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Protein

Actin, cytoplasmic 2

Gene

Actg1

Organism
Rattus norvegicus (Rat)
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

  • adherens junction organization Source: Reactome
  • response to calcium ion Source: RGD
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-190873. Gap junction degradation.
R-RNO-196025. Formation of annular gap junctions.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-418990. Adherens junctions interactions.
R-RNO-437239. Recycling pathway of L1.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-445095. Interaction between L1 and Ankyrins.
R-RNO-446353. Cell-extracellular matrix interactions.
R-RNO-5626467. RHO GTPases activate IQGAPs.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 2
Alternative name(s):
Gamma-actin
Cleaved into the following chain:
Gene namesi
Name:Actg1
Synonyms:Actg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componentsi: Chromosome 10, Chromosome 3

Organism-specific databases

RGDi1304556. Actg1.

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_0000367102Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 375374Actin, cytoplasmic 2, N-terminally processedPRO_0000000835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processedBy similarity
Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
Modified residuei73 – 731Tele-methylhistidineBy similarity
Modified residuei84 – 841N6-methyllysineBy 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
Monomethylation at Lys-84 (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

PaxDbiP63259.
PRIDEiP63259.

2D gel databases

World-2DPAGE0004:P63259.

PTM databases

iPTMnetiP63259.
PhosphoSiteiP63259.

Expressioni

Gene expression databases

ExpressionAtlasiP63259. baseline.
GenevisibleiP63259. RN.

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

BioGridi252365. 2 interactions.
IntActiP63259. 3 interactions.
MINTiMINT-4578567.
STRINGi10116.ENSRNOP00000044296.

Structurei

3D structure databases

ProteinModelPortaliP63259.
SMRiP63259. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP63259.
KOiK05692.
OrthoDBiEOG72RMZ1.
PhylomeDBiP63259.
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.

P63259-1 [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:July 21, 1986 - v1
Checksum:i54D08F986964EFD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52815 mRNA. Translation: CAA36999.1.
PIRiA38571. ATRTC.
S11222.
RefSeqiNP_001120921.1. NM_001127449.1.
UniGeneiRn.101464.
Rn.106826.

Genome annotation databases

EnsembliENSRNOT00000054976; ENSRNOP00000051859; ENSRNOG00000036701.
ENSRNOT00000079310; ENSRNOP00000072273; ENSRNOG00000053452.
GeneIDi287876.
KEGGirno:287876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52815 mRNA. Translation: CAA36999.1.
PIRiA38571. ATRTC.
S11222.
RefSeqiNP_001120921.1. NM_001127449.1.
UniGeneiRn.101464.
Rn.106826.

3D structure databases

ProteinModelPortaliP63259.
SMRiP63259. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi252365. 2 interactions.
IntActiP63259. 3 interactions.
MINTiMINT-4578567.
STRINGi10116.ENSRNOP00000044296.

PTM databases

iPTMnetiP63259.
PhosphoSiteiP63259.

2D gel databases

World-2DPAGE0004:P63259.

Proteomic databases

PaxDbiP63259.
PRIDEiP63259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000054976; ENSRNOP00000051859; ENSRNOG00000036701.
ENSRNOT00000079310; ENSRNOP00000072273; ENSRNOG00000053452.
GeneIDi287876.
KEGGirno:287876.

Organism-specific databases

CTDi71.
RGDi1304556. Actg1.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP63259.
KOiK05692.
OrthoDBiEOG72RMZ1.
PhylomeDBiP63259.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-RNO-190873. Gap junction degradation.
R-RNO-196025. Formation of annular gap junctions.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-418990. Adherens junctions interactions.
R-RNO-437239. Recycling pathway of L1.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-445095. Interaction between L1 and Ankyrins.
R-RNO-446353. Cell-extracellular matrix interactions.
R-RNO-5626467. RHO GTPases activate IQGAPs.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5663220. RHO GTPases Activate Formins.

Miscellaneous databases

PROiP63259.

Gene expression databases

ExpressionAtlasiP63259. baseline.
GenevisibleiP63259. RN.

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

  1. "A cDNA sequence encoding cytoskeletal gamma-actin from rat."
    Brown C.W., McHugh K.M., Lessard J.L.
    Nucleic Acids Res. 18:5312-5312(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "A microsequencing approach to identify proteins which appear to interact with thyrotropin in rat FRTL-5 thyroid cells."
    Akamizu T., Saji M., Kohn L.D.
    Biochem. Biophys. Res. Commun. 170:351-358(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 4-19 AND 228-231.
  3. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 29-37; 51-62 AND 85-95, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.

Entry informationi

Entry nameiACTG_RAT
AccessioniPrimary (citable) accession number: P63259
Secondary accession number(s): P02571, P14104, P99022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 109 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.