134.
KOiK10354.
OMAiMGSANKT.
OrthoDBiEOG72RMZ1.
PhylomeDBiP68134.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSiActa1. mouse.
PROiP68134.
SOURCEiSearch...

Gene expression databases

BgeeiP68134.
CleanExiMM_ACTA1.
GenevisibleiP68134. MM.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
    Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
    Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: OXIDATION AT MET-46 AND MET-49, DEOXIDATION AT MET-46 AND MET-49.

Entry informationi

Entry nameiACTS_MOUSE
AccessioniPrimary (citable) accession number: P68134
Secondary accession number(s): P02568, P99020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.