Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Actin, alpha skeletal muscle (Alpha-actin-1)

 ACTS_RABIT              Reviewed;         377 AA.
P68135; P02568; P99020;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=Actin, alpha skeletal muscle;
AltName: Full=Alpha-actin-1;
Flags: Precursor;
Name=ACTA1; Synonyms=ACTA;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
PROTEIN SEQUENCE OF 3-377, AND ACETYLATION AT ASP-3.
TISSUE=Skeletal muscle;
PubMed=1150665;
Collins J.H., Elzinga M.;
"The primary structure of actin from rabbit skeletal muscle.
Completion and analysis of the amino acid sequence.";
J. Biol. Chem. 250:5915-5920(1975).
[2]
SEQUENCE REVISION TO 5; 7; 14 AND 75-81.
PubMed=213279; DOI=10.1111/j.1432-1033.1978.tb12624.x;
Vandekerckhove J., Weber K.;
"Actin amino-acid sequences. Comparison of actins from calf thymus,
bovine brain, and SV40-transformed mouse 3T3 cells with rabbit
skeletal muscle actin.";
Eur. J. Biochem. 90:451-462(1978).
[3]
SEQUENCE REVISION.
PubMed=588555; DOI=10.1021/bi00645a025;
Lu R.C., Elzinga M.;
"Partial amino acid sequence of brain actin and its homology with
muscle actin.";
Biochemistry 16:5801-5806(1977).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-147; 194-283 AND 311-377.
PubMed=6687628; DOI=10.1038/302718a0;
Putney S.D., Herlihy W.C., Schimmel P.R.;
"A new troponin T and cDNA clones for 13 different muscle proteins,
found by shotgun sequencing.";
Nature 302:718-721(1983).
[5]
PROTEIN SEQUENCE OF 3-377.
TISSUE=Skeletal muscle;
PubMed=499690; DOI=10.1111/j.1432-0436.1979.tb01021.x;
Vandekerckhove J., Weber K.;
"The complete amino acid sequence of actins from bovine aorta, bovine
heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A
protein-chemical analysis of muscle actin differentiation.";
Differentiation 14:123-133(1979).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=2395459; DOI=10.1038/347037a0;
Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C.;
"Atomic structure of the actin:DNase I complex.";
Nature 347:37-44(1990).
[7]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
PubMed=12813032; DOI=10.1074/jbc.M303689200;
Graceffa P., Dominguez R.;
"Crystal structure of monomeric actin in the ATP state. Structural
basis of nucleotide-dependent actin dynamics.";
J. Biol. Chem. 278:34172-34180(2003).
[8]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 3-377 IN COMPLEX WITH ATP.
PubMed=15099571; DOI=10.1016/j.jsb.2003.12.006;
Reutzel R., Yoshioka C., Govindasamy L., Yarmola E.G.,
Agbandje-McKenna M., Bubb M.R., McKenna R.;
"Actin crystal dynamics: structural implications for F-actin
nucleation, polymerization, and branching mediated by the anti-
parallel dimer.";
J. Struct. Biol. 146:291-301(2004).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-377, AND ADP-RIBOSYLATION
AT ARG-179 BY SPVB.
PubMed=16905096; DOI=10.1016/j.str.2006.05.022;
Margarit S.M., Davidson W., Frego L., Stebbins C.E.;
"A steric antagonism of actin polymerization by a Salmonella virulence
protein.";
Structure 14:1219-1229(2006).
[10]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH COBL; GSN AND
TMSB4X, AND SUBUNIT.
PubMed=23009842; DOI=10.1016/j.bpj.2012.07.030;
Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W.,
Reisler E.;
"Structural states and dynamics of the D-loop in actin.";
Biophys. J. 103:930-939(2012).
-!- FUNCTION: Actins are highly conserved proteins that are involved
in various types of cell motility and are ubiquitously expressed
in all eukaryotic cells.
-!- SUBUNIT: 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. Interacts with TTID. Interacts
(via its C-terminus) with USP25 (By similarity). Identified in a
complex composed of ACTA1, COBL, GSN AND TMSB4X. {ECO:0000250,
ECO:0000269|PubMed:15099571, ECO:0000269|PubMed:23009842}.
-!- INTERACTION:
Self; NbExp=30; IntAct=EBI-367540, EBI-367540;
C5IZN1:- (xeno); NbExp=3; IntAct=EBI-367540, EBI-16066991;
Q05193-5:- (xeno); NbExp=5; IntAct=EBI-367540, EBI-8446026;
Q12386:ARP8 (xeno); NbExp=2; IntAct=EBI-367540, EBI-2967;
Q8IRS7:cib (xeno); NbExp=2; IntAct=EBI-367540, EBI-15573246;
P26932:CNN1 (xeno); NbExp=5; IntAct=EBI-367540, EBI-8602797;
Q03048:COF1 (xeno); NbExp=3; IntAct=EBI-367540, EBI-4853;
Q06440:CRN1 (xeno); NbExp=3; IntAct=EBI-367540, EBI-4950;
P00639:DNASE1 (xeno); NbExp=3; IntAct=EBI-367540, EBI-8545986;
P50402:EMD (xeno); NbExp=3; IntAct=EBI-367540, EBI-489887;
Q6ZPF4-1:Fmnl3 (xeno); NbExp=3; IntAct=EBI-367540, EBI-16027300;
Q61553:Fscn1 (xeno); NbExp=2; IntAct=EBI-367540, EBI-2308857;
P06396:GSN (xeno); NbExp=10; IntAct=EBI-367540, EBI-351506;
P08799:mhcA (xeno); NbExp=8; IntAct=EBI-367540, EBI-2928504;
Q8K4J6:Mkl1 (xeno); NbExp=15; IntAct=EBI-367540, EBI-8291665;
O70468:Mybpc3 (xeno); NbExp=2; IntAct=EBI-367540, EBI-8347074;
P07737:PFN1 (xeno); NbExp=2; IntAct=EBI-367540, EBI-713780;
Q9KS12:rtxA (xeno); NbExp=4; IntAct=EBI-367540, EBI-15741102;
Q9U1K1-1:spir (xeno); NbExp=6; IntAct=EBI-367540, EBI-3431623;
P21454:spvB (xeno); NbExp=2; IntAct=EBI-367540, EBI-15595598;
Q6GX35:tarP (xeno); NbExp=4; IntAct=EBI-367540, EBI-15605056;
Q9NG25:toxofilin (xeno); NbExp=2; IntAct=EBI-367540, EBI-15662915;
P58771:Tpm1 (xeno); NbExp=2; IntAct=EBI-367540, EBI-298478;
P53250:TWF1 (xeno); NbExp=5; IntAct=EBI-367540, EBI-19663;
Q91YR1:Twf1 (xeno); NbExp=2; IntAct=EBI-367540, EBI-527441;
P12003-1:VCL (xeno); NbExp=2; IntAct=EBI-367540, EBI-6138078;
P18206-2:VCL (xeno); NbExp=2; IntAct=EBI-367540, EBI-11027067;
Q87GE5:VPA1370 (xeno); NbExp=10; IntAct=EBI-367540, EBI-15666619;
O00401:WASL (xeno); NbExp=2; IntAct=EBI-367540, EBI-957615;
Q91YD9:Wasl (xeno); NbExp=5; IntAct=EBI-367540, EBI-642417;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- PTM: Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella
spp. This modification blocks subsequent polymerization and leads
to cell death.
-!- PTM: Monomethylation at Lys-86 (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). {ECO:0000250}.
-!- 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.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V00872; CAA24241.1; -; mRNA.
EMBL; V00873; CAA24242.1; -; mRNA.
EMBL; V00874; CAA24243.1; -; mRNA.
PIR; A92182; ATRB.
PIR; I46471; I46471.
PIR; I46472; I46472.
PIR; I46473; I46473.
UniGene; Ocu.1731; -.
PDB; 1ALM; Model; -; V/W/X/Y/Z=3-374.
PDB; 1ATN; X-ray; 2.80 A; A=3-374.
PDB; 1EQY; X-ray; 2.30 A; A=1-377.
PDB; 1ESV; X-ray; 2.00 A; A=1-377.
PDB; 1H1V; X-ray; 3.00 A; A=3-377.
PDB; 1IJJ; X-ray; 2.85 A; A/B=1-377.
PDB; 1J6Z; X-ray; 1.54 A; A=3-377.
PDB; 1KXP; X-ray; 2.10 A; A=3-377.
PDB; 1LCU; X-ray; 3.50 A; A/B=7-377.
PDB; 1LOT; X-ray; 2.50 A; B=3-377.
PDB; 1M8Q; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1MA9; X-ray; 2.40 A; B=3-377.
PDB; 1MVW; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1NWK; X-ray; 1.85 A; A=3-377.
PDB; 1O18; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1O19; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1O1A; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1O1B; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1O1C; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1O1D; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1O1E; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1O1F; EM; 70.00 A; 0/1/2/3/4/5/6/7/8/V/W/X/Y/Z=3-377.
PDB; 1O1G; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
PDB; 1P8Z; X-ray; 2.60 A; A=1-377.
PDB; 1QZ5; X-ray; 1.45 A; A=3-377.
PDB; 1QZ6; X-ray; 1.60 A; A=3-377.
PDB; 1RDW; X-ray; 2.30 A; X=3-377.
PDB; 1RFQ; X-ray; 3.00 A; A/B=3-377.
PDB; 1RGI; X-ray; 3.00 A; A=1-377.
PDB; 1S22; X-ray; 1.60 A; A=3-377.
PDB; 1SQK; X-ray; 2.50 A; A=1-377.
PDB; 1T44; X-ray; 2.00 A; A=8-377.
PDB; 1UY5; Model; -; A=3-374.
PDB; 1WUA; X-ray; 1.45 A; A=3-377.
PDB; 1Y64; X-ray; 3.05 A; A=3-377.
PDB; 1YXQ; X-ray; 2.01 A; A/B=3-377.
PDB; 2A3Z; X-ray; 2.08 A; A=3-377.
PDB; 2A40; X-ray; 1.80 A; A/D=3-377.
PDB; 2A41; X-ray; 2.60 A; A=3-377.
PDB; 2A42; X-ray; 1.85 A; A=3-377.
PDB; 2A5X; X-ray; 2.49 A; A=3-377.
PDB; 2ASM; X-ray; 1.60 A; A=3-377.
PDB; 2ASO; X-ray; 1.70 A; A=3-377.
PDB; 2ASP; X-ray; 1.64 A; A=3-377.
PDB; 2D1K; X-ray; 2.50 A; A=3-377.
PDB; 2FF3; X-ray; 2.00 A; B=3-377.
PDB; 2FF6; X-ray; 2.05 A; A=3-377.
PDB; 2FXU; X-ray; 1.35 A; A=3-377.
PDB; 2GWJ; X-ray; 1.90 A; A=7-377.
PDB; 2GWK; X-ray; 2.00 A; A/B=7-377.
PDB; 2HMP; X-ray; 1.90 A; A/B=3-377.
PDB; 2PAV; X-ray; 1.80 A; A=3-377.
PDB; 2PBD; X-ray; 1.50 A; A=1-377.
PDB; 2Q0R; X-ray; 1.70 A; A=3-377.
PDB; 2Q0U; X-ray; 1.45 A; A=3-377.
PDB; 2Q1N; X-ray; 2.70 A; A/B=3-377.
PDB; 2Q31; X-ray; 2.70 A; A/B=3-377.
PDB; 2Q36; X-ray; 2.50 A; A=3-377.
PDB; 2Q97; X-ray; 2.50 A; A=3-377.
PDB; 2V51; X-ray; 2.35 A; B/D=1-377.
PDB; 2V52; X-ray; 1.45 A; B=1-377.
PDB; 2VCP; X-ray; 3.20 A; A/B=3-377.
PDB; 2VYP; X-ray; 2.35 A; A/B=1-377.
PDB; 2W49; EM; 35.00 A; D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S=3-374.
PDB; 2W4U; EM; 35.00 A; D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S=3-374.
PDB; 2Y83; EM; 22.90 A; O/P/Q/R/S/T=3-377.
PDB; 2YJE; X-ray; 3.10 A; A/B/C=1-377.
PDB; 2YJF; X-ray; 3.50 A; A/B/C/D/E=1-377.
PDB; 2ZWH; Fiber; 3.30 A; A=3-377.
PDB; 3B5U; EM; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-377.
PDB; 3BUZ; X-ray; 2.81 A; B=3-377.
PDB; 3CJB; X-ray; 3.21 A; A=1-377.
PDB; 3CJC; X-ray; 3.90 A; A=1-377.
PDB; 3DAW; X-ray; 2.55 A; A=1-377.
PDB; 3FFK; X-ray; 3.00 A; B/E=1-377.
PDB; 3G37; EM; -; O/P/Q/R/S/T/U/V/W/X/Y/Z=3-377.
PDB; 3HBT; X-ray; 2.70 A; A=3-377.
PDB; 3J4K; EM; 8.00 A; A/B/C/D/E=3-377.
PDB; 3J8A; EM; 3.70 A; A/B/C/D/E=3-377.
PDB; 3J8I; EM; 4.70 A; D/E/F/G/H=1-377.
PDB; 3J8J; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K=1-377.
PDB; 3J8K; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J=1-377.
PDB; 3JBI; EM; 8.50 A; A/B=3-377.
PDB; 3JBJ; EM; 7.60 A; A/B=3-377.
PDB; 3JBK; EM; 8.20 A; A/B=3-377.
PDB; 3M1F; X-ray; 2.89 A; A=3-377.
PDB; 3M3N; X-ray; 7.00 A; A/B=3-377.
PDB; 3M6G; X-ray; 2.00 A; A/B=3-373.
PDB; 3MFP; EM; -; A=3-377.
PDB; 3MN5; X-ray; 1.50 A; A=3-377.
PDB; 3SJH; X-ray; 1.75 A; A=3-377.
PDB; 3TPQ; X-ray; 3.45 A; A/B/C/D/E=3-377.
PDB; 3TU5; X-ray; 3.00 A; A=1-377.
PDB; 3U8X; X-ray; 2.00 A; A/C=3-377.
PDB; 3U9Z; X-ray; 2.09 A; A=3-377.
PDB; 3UE5; X-ray; 2.76 A; A=3-377.
PDB; 4A7F; EM; 7.70 A; A/D/E/F/I=3-377.
PDB; 4A7H; EM; 7.80 A; A/D/E/F/G=3-377.
PDB; 4A7L; EM; 8.10 A; A/D/E/F/I=3-377.
PDB; 4A7N; EM; 8.90 A; A/B/C/D/E=3-377.
PDB; 4B1V; X-ray; 1.75 A; A/B=2-377.
PDB; 4B1W; X-ray; 1.95 A; B=2-377.
PDB; 4B1X; X-ray; 1.80 A; B=2-377.
PDB; 4B1Y; X-ray; 1.29 A; B=2-377.
PDB; 4B1Z; X-ray; 3.30 A; A/B/C/D/E/F=2-377.
PDB; 4EAH; X-ray; 3.40 A; D/F/G/H=1-377.
PDB; 4GY2; X-ray; 2.71 A; B=3-377.
PDB; 4H03; X-ray; 1.75 A; B=3-377.
PDB; 4H0T; X-ray; 2.20 A; B=3-377.
PDB; 4H0V; X-ray; 2.03 A; B=3-377.
PDB; 4H0X; X-ray; 2.33 A; B=3-377.
PDB; 4H0Y; X-ray; 1.94 A; B=3-377.
PDB; 4K41; X-ray; 1.40 A; A=3-377.
PDB; 4K42; X-ray; 2.90 A; A/B/C/D=3-377.
PDB; 4K43; X-ray; 2.90 A; A/B=3-377.
PDB; 4PKG; X-ray; 1.80 A; A=1-377.
PDB; 4PKH; X-ray; 2.15 A; A/D/F/I=1-377.
PDB; 4PKI; X-ray; 2.30 A; A=1-377.
PDB; 4PL8; X-ray; 2.00 A; A/B=3-377.
PDB; 4V0U; X-ray; 7.88 A; A/B/C/L/M=3-377.
PDB; 4WYB; X-ray; 3.49 A; A/C/E/G/I/K/M/O/Q/S/U/X=1-377.
PDB; 4Z94; X-ray; 2.40 A; A=1-377.
PDB; 5H53; EM; 5.20 A; D/E=3-377.
PDB; 5JLF; EM; 3.60 A; A/B/C/D/E=3-377.
PDB; 5KG8; EM; 9.10 A; B/C/D=3-377.
PDBsum; 1ALM; -.
PDBsum; 1ATN; -.
PDBsum; 1EQY; -.
PDBsum; 1ESV; -.
PDBsum; 1H1V; -.
PDBsum; 1IJJ; -.
PDBsum; 1J6Z; -.
PDBsum; 1KXP; -.
PDBsum; 1LCU; -.
PDBsum; 1LOT; -.
PDBsum; 1M8Q; -.
PDBsum; 1MA9; -.
PDBsum; 1MVW; -.
PDBsum; 1NWK; -.
PDBsum; 1O18; -.
PDBsum; 1O19; -.
PDBsum; 1O1A; -.
PDBsum; 1O1B; -.
PDBsum; 1O1C; -.
PDBsum; 1O1D; -.
PDBsum; 1O1E; -.
PDBsum; 1O1F; -.
PDBsum; 1O1G; -.
PDBsum; 1P8Z; -.
PDBsum; 1QZ5; -.
PDBsum; 1QZ6; -.
PDBsum; 1RDW; -.
PDBsum; 1RFQ; -.
PDBsum; 1RGI; -.
PDBsum; 1S22; -.
PDBsum; 1SQK; -.
PDBsum; 1T44; -.
PDBsum; 1UY5; -.
PDBsum; 1WUA; -.
PDBsum; 1Y64; -.
PDBsum; 1YXQ; -.
PDBsum; 2A3Z; -.
PDBsum; 2A40; -.
PDBsum; 2A41; -.
PDBsum; 2A42; -.
PDBsum; 2A5X; -.
PDBsum; 2ASM; -.
PDBsum; 2ASO; -.
PDBsum; 2ASP; -.
PDBsum; 2D1K; -.
PDBsum; 2FF3; -.
PDBsum; 2FF6; -.
PDBsum; 2FXU; -.
PDBsum; 2GWJ; -.
PDBsum; 2GWK; -.
PDBsum; 2HMP; -.
PDBsum; 2PAV; -.
PDBsum; 2PBD; -.
PDBsum; 2Q0R; -.
PDBsum; 2Q0U; -.
PDBsum; 2Q1N; -.
PDBsum; 2Q31; -.
PDBsum; 2Q36; -.
PDBsum; 2Q97; -.
PDBsum; 2V51; -.
PDBsum; 2V52; -.
PDBsum; 2VCP; -.
PDBsum; 2VYP; -.
PDBsum; 2W49; -.
PDBsum; 2W4U; -.
PDBsum; 2Y83; -.
PDBsum; 2YJE; -.
PDBsum; 2YJF; -.
PDBsum; 2ZWH; -.
PDBsum; 3B5U; -.
PDBsum; 3BUZ; -.
PDBsum; 3CJB; -.
PDBsum; 3CJC; -.
PDBsum; 3DAW; -.
PDBsum; 3FFK; -.
PDBsum; 3G37; -.
PDBsum; 3HBT; -.
PDBsum; 3J4K; -.
PDBsum; 3J8A; -.
PDBsum; 3J8I; -.
PDBsum; 3J8J; -.
PDBsum; 3J8K; -.
PDBsum; 3JBI; -.
PDBsum; 3JBJ; -.
PDBsum; 3JBK; -.
PDBsum; 3M1F; -.
PDBsum; 3M3N; -.
PDBsum; 3M6G; -.
PDBsum; 3MFP; -.
PDBsum; 3MN5; -.
PDBsum; 3SJH; -.
PDBsum; 3TPQ; -.
PDBsum; 3TU5; -.
PDBsum; 3U8X; -.
PDBsum; 3U9Z; -.
PDBsum; 3UE5; -.
PDBsum; 4A7F; -.
PDBsum; 4A7H; -.
PDBsum; 4A7L; -.
PDBsum; 4A7N; -.
PDBsum; 4B1V; -.
PDBsum; 4B1W; -.
PDBsum; 4B1X; -.
PDBsum; 4B1Y; -.
PDBsum; 4B1Z; -.
PDBsum; 4EAH; -.
PDBsum; 4GY2; -.
PDBsum; 4H03; -.
PDBsum; 4H0T; -.
PDBsum; 4H0V; -.
PDBsum; 4H0X; -.
PDBsum; 4H0Y; -.
PDBsum; 4K41; -.
PDBsum; 4K42; -.
PDBsum; 4K43; -.
PDBsum; 4PKG; -.
PDBsum; 4PKH; -.
PDBsum; 4PKI; -.
PDBsum; 4PL8; -.
PDBsum; 4V0U; -.
PDBsum; 4WYB; -.
PDBsum; 4Z94; -.
PDBsum; 5H53; -.
PDBsum; 5JLF; -.
PDBsum; 5KG8; -.
ProteinModelPortal; P68135; -.
SMR; P68135; -.
DIP; DIP-29021N; -.
ELM; P68135; -.
IntAct; P68135; 86.
MINT; MINT-1489367; -.
STRING; 9986.ENSOCUP00000006542; -.
iPTMnet; P68135; -.
PRIDE; P68135; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
HOGENOM; HOG000233340; -.
HOVERGEN; HBG003771; -.
InParanoid; P68135; -.
SABIO-RK; P68135; -.
EvolutionaryTrace; P68135; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005884; C:actin filament; IDA:CAFA.
GO; GO:0032432; C:actin filament bundle; IDA:CAFA.
GO; GO:0044297; C:cell body; ISS:AgBase.
GO; GO:0005737; C:cytoplasm; ISS:AgBase.
GO; GO:0031941; C:filamentous actin; IDA:CAFA.
GO; GO:0030175; C:filopodium; ISS:AgBase.
GO; GO:0030027; C:lamellipodium; ISS:AgBase.
GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
GO; GO:0005865; C:striated muscle thin filament; ISS:UniProtKB.
GO; GO:0003785; F:actin monomer binding; IDA:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
GO; GO:0032036; F:myosin heavy chain binding; IPI:CAFA.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0031432; F:titin binding; IPI:CAFA.
GO; GO:0005523; F:tropomyosin binding; IPI:CAFA.
GO; GO:0031013; F:troponin I binding; IPI:CAFA.
GO; GO:0051017; P:actin filament bundle assembly; IDA:CAFA.
GO; GO:0030041; P:actin filament polymerization; IDA:CAFA.
GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
GO; GO:1904623; P:positive regulation of actin-dependent ATPase activity; IDA:CAFA.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:UniProtKB.
InterPro; IPR004000; Actin.
InterPro; IPR020902; Actin/actin-like_CS.
InterPro; IPR004001; Actin_CS.
PANTHER; PTHR11937; PTHR11937; 1.
Pfam; PF00022; Actin; 1.
PRINTS; PR00190; ACTIN.
SMART; SM00268; ACTIN; 1.
PROSITE; PS00406; ACTINS_1; 1.
PROSITE; PS00432; ACTINS_2; 1.
PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; ATP-binding;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Methylation; Muscle protein; Nucleotide-binding; Reference proteome.
PROPEP 1 2 Removed in mature form.
{ECO:0000269|PubMed:1150665,
ECO:0000269|PubMed:499690}.
/FTId=PRO_0000000850.
CHAIN 3 377 Actin, alpha skeletal muscle.
/FTId=PRO_0000000851.
MOD_RES 3 3 N-acetylaspartate.
{ECO:0000269|PubMed:1150665}.
MOD_RES 63 63 N6-malonyllysine. {ECO:0000250}.
MOD_RES 86 86 N6-methyllysine.
{ECO:0000250|UniProtKB:P68133}.
MOD_RES 179 179 ADP-ribosylarginine; by SpvB.
{ECO:0000305|PubMed:16905096}.
TURN 4 8 {ECO:0000244|PDB:1ATN}.
STRAND 10 14 {ECO:0000244|PDB:4B1Y}.
STRAND 16 23 {ECO:0000244|PDB:4B1Y}.
STRAND 26 28 {ECO:0000244|PDB:1WUA}.
STRAND 30 34 {ECO:0000244|PDB:4B1Y}.
STRAND 37 40 {ECO:0000244|PDB:4B1Y}.
TURN 42 44 {ECO:0000244|PDB:2FXU}.
STRAND 45 48 {ECO:0000244|PDB:1LCU}.
STRAND 49 51 {ECO:0000244|PDB:4PKG}.
STRAND 54 56 {ECO:0000244|PDB:4H0T}.
HELIX 57 62 {ECO:0000244|PDB:4B1Y}.
HELIX 64 66 {ECO:0000244|PDB:4B1Y}.
STRAND 67 70 {ECO:0000244|PDB:4B1Y}.
STRAND 72 74 {ECO:0000244|PDB:4B1Y}.
HELIX 81 93 {ECO:0000244|PDB:4B1Y}.
TURN 94 96 {ECO:0000244|PDB:4K41}.
HELIX 100 102 {ECO:0000244|PDB:4B1Y}.
STRAND 105 109 {ECO:0000244|PDB:4B1Y}.
HELIX 115 127 {ECO:0000244|PDB:4B1Y}.
STRAND 132 138 {ECO:0000244|PDB:4B1Y}.
HELIX 139 146 {ECO:0000244|PDB:4B1Y}.
STRAND 150 157 {ECO:0000244|PDB:4B1Y}.
STRAND 158 160 {ECO:0000244|PDB:2ZWH}.
STRAND 162 168 {ECO:0000244|PDB:4B1Y}.
HELIX 174 176 {ECO:0000244|PDB:4B1Y}.
STRAND 178 180 {ECO:0000244|PDB:4B1Y}.
HELIX 184 196 {ECO:0000244|PDB:4B1Y}.
TURN 197 199 {ECO:0000244|PDB:4B1Y}.
HELIX 205 218 {ECO:0000244|PDB:4B1Y}.
HELIX 225 234 {ECO:0000244|PDB:4B1Y}.
STRAND 236 238 {ECO:0000244|PDB:2PBD}.
STRAND 240 243 {ECO:0000244|PDB:4B1Y}.
STRAND 245 247 {ECO:0000244|PDB:1ESV}.
STRAND 249 253 {ECO:0000244|PDB:4B1Y}.
HELIX 255 264 {ECO:0000244|PDB:4B1Y}.
HELIX 266 269 {ECO:0000244|PDB:4B1Y}.
HELIX 276 285 {ECO:0000244|PDB:4B1Y}.
HELIX 289 291 {ECO:0000244|PDB:4B1Y}.
HELIX 292 296 {ECO:0000244|PDB:4B1Y}.
STRAND 299 303 {ECO:0000244|PDB:4B1Y}.
HELIX 304 306 {ECO:0000244|PDB:4B1Y}.
STRAND 308 310 {ECO:0000244|PDB:1IJJ}.
HELIX 311 322 {ECO:0000244|PDB:4B1Y}.
HELIX 324 326 {ECO:0000244|PDB:2PBD}.
HELIX 337 339 {ECO:0000244|PDB:4B1Y}.
HELIX 340 350 {ECO:0000244|PDB:4B1Y}.
HELIX 352 357 {ECO:0000244|PDB:4B1Y}.
STRAND 358 360 {ECO:0000244|PDB:4B1Y}.
HELIX 361 367 {ECO:0000244|PDB:4B1Y}.
HELIX 368 370 {ECO:0000244|PDB:2Q0U}.
HELIX 371 375 {ECO:0000244|PDB:4B1Y}.
SEQUENCE 377 AA; 42051 MW; DF2A3A046346A179 CRC64;
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
KQEYDEAGPS IVHRKCF


Related products :

Catalog number Product name Quantity
E1634Rb ELISA kit ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Oryctolagus cuniculus,Rabbit 96T
U1634h CLIA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Homo sapiens,Human 96T
E1634Rb ELISA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Oryctolagus cuniculus,Rabbit 96T
E1634h ELISA kit ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Homo sapiens,Human 96T
E1634h ELISA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Homo sapiens,Human 96T
U1634Rb CLIA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Oryctolagus cuniculus,Rabbit 96T
E1634r ELISA kit Acta,Acta1,Actin, alpha skeletal muscle,Alpha-actin-1,Rat,Rattus norvegicus 96T
E1634m ELISA kit Acta,Acta1,Actin, alpha skeletal muscle,Alpha-actin-1,Mouse,Mus musculus 96T
U1634b CLIA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Bos taurus,Bovine 96T
E1634b ELISA kit ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Bos taurus,Bovine 96T
U1634r CLIA Acta,Acta1,Actin, alpha skeletal muscle,Alpha-actin-1,Rat,Rattus norvegicus 96T
E1634b ELISA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Bos taurus,Bovine 96T
U1634m CLIA Acta,Acta1,Actin, alpha skeletal muscle,Alpha-actin-1,Mouse,Mus musculus 96T
E1634r ELISA Acta,Acta1,Actin, alpha skeletal muscle,Alpha-actin-1,Rat,Rattus norvegicus 96T
E1634m ELISA Acta,Acta1,Actin, alpha skeletal muscle,Alpha-actin-1,Mouse,Mus musculus 96T
E1634p ELISA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Pig,Sus scrofa 96T
E1634p ELISA kit ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Pig,Sus scrofa 96T
U1634p CLIA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Pig,Sus scrofa 96T
18-272-196320 skeletal muscle Actin - Rabbit polyclonal to skeletal muscle Actin; Alpha-actin-1 Polyclonal 1 ml
U1634c CLIA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Chicken,Gallus gallus 96T
E1634c ELISA kit ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Chicken,Gallus gallus 96T
E1634c ELISA ACTA,ACTA1,Actin, alpha skeletal muscle,Alpha-actin-1,Chicken,Gallus gallus 96T
20-272-191692 alpha smooth muscle Actin - Mouse monoclonal [SPM332] to alpha smooth muscle Actin; Alpha-actin-2; Cell growth-inhibiting gene 46 protein Monoclonal 1 ml
18-272-196321 skeletal muscle Actin prediluted - Rabbit polyclonal to skeletal muscle Actin prediluted; Alpha-actin-1 Polyclonal 7 ml
20-272-191632 alpha smooth muscle Actin - Mouse monoclonal [0.N.5] to alpha smooth muscle Actin; Alpha-actin-2; Cell growth-inhibiting gene 46 protein Monoclonal 0.25 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur