ACTG2

Identifiers

ACTG2, ACT, ACTA3, ACTE, ACTL3, ACTSG, VSCM, actin, gamma 2, smooth muscle, enteric

External IDs

MGI: 104589 HomoloGene: 123845 GeneCards: ACTG2

Gene ontology
Molecular function	• nucleotide binding • ATP binding
Cellular component	• cytoplasm • filopodium • extracellular space • cell body • myosin filament • cytosol • blood microparticle • extracellular exosome • cytoskeleton • cell periphery • lamellipodium
Biological process	• mesenchyme migration • positive regulation of gene expression • muscle contraction
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


72


11468

Ensembl


ENSG00000163017


ENSMUSG00000059430

UniProt


P63267


P63268

RefSeq (mRNA)


NM_001615 NM_001199893


NM_009610

RefSeq (protein)


NP_001186822.1 NP_001606.1


NP_033740.2

Location (UCSC)

Chr 2: 73.89 – 73.92 Mb

Chr 6: 83.51 – 83.54 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Actin, gamma-enteric smooth muscle is a protein that in humans is encoded by the ACTG2 gene.^[3]^[4]^[5]

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.^[5]

Interactions

ACTG2 has been shown to interact with Emerin.^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "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

Human ACTG2 genome location and ACTG2 gene details page in the UCSC Genome Browser.

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.
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. 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.
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. 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. 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. 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. 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
1j6z: UNCOMPLEXED ACTIN
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

Proteins of the cytoskeleton

Human

Microfilaments
and ABPs

Myofilament

Actins	A1 A2 B C1 G1 G2

Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1

Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

Intermediate
filaments

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 7 8 9

Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86

Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80

Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Microtubules
and MAPs

Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3

Dyneins	axonemal: DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic: DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3

Other	Tau protein Dynactin DCTN1 Tubulins TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3

Catenins

Membrane

Dystrophin
- Dystroglycan
Utrophin
Ankyrin
- ANK1
- ANK2
- ANK3
Spectrin
- SPTA1
- SPTAN1
- SPTB
- SPTBN1
- SPTBN2
- SPTBN4
- SPTBN5

Other

Plakins
- Corneodesmosin
- Desmoplakin
- Dystonin
- Envoplakin
- MACF1
- Periplakin
- Plectin
Talin
- TLN1
Vinculin
Plakophilin
- PKP1
- PKP2

Nonhuman

See also: cytoskeletal defects

This article is issued from Wikipedia - version of the 11/30/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

ACTG2

Interactions

References

External links

Further reading