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Protein

Actin, cytoplasmic 2

Gene

ACTG1

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

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-GGA-190873. Gap junction degradation.
R-GGA-196025. Formation of annular gap junctions.
R-GGA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-GGA-3928662. EPHB-mediated forward signaling.
R-GGA-3928665. EPH-ephrin mediated repulsion of cells.
R-GGA-4420097. VEGFA-VEGFR2 Pathway.
R-GGA-5626467. RHO GTPases activate IQGAPs.
R-GGA-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 2
Alternative name(s):
Gamma-actin
Cleaved into the following chain:
Gene namesi
Name:ACTG1
ORF Names:RCJMB04_1h13
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 2PRO_0000367105Add
BLAST
Initiator methionineiRemoved; alternate1 Publication
Chaini2 – 375374Actin, cytoplasmic 2, N-terminally processedPRO_0000280766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in Actin, cytoplasmic 2; alternateBy similarity
Modified residuei2 – 21N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed1 Publication
Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
Modified residuei73 – 731Tele-methylhistidineBy similarity

Post-translational modificationi

Oxidation of Met-44 and Met-47 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

PaxDbiQ5ZMQ2.
PRIDEiQ5ZMQ2.

Expressioni

Gene expression databases

ExpressionAtlasiQ5ZMQ2. baseline.

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.

Protein-protein interaction databases

IntActiQ5ZMQ2. 1 interaction.
STRINGi9031.ENSGALP00000039176.

Structurei

3D structure databases

ProteinModelPortaliQ5ZMQ2.
SMRiQ5ZMQ2. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiQ5ZMQ2.
KOiK05692.
OMAiTFQQART.

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.

Q5ZMQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,793
Last modified:November 23, 2004 - v1
Checksum:i54D08F986964EFD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ719332 mRNA. Translation: CAG30991.1.
RefSeqiNP_001295542.1. NM_001308613.1.
XP_015135388.1. XM_015279902.1.
UniGeneiGga.43416.
Gga.4520.

Genome annotation databases

EnsembliENSGALT00000045981; ENSGALP00000042680; ENSGALG00000028749.
GeneIDi776816.
KEGGigga:776816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ719332 mRNA. Translation: CAG30991.1.
RefSeqiNP_001295542.1. NM_001308613.1.
XP_015135388.1. XM_015279902.1.
UniGeneiGga.43416.
Gga.4520.

3D structure databases

ProteinModelPortaliQ5ZMQ2.
SMRiQ5ZMQ2. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5ZMQ2. 1 interaction.
STRINGi9031.ENSGALP00000039176.

Proteomic databases

PaxDbiQ5ZMQ2.
PRIDEiQ5ZMQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000045981; ENSGALP00000042680; ENSGALG00000028749.
GeneIDi776816.
KEGGigga:776816.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiQ5ZMQ2.
KOiK05692.
OMAiTFQQART.

Enzyme and pathway databases

ReactomeiR-GGA-190873. Gap junction degradation.
R-GGA-196025. Formation of annular gap junctions.
R-GGA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-GGA-3928662. EPHB-mediated forward signaling.
R-GGA-3928665. EPH-ephrin mediated repulsion of cells.
R-GGA-4420097. VEGFA-VEGFR2 Pathway.
R-GGA-5626467. RHO GTPases activate IQGAPs.
R-GGA-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

PROiQ5ZMQ2.

Gene expression databases

ExpressionAtlasiQ5ZMQ2. baseline.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: CB.
    Tissue: Bursa of Fabricius.
  2. Bienvenut W.V., Black E.J., Gillespie D.A.
    Submitted (JAN-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-37; 85-113; 178-191; 197-206; 239-254; 291-326 AND 360-372, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.

Entry informationi

Entry nameiACTG_CHICK
AccessioniPrimary (citable) accession number: Q5ZMQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: November 23, 2004
Last modified: June 8, 2016
This is version 85 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.