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Protein

Actin, alpha skeletal muscle

Gene

ACTA1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 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

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Gene namesi
Name:ACTA1
Synonyms:ACTA
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 3

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 form1 PublicationPRO_0000000854
Chaini3 – 377375Actin, alpha skeletal musclePRO_0000000855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartate1 Publication
Modified residuei46 – 461Methionine (R)-sulfoxideBy similarity
Modified residuei49 – 491Methionine (R)-sulfoxideBy similarity
Modified residuei75 – 751Tele-methylhistidineBy 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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation

Proteomic databases

PaxDbiP68139.
PRIDEiP68139.

Expressioni

Gene expression databases

BgeeiENSGALG00000011086.

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.1 Publication

Protein-protein interaction databases

BioGridi682339. 4 interactions.
DIPiDIP-41824N.
IntActiP68139. 2 interactions.
MINTiMINT-152140.
STRINGi9031.ENSGALP00000015988.

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 strandi30 – 345Combined sources
Beta strandi37 – 404Combined sources
Helixi57 – 626Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 704Combined sources
Beta strandi72 – 743Combined sources
Helixi81 – 9313Combined sources
Turni94 – 963Combined 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
Helixi208 – 21811Combined sources
Helixi225 – 23410Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi249 – 2535Combined sources
Helixi255 – 2617Combined sources
Turni262 – 2643Combined sources
Helixi266 – 2694Combined sources
Helixi276 – 2849Combined sources
Helixi289 – 2913Combined sources
Helixi292 – 2965Combined sources
Beta strandi299 – 3035Combined sources
Helixi304 – 3063Combined sources
Helixi311 – 32212Combined sources
Turni335 – 3384Combined sources
Helixi340 – 35011Combined sources
Helixi352 – 3576Combined sources
Beta strandi358 – 3603Combined sources
Helixi361 – 3677Combined sources
Helixi369 – 3724Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDUX-ray2.20B/E1-377[»]
ProteinModelPortaliP68139.
SMRiP68139. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68139.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP68139.
KOiK10354.
OMAiIXMESAG.
OrthoDBiEOG091G08LD.

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.

P68139-1 [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
V01507 Genomic DNA. Translation: CAA24753.1.
PIRiA93432. ATCH.
RefSeqiNP_001026234.1. NM_001031063.1.
UniGeneiGga.5962.

Genome annotation databases

EnsembliENSGALT00000018064; ENSGALP00000018042; ENSGALG00000011086.
GeneIDi421534.
KEGGigga:421534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01507 Genomic DNA. Translation: CAA24753.1.
PIRiA93432. ATCH.
RefSeqiNP_001026234.1. NM_001031063.1.
UniGeneiGga.5962.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDUX-ray2.20B/E1-377[»]
ProteinModelPortaliP68139.
SMRiP68139. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi682339. 4 interactions.
DIPiDIP-41824N.
IntActiP68139. 2 interactions.
MINTiMINT-152140.
STRINGi9031.ENSGALP00000015988.

Proteomic databases

PaxDbiP68139.
PRIDEiP68139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000018064; ENSGALP00000018042; ENSGALG00000011086.
GeneIDi421534.
KEGGigga:421534.

Organism-specific databases

CTDi58.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP68139.
KOiK10354.
OMAiIXMESAG.
OrthoDBiEOG091G08LD.

Miscellaneous databases

EvolutionaryTraceiP68139.
PROiP68139.

Gene expression databases

BgeeiENSGALG00000011086.

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_CHICK
AccessioniPrimary (citable) accession number: P68139
Secondary accession number(s): P02568, P99020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 7, 2016
This is version 99 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.