Actin, alpha 1

Actin, alpha 1, skeletal muscle

PDB rendering based on 1atn.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1T44

Identifiers

Symbols

ACTA1 ; ACTA; ASMA; CFTD; CFTD1; CFTDM; MPFD; NEM1; NEM2; NEM3

External IDs

OMIM: 102610 MGI: 87902 HomoloGene: 121702 GeneCards: ACTA1 Gene

Gene ontology
Molecular function	• structural constituent of cytoskeleton • protein binding • ATP binding • myosin binding • ADP binding
Cellular component	• stress fiber • extracellular space • cytosol • striated muscle thin filament • actin filament • actin cytoskeleton • sarcomere • lamellipodium • filopodium • cell body • extracellular exosome • blood microparticle
Biological process	• muscle contraction • response to mechanical stimulus • response to extracellular stimulus • response to lithium ion • positive regulation of gene expression • cell growth • muscle filament sliding • skeletal muscle thin filament assembly • skeletal muscle fiber adaptation • response to steroid hormone • skeletal muscle fiber development • mesenchyme migration
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
229.43 – 229.43 Mb

Chr 8:
123.89 – 123.89 Mb

PubMed search

Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene.^[1]^[2]

Actin alpha 1 which is expressed in skeletal muscle is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.^[3]

Skeletal actin gene expression

Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation.^[4] Such conditions result in fusion of committed cells (satellite cells) into myotubes, to form muscle fibers. Skeletal actin itself, when expressed, causes expression of several other "myogenic genes", which are essential to muscle formation.^[5] One key transcription factor that activates skeletal actin gene expression is Serum Response Factor ("SRF"), a protein that binds to specific sites on the promoter DNA of the actin gene.^[6] SRF may bring a number of other proteins to the promoter of skeletal actin, such as andogen receptor, and thereby contribute to induction of skeletal actin gene expression by androgenic (often termed "anabolic") steroids.^[7]

Interactions

Actin, alpha 1 has been shown to interact with TMSB4X,^[8]^[9] MIB2^[10] and PRKCE.^[11]

References

↑ Mogensen J, Kruse TA, Borglum (March 1999). "Assignment of the human skeletal muscle [FC12]a-actin gene (ACTA1) to chromosome 1q42.13-->q42.2 by radiation hybrid mapping". Cytogenet Cell Genet 83 (3-4): 224–5. doi:10.1159/000015184. PMID 10072583.
↑ Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L (August 1983). "Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed". Mol Cell Biol 3 (5): 787–95. doi:10.1128/mcb.3.5.787. PMC 368601. PMID 6865942.
↑ "Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle".
↑ Bandman, E (1992). "Contractile protein isoforms in muscle development.". Developmental Biology 154 (2): 273–83. doi:10.1016/0012-1606(92)90067-Q. PMID 1358730.
↑ Gunning, PW; Ferguson, V; Brennan, KJ; Hardeman, EC (2001). "Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle.". Journal of Cell Science 114 (Pt 3): 513–24. PMID 11171321.
↑ Belaguli, NS; Zhou, W; Trinh, TH; Majesky, MW; Schwartz, RJ (1999). "Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets.". Molecular and Cellular Biology 19 (7): 4582–91. PMC 84256. PMID 10373507.
↑ Vlahopoulos, S; Zimmer, WE; Jenster, G; Belaguli, NS; Balk, SP; Brinkmann, AO; Lanz, RB; Zoumpourlis, VC; Schwartz, RJ (2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene.". The Journal of Biological Chemistry 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502.
↑ Ballweber, Edda; Hannappel Ewald; Huff Thomas; Stephan Harald; Haener Markus; Taschner Nicole; Stoffler Daniel; Aebi Ueli; Mannherz Hans Georg (January 2002). "Polymerisation of chemically cross-linked actin:thymosin beta(4) complex to filamentous actin: alteration in helical parameters and visualisation of thymosin beta(4) binding on F-actin". J. Mol. Biol. (England) 315 (4): 613–25. doi:10.1006/jmbi.2001.5281. ISSN 0022-2836. PMID 11812134.
↑ Safer, D; Sosnick T R; Elzinga M (May 1997). "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends". Biochemistry (UNITED STATES) 36 (19): 5806–16. doi:10.1021/bi970185v. ISSN 0006-2960. PMID 9153421.
↑ Takeuchi, Tamotsu; Heng Henry H Q; Ye Christine J; Liang Sheng-Ben; Iwata Jun; Sonobe Hiroshi; Ohtsuki Yuji (October 2003). "Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma". Am. J. Pathol. (United States) 163 (4): 1395–404. doi:10.1016/S0002-9440(10)63497-9. ISSN 0002-9440. PMC 1868282. PMID 14507647.
↑ England, Karen; Ashford David; Kidd Daniel; Rumsby Martin (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cell. Signal. (England) 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. ISSN 0898-6568. PMID 11897493.

External links

GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy

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.
Di Fiore PP, Scita G (2002). "Eps8 in the midst of GTPases.". Int. J. Biochem. Cell Biol. 34 (10): 1178–83. doi:10.1016/S1357-2725(02)00064-X. PMID 12127568.
Ogawa H, Shiraki H, Matsuda Y, Nakagawa H (1978). "Interaction of adenylosuccinate synthetase with F-actin.". Eur. J. Biochem. 85 (2): 331–7. doi:10.1111/j.1432-1033.1978.tb12243.x. PMID 648524.
den Hartigh JC, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J (1992). "The EGF receptor is an actin-binding protein.". J. Cell Biol. 119 (2): 349–55. doi:10.1083/jcb.119.2.349. PMC 2289650. PMID 1383230.
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.
Levine BA, Moir AJ, Patchell VB, Perry SV (1992). "Binding sites involved in the interaction of actin with the N-terminal region of dystrophin.". FEBS Lett. 298 (1): 44–8. doi:10.1016/0014-5793(92)80019-D. PMID 1544421.
Rijken PJ, Hage WJ, van Bergen en Henegouwen PM; et al. (1992). "Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells.". J. Cell. Sci. 100 (3): 491–9. PMID 1808202.
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.
Winder SJ, Walsh MP (1990). "Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation.". J. Biol. Chem. 265 (17): 10148–55. PMID 2161834.
Kabsch W, Mannherz HG, Suck D; et al. (1990). "Atomic structure of the actin:DNase I complex.". Nature 347 (6288): 37–44. doi:10.1038/347037a0. PMID 2395459.
Takahashi K, Hiwada K, Kokubu T (1988). "Vascular smooth muscle calponin. A novel troponin T-like protein.". Hypertension 11 (6 Pt 2): 620–6. doi:10.1161/01.hyp.11.6.620. PMID 2455687.
Taylor A, Erba HP, Muscat GE, Kedes L (1989). "Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains.". Genomics 3 (4): 323–36. doi:10.1016/0888-7543(88)90123-1. PMID 2907503.
Shen BW, Josephs R, Steck TL (1986). "Ultrastructure of the intact skeleton of the human erythrocyte membrane.". J. Cell Biol. 102 (3): 997–1006. doi:10.1083/jcb.102.3.997. PMC 2114132. PMID 2936753.
Burgess DR, Broschat KO, Hayden JM (1987). "Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins.". J. Cell Biol. 104 (1): 29–40. doi:10.1083/jcb.104.1.29. PMC 2117036. PMID 3793760.
Kedes L, Ng SY, Lin CS; et al. (1986). "The human beta-actin multigene family.". Trans. Assoc. Am. Physicians 98: 42–6. PMID 3842206.
Hanauer A, Levin M, Heilig R; et al. (1983). "Isolation and characterization of cDNA clones for human skeletal muscle alpha actin.". Nucleic Acids Res. 11 (11): 3503–16. doi:10.1093/nar/11.11.3503. PMC 325982. PMID 6190133.
Bretscher A, Weber K (1980). "Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner.". Cell 20 (3): 839–47. doi:10.1016/0092-8674(80)90330-X. PMID 6893424.

PDB gallery

1atn: Atomic structure of the actin:DNASE I complex

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.

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

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Actin, alpha 1

Skeletal actin gene expression

Interactions

See also

References

External links

Further reading