Protein-coding gene in the species Homo sapiens
ACTG2 Identifiers Aliases ACTG2 , ACT, ACTA3, ACTE, ACTL3, ACTSG, VSCM, actin, gamma 2, smooth muscle, enteric, actin gamma 2, smooth muscle, VSCM1, MMIHS5External IDs OMIM : 102545 MGI : 104589 HomoloGene : 123845 GeneCards : ACTG2 Orthologs Species Human Mouse Entrez Ensembl UniProt RefSeq (mRNA) RefSeq (protein) Location (UCSC) Chr 2: 73.89 – 73.92 Mb Chr 6: 83.49 – 83.51 Mb PubMed search[3] [4] Wikidata
Actin, gamma-enteric smooth muscle is a protein that in humans is encoded by the ACTG2 gene .[5] [6] [7]
Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three 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 co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, gamma 2, encoded by this gene, is a smooth muscle actin found in enteric tissues.[7]
Interactions
ACTG2 has been shown to interact with Emerin .[8]
References
^ a b c GRCh38: Ensembl release 89: ENSG00000163017 - Ensembl , May 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000059430 - Ensembl , May 2017
^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ Miwa T, Manabe Y, Kurokawa K, Kamada S, Kanda N, Bruns G, Ueyama H, Kakunaga T (July 1991). "Structure, chromosome location, and expression of the human smooth muscle (enteric type) gamma-actin gene: evolution of six human actin genes" . Mol Cell Biol . 11 (6): 3296–306. doi :10.1128/mcb.11.6.3296 . PMC 360182 . PMID 1710027 .
^ Ueyama H (May 1991). "A HindIII DNA polymorphism in the human enteric type smooth muscle actin gene (ACTSG)" . Nucleic Acids Res . 19 (2): 411. doi :10.1093/nar/19.2.411 . PMC 333620 . PMID 1673027 .
^ a b "Entrez Gene: ACTG2 actin, gamma 2, smooth muscle, enteric" .
^ Lattanzi, Giovanna; Cenni Vittoria; Marmiroli Sandra; Capanni Cristina; Mattioli Elisabetta; Merlini Luciano; Squarzoni Stefano; Maraldi Nadir Mario (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun . United States. 303 (3): 764–70. doi :10.1016/S0006-291X(03)00415-7 . ISSN 0006-291X . PMID 12670476 .
External links
Further reading
Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease". Folia Biol. (Praha) . 42 (5): 227–30. doi :10.1007/BF02818986 . PMID 8997639 . S2CID 7617882 .
Adams LD, Tomasselli AG, Robbins P, et al. (1992). "HIV-1 protease cleaves actin during acute infection of human T-lymphocytes" . AIDS Res. Hum. Retroviruses . 8 (2): 291–5. doi :10.1089/aid.1992.8.291 . PMID 1540415 .
Tomasselli AG, Hui JO, Adams L, et al. (1991). "Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus" . J. Biol. Chem . 266 (22): 14548–53. doi :10.1016/S0021-9258(18)98721-1 . PMID 1907279 .
Shoeman RL, Kesselmier C, Mothes E, et al. (1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease" . FEBS Lett . 278 (2): 199–203. doi :10.1016/0014-5793(91)80116-K . PMID 1991513 . S2CID 37002682 .
Miwa T, Kamada S (1990). "The nucleotide sequence of a human smooth muscle (enteric type) gamma-actin cDNA" . Nucleic Acids Res . 18 (14): 4263. doi :10.1093/nar/18.14.4263 . PMC 331204 . PMID 2377475 .
Ueyama H, Inazawa J, Nishino H, et al. (1995). "Chromosomal mapping of the human smooth muscle actin gene (enteric type, ACTA3) to 2p13.1 and molecular nature of the hindIII polymorphism". Genomics . 25 (3): 720–3. doi :10.1016/0888-7543(95)80016-F . PMID 7759108 .
Szucsik JC, Lessard JL (1996). "Cloning and sequence analysis of the mouse smooth muscle gamma-enteric actin gene". Genomics . 28 (2): 154–62. doi :10.1006/geno.1995.1126 . PMID 8530021 .
Bukrinskaya A, Brichacek B, Mann A, Stevenson M (1999). "Establishment of a Functional Human Immunodeficiency Virus Type 1 (HIV-1) Reverse Transcription Complex Involves the Cytoskeleton" . J. Exp. Med . 188 (11): 2113–25. doi :10.1084/jem.188.11.2113 . PMC 2212381 . PMID 9841925 .
Zhang H, Wang L, Kao S, et al. (1999). "Functional interaction between the cytoplasmic leucine-zipper domain of HIV-1 gp41 and p115-RhoGEF" . Curr. Biol . 9 (21): 1271–4. doi :10.1016/S0960-9822(99)80511-9 . PMC 4513661 . PMID 10556093 .
Kohnen G, Campbell S, Jeffers MD, Cameron IT (2000). "Spatially regulated differentiation of endometrial vascular smooth muscle cells" . Hum. Reprod . 15 (2): 284–92. doi :10.1093/humrep/15.2.284 . PMID 10655297 .
Filmore RA, Dean DA, Zimmer WE (2003). "The smooth muscle gamma-actin gene is androgen responsive in prostate epithelia" . Gene Expr . 10 (5–6): 201–11. doi :10.3727/000000002783992424 . PMC 5977519 . PMID 12450213 .
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences" . Proc. Natl. Acad. Sci. U.S.A . 99 (26): 16899–903. Bibcode :2002PNAS...9916899M . doi :10.1073/pnas.242603899 . PMC 139241 . PMID 12477932 .
Cheng C, Sharp PA (2003). "RNA Polymerase II Accumulation in the Promoter-Proximal Region of the Dihydrofolate Reductase and γ-Actin Genes" . Mol. Cell. Biol . 23 (6): 1961–7. doi :10.1128/MCB.23.6.1961-1967.2003 . PMC 149466 . PMID 12612070 .
Wu RF, Gu Y, Xu YC, et al. (2004). "Human Immunodeficiency Virus Type 1 Tat Regulates Endothelial Cell Actin Cytoskeletal Dynamics through PAK1 Activation and Oxidant Production" . J. Virol . 78 (2): 779–89. doi :10.1128/JVI.78.2.779-789.2004 . PMC 368750 . PMID 14694110 .
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs" . Nat. Genet . 36 (1): 40–5. doi :10.1038/ng1285 . PMID 14702039 .
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)" . Genome Res . 14 (10B): 2121–7. doi :10.1101/gr.2596504 . PMC 528928 . PMID 15489334 .
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4" . Nature . 434 (7034): 724–31. Bibcode :2005Natur.434..724H . doi :10.1038/nature03466 . PMID 15815621 .
PDB gallery
1atn : Atomic structure of the actin:DNASE I complex
1c0f : CRYSTAL STRUCTURE OF DICTYOSTELIUM CAATP-ACTIN IN COMPLEX WITH GELSOLIN SEGMENT 1
1c0g : CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)
1d4x : Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.
1dej : CRYSTAL STRUCTURE OF A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 646: Q228K/T229A/A230Y/A231K/S232E/E360H) IN COMPLEX WITH HUMAN GELSOLIN SEGMENT 1
1eqy : COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1
1esv : COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1
1h1v : GELSOLIN G4-G6/ACTIN COMPLEX
1hlu : STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE
1ijj : THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION
1kxp : CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN
1lcu : Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution
1lot : CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN
1m8q : Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle
1ma9 : Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin
1mdu : Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)
1mvw : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1nlv : Crystal Structure Of Dictyostelium Discoideum Actin Complexed With Ca ATP And Human Gelsolin Segment 1
1nm1 : Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution
1nmd : Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP
1nwk : CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE
1o18 : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o19 : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1a : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1b : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1c : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1d : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1e : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1f : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1g : MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1p8z : Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156
1qz5 : Structure of rabbit actin in complex with kabiramide C
1qz6 : Structure of rabbit actin in complex with jaspisamide A
1rdw : Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer
1rfq : Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer
1rgi : Crystal structure of gelsolin domains G1-G3 bound to actin
1s22 : Absolute Stereochemistry of Ulapualide A
1sqk : CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN
1t44 : Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation
1wua : The structure of Aplyronine A-actin complex
1y64 : Bni1p Formin Homology 2 Domain complexed with ATP-actin
1yxq : Crystal structure of actin in complex with swinholide A
2a3z : Ternary complex of the WH2 domain of WASP with Actin-DNAse I
2a40 : Ternary complex of the WH2 domain of WAVE with Actin-DNAse I
2a41 : Ternary complex of the WH2 Domain of WIP with Actin-DNAse I
2a42 : Actin-DNAse I Complex
2a5x : Crystal Structure of a Cross-linked Actin Dimer
2asm : Structure of Rabbit Actin In Complex With Reidispongiolide A
2aso : Structure of Rabbit Actin In Complex With Sphinxolide B
2asp : Structure of Rabbit Actin In Complex With Reidispongiolide C
2btf : THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN
2d1k : Ternary complex of the WH2 domain of mim with actin-dnase I
2ff3 : Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin
2ff6 : Crystal structure of Gelsolin domain 1:ciboulot domain 2 hybrid in complex with actin
2fxu : X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
2gwj : SpvB ADP-ribosylated actin: hexagonal crystal form
2gwk : SpvB ADP-ribosylated actin: orthorhombic crystal form
2hf3 : Crystal structure of monomeric Actin in the ADP bound state
2hf4 : Crystal structure of Monomeric Actin in its ATP-bound state
2hmp : Uncomplexed actin cleaved with protease ECP32
2oan : Structure of oxidized beta-actin
2q1n : Actin Dimer Cross-linked Between Residues 41 and 374
2q31 : Actin Dimer Cross-linked Between Residues 41 and 374 and proteolytically cleaved by subtilisin between residues 47 and 48.
2q36 : Actin Dimer Cross-linked between Residues 191 and 374 and complexed with Kabiramide C