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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)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000008461 – 2Removed in mature formBy similarity2
ChainiPRO_00000008473 – 377Actin, alpha skeletal muscleAdd BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylaspartateBy similarity1
Modified residuei46Methionine (R)-sulfoxide1 Publication1
Modified residuei49Methionine (R)-sulfoxide1 Publication1
Modified residuei63N6-malonyllysineBy similarity1
Modified residuei86N6-methyllysineBy similarity1

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.
PhosphoSitePlusiP68134.
SwissPalmiP68134.

Expressioni

Gene expression databases

BgeeiENSMUSG00000031972.
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 interactors.
IntActiP68134. 24 interactors.
MINTiMINT-149880.
STRINGi10090.ENSMUSP00000034453.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 14Combined sources5
Beta strandi16 – 23Combined sources8
Beta strandi26 – 28Combined sources3
Beta strandi30 – 34Combined sources5
Helixi57 – 62Combined sources6
Turni63 – 66Combined sources4
Beta strandi72 – 74Combined sources3
Helixi81 – 93Combined sources13
Helixi100 – 102Combined sources3
Beta strandi105 – 109Combined sources5
Helixi115 – 127Combined sources13
Beta strandi132 – 138Combined sources7
Helixi139 – 146Combined sources8
Beta strandi150 – 157Combined sources8
Beta strandi162 – 168Combined sources7
Helixi174 – 176Combined sources3
Beta strandi178 – 181Combined sources4
Helixi184 – 197Combined sources14
Helixi205 – 218Combined sources14
Helixi225 – 229Combined sources5
Beta strandi240 – 243Combined sources4
Beta strandi249 – 253Combined sources5
Helixi255 – 264Combined sources10
Helixi266 – 269Combined sources4
Helixi276 – 285Combined sources10
Helixi289 – 291Combined sources3
Helixi292 – 296Combined sources5
Beta strandi299 – 303Combined sources5
Helixi304 – 306Combined sources3
Helixi311 – 322Combined sources12
Helixi337 – 339Combined sources3
Helixi340 – 350Combined sources11
Helixi352 – 354Combined sources3
Turni355 – 357Combined sources3
Beta strandi358 – 360Combined sources3
Helixi361 – 367Combined sources7
Helixi368 – 370Combined sources3
Helixi371 – 375Combined sources5

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68134.
KOiK10354.
OMAiIXMESAG.
OrthoDBiEOG091G08LD.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B1UX-ray2.00B2-377[»]
ProteinModelPortaliP68134.
SMRiP68134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP68134.
PhosphoSitePlusiP68134.
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.
OMAiIXMESAG.
OrthoDBiEOG091G08LD.
PhylomeDBiP68134.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSiActa1. mouse.
PROiP68134.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031972.
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...

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: November 2, 2016
This is version 113 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.