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ACTG2 actin gamma 2, smooth muscle [ Homo sapiens (human) ]

Gene ID: 72, updated on 11-Jan-2019

Summary

Official Symbol
ACTG2provided by HGNC
Official Full Name
actin gamma 2, smooth muscleprovided by HGNC
Primary source
HGNC:HGNC:145
See related
Ensembl:ENSG00000163017 MIM:102545
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
ACT; ACTE; VSCM; ACTA3; ACTL3; ACTSG
Summary
Actins are highly conserved proteins that are involved in various types of cell motility and in the maintenance of the cytoskeleton. Three types of actins, alpha, beta and gamma, have been identified in vertebrates. Alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. This gene encodes actin gamma 2; a smooth muscle actin found in enteric tissues. Alternative splicing results in multiple transcript variants encoding distinct isoforms. Based on similarity to peptide cleavage of related actins, the mature protein of this gene is formed by removal of two N-terminal peptides.[provided by RefSeq, Dec 2010]
Expression
Biased expression in prostate (RPKM 1093.2), urinary bladder (RPKM 1063.1) and 7 other tissues See more
Orthologs

Genomic context

See ACTG2 in Genome Data Viewer
Location:
2p13.1
Exon count:
9
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 2 NC_000002.12 (73892966..73919653)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 2 NC_000002.11 (74120093..74146780)

Chromosome 2 - NC_000002.12Genomic Context describing neighboring genes Neighboring gene STAM binding protein Neighboring gene uncharacterized LOC112268419 Neighboring gene zinc finger DHHC-type containing 6 pseudogene Neighboring gene deoxyguanosine kinase Neighboring gene DGUOK antisense RNA 1 Neighboring gene RNA, 5S ribosomal pseudogene 97

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

HIV-1 interactions

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env Gelsolin overexpression impairs HIV-1 gp120-induced cortical F-actin reorganization and capping and gp120-mediated CD4-CCR5 and CD4-CXCR4 redistribution in permissive lymphocytes PubMed
env The N-terminal leucine-rich repeat fragment of Slit2 inhibits HIV-1 gp120-induced actin polymerization in T cells PubMed
env HIV-1 gp120-CXCR4 signaling triggers cofilin activation and actin reorganization, which are important for a post entry process leading to viral nuclear localization PubMed
env Syntenin-1 is recruited toward HIV-1 gp120/gp41-driven virus/cell and cell/cell contacts, associates with CD4, limits HIV-1-induced cell fusion and viral entry, and modulates gp120/gp41-triggered actin polymerization and PIP2 accumulation PubMed
env Inducible T-cell kinase (ITK) affects viral entry and gp120-induced actin reorganization PubMed
Envelope surface glycoprotein gp160, precursor env Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 PubMed
Envelope transmembrane glycoprotein gp41 env Syntenin-1 is recruited toward HIV-1 gp120/gp41-driven virus/cell and cell/cell contacts, associates with CD4, limits HIV-1-induced cell fusion and viral entry, and modulates gp120/gp41-triggered actin polymerization and PIP2 accumulation PubMed
env The interaction of the long cytoplasmic tail of HIV-1 gp41 with the carboxy-terminal regulatory domain of p115-RhoGEF inhibits p115-mediated actin stress fiber formation and activation of serum response factor (SRF) PubMed
Nef nef HIV-1 Nef inhibits CXCL12 induced chemotaxis in Jurkat cells, monocytes, and PBMCs, which leads to marked downregulation of F-actin accumulation in cells PubMed
nef HIV-1 Nef induces loss of F-actin assembly and inhibits retinoid receptor-mediated transcription PubMed
nef HIV-1 Nef requires a PAK2 recruitment motif (F195/191I) for inhibition of actin remodeling and induction of cofilin hyperphosphorylation PubMed
Pr55(Gag) gag Tec kinase chemical inhibitors diminish the recruitment of ITK to the plasma membrane perturbing HIV-1 Gag-ITK co-localization, disrupting F-actin polymerization, and inhibiting HIV-1 release and replication PubMed
gag HIV-1 Gag, ITK, and F-actin are located in overlapping and discrete regions of T cell-T cell contact sites PubMed
gag Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 PubMed
gag HIV-1 Gag assembly and budding occur through an actin-driven mechanism PubMed
Tat tat Microarray analysis indicates HIV-1 Tat-induced upregulation of actin, gamma 2 (ACTG2) in primary human brain microvascular endothelial cells PubMed
tat Treatment with cannabinoids inhibits HIV-1 Tat-enhanced attachment of U937 cells to collagen IV, laminin, or ECM1 proteins, which is linked to the cannabinoid receptor type 2 and the modulation of beta1-integrin and actin distribution PubMed
tat Treatment of primary hippocampal neurons with HIV-1 Tat produces a significant early reduction in F-actin labeled puncta. The cysteine rich domain (residues 22-37) of Tat is required for Tat-mediated reduction of F-actin labeled puncta PubMed
tat Uptake of the HIV-1 Tat protein is regulated by arrangement of the actin cytoskeleton in epithelial cells PubMed
tat In Jurkat cells expressing HIV-1 Tat, decreased expression levels are found for basic cytoskeletal proteins such as actin, beta-tubulin, annexin, cofilin, gelsolin, and Rac/Rho-GDI complex PubMed
tat HIV-1 Tat induces actin cytoskeletal rearrangements through p21-activated kinase 1 (PAK1) and downstream activation of the endothelial NADPH oxidase, an effect that is lost by introduction of mutations into the Tat cysteine-rich or basic domains PubMed
matrix gag The localization of the HIV-1 reverse transcription complex to actin microfilaments is mediated by the interaction of a reverse transcription complex component (HIV-1 Matrix) with actin, but not vimentin (intermediate filaments) or tubulin (microtubules) PubMed
nucleocapsid gag HIV-1 NC-like aggregates are associated with dsDNA synthesis by HIV-1 RT and appear to efficiently bind to F-actin filaments, a property that may be involved in targeting complexes to the nuclear envelope PubMed
gag Mature HIV-1 Nucleocapsid, as well as the nucleocapsid domain of the HIV-1 Gag polyprotein, binds filamentous actin resulting in incorporation of actin into virus particles and enhancement of cell motility PubMed
retropepsin gag-pol Actin, one of the most abundant proteins of the cell, is hydrolyzed by the human immunodeficiency virus type 1 (HIV-1) protease during acute infection of cultured human T lymphocytes PubMed
gag-pol HIV-1 protease cleaves actin in vitro at amino acid residues 66-67, 94-95, and 126-127 PubMed
reverse transcriptase gag-pol HIV-1 NC-like aggregates are associated with dsDNA synthesis by HIV-1 RT and appear to efficiently bind to F-actin filaments, a property that may be involved in targeting complexes to the nuclear envelope PubMed
gag-pol The localization of the HIV-1 reverse transcription complex to actin microfilaments is mediated by the interaction of a reverse transcription complex component (HIV-1 Matrix) with actin, but not vimentin (intermediate filaments) or tubulin (microtubules) PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • Common Pathways Underlying Drug Addiction, organism-specific biosystem (from WikiPathways)
    Common Pathways Underlying Drug Addiction, organism-specific biosystemThe pathway was modeled after Figure 2 in Li, et al. 2008 and is based on the common pathways identified in their study as well as protein interaction data. Specifically, glutamate and dopamine neuro...
  • Muscle contraction, organism-specific biosystem (from REACTOME)
    Muscle contraction, organism-specific biosystemIn this module, the processes by which calcium binding triggers actin - myosin interactions and force generation in smooth and striated muscle tissues are annotated.
  • Smooth Muscle Contraction, organism-specific biosystem (from REACTOME)
    Smooth Muscle Contraction, organism-specific biosystemLayers of smooth muscle cells can be found in the walls of numerous organs and tissues within the body. Smooth muscle tissue lacks the striated banding pattern characteristic of skeletal and cardiac ...
  • Vascular smooth muscle contraction, organism-specific biosystem (from KEGG)
    Vascular smooth muscle contraction, organism-specific biosystemThe vascular smooth muscle cell (VSMC) is a highly specialized cell whose principal function is contraction. On contraction, VSMCs shorten, thereby decreasing the diameter of a blood vessel to regula...
  • Vascular smooth muscle contraction, conserved biosystem (from KEGG)
    Vascular smooth muscle contraction, conserved biosystemThe vascular smooth muscle cell (VSMC) is a highly specialized cell whose principal function is contraction. On contraction, VSMCs shorten, thereby decreasing the diameter of a blood vessel to regula...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
ATP binding IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
mesenchyme migration ISS
Inferred from Sequence or Structural Similarity
more info
 
muscle contraction TAS
Traceable Author Statement
more info
 
positive regulation of gene expression ISS
Inferred from Sequence or Structural Similarity
more info
 
Component Evidence Code Pubs
blood microparticle HDA PubMed 
cell body ISS
Inferred from Sequence or Structural Similarity
more info
 
cell periphery IEA
Inferred from Electronic Annotation
more info
 
cytoplasm ISS
Inferred from Sequence or Structural Similarity
more info
 
cytosol TAS
Traceable Author Statement
more info
 
extracellular exosome HDA PubMed 
extracellular space HDA PubMed 
filopodium ISS
Inferred from Sequence or Structural Similarity
more info
 
lamellipodium ISS
Inferred from Sequence or Structural Similarity
more info
 
myosin filament ISS
Inferred from Sequence or Structural Similarity
more info
 

General protein information

Preferred Names
actin, gamma-enteric smooth muscle
Names
actin, gamma 2, smooth muscle, enteric
actin-like protein
alpha-actin-3

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_034140.1 RefSeqGene

    Range
    5001..31688
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001199893.1NP_001186822.1  actin, gamma-enteric smooth muscle isoform 2 precursor

    See identical proteins and their annotated locations for NP_001186822.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) lacks an in-frame exon in the 5' coding region, compared to variant 1, that results in a shorter isoform (2), compared to isoform 1.
    Source sequence(s)
    AK304523, BC012617, BI850192, X16940
    Consensus CDS
    CCDS56124.1
    UniProtKB/Swiss-Prot
    P63267
    Related
    ENSP00000386929.3, ENST00000409731.7
    Conserved Domains (1) summary
    cl17037
    Location:1333
    NBD_sugar-kinase_HSP70_actin; Nucleotide-Binding Domain of the sugar kinase/HSP70/actin superfamily
  2. NM_001615.3NP_001606.1  actin, gamma-enteric smooth muscle isoform 1 precursor

    See identical proteins and their annotated locations for NP_001606.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).
    Source sequence(s)
    BC012617, BI850192, X16940
    Consensus CDS
    CCDS1930.1
    UniProtKB/Swiss-Prot
    P63267
    Related
    ENSP00000295137.3, ENST00000345517.7
    Conserved Domains (1) summary
    PTZ00281
    Location:1376
    PTZ00281; actin; Provisional

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000002.12 Reference GRCh38.p12 Primary Assembly

    Range
    73892966..73919653
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
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