ACTS_RABIT
ID ACTS_RABIT Reviewed; 377 AA.
AC P68135; P02568; P99020;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Actin, alpha skeletal muscle;
DE AltName: Full=Alpha-actin-1;
DE Contains:
DE RecName: Full=Actin, alpha skeletal muscle, intermediate form;
DE Flags: Precursor;
GN Name=ACTA1; Synonyms=ACTA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE OF 3-377, ACETYLATION AT ASP-3, AND METHYLATION AT HIS-75.
RC TISSUE=Skeletal muscle;
RX PubMed=1150665; DOI=10.1016/s0021-9258(19)41139-3;
RA Collins J.H., Elzinga M.;
RT "The primary structure of actin from rabbit skeletal muscle. Completion and
RT analysis of the amino acid sequence.";
RL J. Biol. Chem. 250:5915-5920(1975).
RN [2]
RP SEQUENCE REVISION TO 5; 7; 14 AND 75-81, AND METHYLATION AT HIS-75.
RX PubMed=213279; DOI=10.1111/j.1432-1033.1978.tb12624.x;
RA Vandekerckhove J., Weber K.;
RT "Actin amino-acid sequences. Comparison of actins from calf thymus, bovine
RT brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle
RT actin.";
RL Eur. J. Biochem. 90:451-462(1978).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=588555; DOI=10.1021/bi00645a025;
RA Lu R.C., Elzinga M.;
RT "Partial amino acid sequence of brain actin and its homology with muscle
RT actin.";
RL Biochemistry 16:5801-5806(1977).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-147; 194-283 AND 311-377.
RX PubMed=6687628; DOI=10.1038/302718a0;
RA Putney S.D., Herlihy W.C., Schimmel P.R.;
RT "A new troponin T and cDNA clones for 13 different muscle proteins, found
RT by shotgun sequencing.";
RL Nature 302:718-721(1983).
RN [5]
RP PROTEIN SEQUENCE OF 3-377, AND METHYLATION AT HIS-75.
RC TISSUE=Skeletal muscle;
RX PubMed=499690; DOI=10.1111/j.1432-0436.1979.tb01021.x;
RA Vandekerckhove J., Weber K.;
RT "The complete amino acid sequence of actins from bovine aorta, bovine
RT heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A
RT protein-chemical analysis of muscle actin differentiation.";
RL Differentiation 14:123-133(1979).
RN [6]
RP INTERACTION WITH ALPHA-ACTININ.
RX PubMed=8449927; DOI=10.1016/s0021-9258(18)53368-8;
RA Lebart M.C., Mejean C., Roustan C., Benyamin Y.;
RT "Further characterization of the alpha-actinin-actin interface and
RT comparison with filamin-binding sites on actin.";
RL J. Biol. Chem. 268:5642-5648(1993).
RN [7] {ECO:0007744|PDB:1ATN}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 3-374 IN COMPLEX WITH ATP;
RP BETA-D-MANNOSE AND N-ACETYL-D-GLUCOSAMINE, AND METHYLATION AT HIS-75.
RX PubMed=2395459; DOI=10.1038/347037a0;
RA Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C.;
RT "Atomic structure of the actin:DNase I complex.";
RL Nature 347:37-44(1990).
RN [8] {ECO:0007744|PDB:1NWK}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 3-377 IN COMPLEX WITH ATP ANALOG
RP AND CALCIUM, AND METHYLATION AT HIS-75.
RX PubMed=12813032; DOI=10.1074/jbc.m303689200;
RA Graceffa P., Dominguez R.;
RT "Crystal structure of monomeric actin in the ATP state. Structural basis of
RT nucleotide-dependent actin dynamics.";
RL J. Biol. Chem. 278:34172-34180(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 3-377 IN COMPLEX WITH ATP.
RX PubMed=15099571; DOI=10.1016/j.jsb.2003.12.006;
RA Reutzel R., Yoshioka C., Govindasamy L., Yarmola E.G., Agbandje-McKenna M.,
RA Bubb M.R., McKenna R.;
RT "Actin crystal dynamics: structural implications for F-actin nucleation,
RT polymerization, and branching mediated by the anti-parallel dimer.";
RL J. Struct. Biol. 146:291-301(2004).
RN [10] {ECO:0007744|PDB:2GWJ, ECO:0007744|PDB:2GWK}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 7-377, ADP-RIBOSYLATION AT
RP ARG-179 BY SPVB, AND METHYLATION AT HIS-75.
RX PubMed=16905096; DOI=10.1016/j.str.2006.05.022;
RA Margarit S.M., Davidson W., Frego L., Stebbins C.E.;
RT "A steric antagonism of actin polymerization by a Salmonella virulence
RT protein.";
RL Structure 14:1219-1229(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH COBL; GSN AND TMSB4X,
RP AND SUBUNIT.
RX PubMed=23009842; DOI=10.1016/j.bpj.2012.07.030;
RA Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W.,
RA Reisler E.;
RT "Structural states and dynamics of the D-loop in actin.";
RL Biophys. J. 103:930-939(2012).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix. Each
CC actin can bind to 4 others. Interacts with alpha-actinin
CC (PubMed:8449927). Identified in a complex composed of ACTA1, COBL, GSN
CC AND TMSB4X (PubMed:23009842). Interacts with TTID (By similarity).
CC Interacts (via its C-terminus) with USP25 (By similarity).
CC {ECO:0000250|UniProtKB:P68133, ECO:0000269|PubMed:15099571,
CC ECO:0000269|PubMed:23009842, ECO:0000269|PubMed:8449927}.
CC -!- INTERACTION:
CC P68135; P68135: ACTA1; NbExp=31; IntAct=EBI-367540, EBI-367540;
CC P68135; Q12386: ARP8; Xeno; NbExp=2; IntAct=EBI-367540, EBI-2967;
CC P68135; Q8IRS7: cib; Xeno; NbExp=2; IntAct=EBI-367540, EBI-15573246;
CC P68135; P26932: CNN1; Xeno; NbExp=5; IntAct=EBI-367540, EBI-8602797;
CC P68135; Q03048: COF1; Xeno; NbExp=3; IntAct=EBI-367540, EBI-4853;
CC P68135; Q06440: CRN1; Xeno; NbExp=3; IntAct=EBI-367540, EBI-4950;
CC P68135; P00639: DNASE1; Xeno; NbExp=3; IntAct=EBI-367540, EBI-8545986;
CC P68135; P50402: EMD; Xeno; NbExp=3; IntAct=EBI-367540, EBI-489887;
CC P68135; Q6ZPF4-1: Fmnl3; Xeno; NbExp=3; IntAct=EBI-367540, EBI-16027300;
CC P68135; Q61553: Fscn1; Xeno; NbExp=2; IntAct=EBI-367540, EBI-2308857;
CC P68135; P06396: GSN; Xeno; NbExp=10; IntAct=EBI-367540, EBI-351506;
CC P68135; P08799: mhcA; Xeno; NbExp=8; IntAct=EBI-367540, EBI-2928504;
CC P68135; Q8K4J6: Mrtfa; Xeno; NbExp=15; IntAct=EBI-367540, EBI-8291665;
CC P68135; O70468: Mybpc3; Xeno; NbExp=2; IntAct=EBI-367540, EBI-8347074;
CC P68135; P07737: PFN1; Xeno; NbExp=2; IntAct=EBI-367540, EBI-713780;
CC P68135; Q9KS12: rtxA; Xeno; NbExp=4; IntAct=EBI-367540, EBI-15741102;
CC P68135; Q9U1K1-1: spir; Xeno; NbExp=6; IntAct=EBI-367540, EBI-3431623;
CC P68135; P21454: spvB; Xeno; NbExp=2; IntAct=EBI-367540, EBI-15595598;
CC P68135; Q6GX35: tarP; Xeno; NbExp=4; IntAct=EBI-367540, EBI-15605056;
CC P68135; Q9NG25: toxofilin; Xeno; NbExp=2; IntAct=EBI-367540, EBI-15662915;
CC P68135; P58771: Tpm1; Xeno; NbExp=2; IntAct=EBI-367540, EBI-298478;
CC P68135; P53250: TWF1; Xeno; NbExp=5; IntAct=EBI-367540, EBI-19663;
CC P68135; Q91YR1: Twf1; Xeno; NbExp=2; IntAct=EBI-367540, EBI-527441;
CC P68135; P12003-1: VCL; Xeno; NbExp=2; IntAct=EBI-367540, EBI-6138078;
CC P68135; P18206-2: VCL; Xeno; NbExp=2; IntAct=EBI-367540, EBI-11027067;
CC P68135; Q87GE5: VPA1370; Xeno; NbExp=10; IntAct=EBI-367540, EBI-15666619;
CC P68135; O00401: WASL; Xeno; NbExp=2; IntAct=EBI-367540, EBI-957615;
CC P68135; Q91YD9: Wasl; Xeno; NbExp=5; IntAct=EBI-367540, EBI-642417;
CC P68135; C5IZN1; Xeno; NbExp=3; IntAct=EBI-367540, EBI-16066991;
CC P68135; Q05193-5; Xeno; NbExp=5; IntAct=EBI-367540, EBI-8446026;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or
CC MICAL3) to form methionine sulfoxide promotes actin filament
CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The
CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin
CC repolymerization. {ECO:0000250|UniProtKB:P68134}.
CC -!- PTM: Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella spp.
CC This modification blocks subsequent polymerization and leads to cell
CC death. {ECO:0000269|PubMed:16905096}.
CC -!- PTM: Monomethylation at Lys-86 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC {ECO:0000250|UniProtKB:P68133}.
CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68133}.
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC beta and gamma have been identified. The alpha actins are found in
CC muscle tissues and are a major constituent of the contractile
CC apparatus. The beta and gamma actins coexist in most cell types as
CC components of the cytoskeleton and as mediators of internal cell
CC motility.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; V00872; CAA24241.1; -; mRNA.
DR EMBL; V00873; CAA24242.1; -; mRNA.
DR EMBL; V00874; CAA24243.1; -; mRNA.
DR PIR; A92182; ATRB.
DR PIR; I46471; I46471.
DR PIR; I46472; I46472.
DR PIR; I46473; I46473.
DR PDB; 1ATN; X-ray; 2.80 A; A=3-374.
DR PDB; 1EQY; X-ray; 2.30 A; A=1-377.
DR PDB; 1ESV; X-ray; 2.00 A; A=1-377.
DR PDB; 1H1V; X-ray; 3.00 A; A=3-377.
DR PDB; 1IJJ; X-ray; 2.85 A; A/B=1-377.
DR PDB; 1J6Z; X-ray; 1.54 A; A=3-377.
DR PDB; 1KXP; X-ray; 2.10 A; A=3-377.
DR PDB; 1LCU; X-ray; 3.50 A; A/B=7-377.
DR PDB; 1LOT; X-ray; 2.50 A; B=3-377.
DR PDB; 1M8Q; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1MA9; X-ray; 2.40 A; B=3-377.
DR PDB; 1MVW; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1NWK; X-ray; 1.85 A; A=3-377.
DR PDB; 1O18; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1O19; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1O1A; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1O1B; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1O1C; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1O1D; EM; 70.00 A; 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1O1E; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1O1F; EM; 70.00 A; 0/1/2/3/4/5/6/7/8/V/W/X/Y/Z=3-377.
DR PDB; 1O1G; EM; 70.00 A; 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z=3-377.
DR PDB; 1P8Z; X-ray; 2.60 A; A=1-377.
DR PDB; 1QZ5; X-ray; 1.45 A; A=3-377.
DR PDB; 1QZ6; X-ray; 1.60 A; A=3-377.
DR PDB; 1RDW; X-ray; 2.30 A; X=3-377.
DR PDB; 1RFQ; X-ray; 3.00 A; A/B=3-377.
DR PDB; 1RGI; X-ray; 3.00 A; A=1-377.
DR PDB; 1S22; X-ray; 1.60 A; A=3-377.
DR PDB; 1SQK; X-ray; 2.50 A; A=1-377.
DR PDB; 1T44; X-ray; 2.00 A; A=8-377.
DR PDB; 1WUA; X-ray; 1.45 A; A=3-377.
DR PDB; 1Y64; X-ray; 3.05 A; A=3-377.
DR PDB; 1YXQ; X-ray; 2.01 A; A/B=3-377.
DR PDB; 2A3Z; X-ray; 2.08 A; A=3-377.
DR PDB; 2A40; X-ray; 1.80 A; A/D=3-377.
DR PDB; 2A41; X-ray; 2.60 A; A=3-377.
DR PDB; 2A42; X-ray; 1.85 A; A=3-377.
DR PDB; 2A5X; X-ray; 2.49 A; A=3-377.
DR PDB; 2ASM; X-ray; 1.60 A; A=3-377.
DR PDB; 2ASO; X-ray; 1.70 A; A=3-377.
DR PDB; 2ASP; X-ray; 1.64 A; A=3-377.
DR PDB; 2D1K; X-ray; 2.50 A; A=3-377.
DR PDB; 2FF3; X-ray; 2.00 A; B=3-377.
DR PDB; 2FF6; X-ray; 2.05 A; A=3-377.
DR PDB; 2FXU; X-ray; 1.35 A; A=3-377.
DR PDB; 2GWJ; X-ray; 1.90 A; A=7-377.
DR PDB; 2GWK; X-ray; 2.00 A; A/B=7-377.
DR PDB; 2HMP; X-ray; 1.90 A; A/B=3-377.
DR PDB; 2PAV; X-ray; 1.80 A; A=3-377.
DR PDB; 2PBD; X-ray; 1.50 A; A=1-377.
DR PDB; 2Q0R; X-ray; 1.70 A; A=3-377.
DR PDB; 2Q0U; X-ray; 1.45 A; A=3-377.
DR PDB; 2Q1N; X-ray; 2.70 A; A/B=3-377.
DR PDB; 2Q31; X-ray; 2.70 A; A/B=3-377.
DR PDB; 2Q36; X-ray; 2.50 A; A=3-377.
DR PDB; 2Q97; X-ray; 2.50 A; A=3-377.
DR PDB; 2V51; X-ray; 2.35 A; B/D=1-377.
DR PDB; 2V52; X-ray; 1.45 A; B=1-377.
DR PDB; 2VCP; X-ray; 3.20 A; A/B=3-377.
DR PDB; 2VYP; X-ray; 2.35 A; A/B=1-377.
DR PDB; 2W49; EM; 35.00 A; D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S=3-374.
DR PDB; 2W4U; EM; 35.00 A; D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S=3-374.
DR PDB; 2Y83; EM; 22.90 A; O/P/Q/R/S/T=3-377.
DR PDB; 2YJE; X-ray; 3.10 A; A/B/C=1-377.
DR PDB; 2YJF; X-ray; 3.50 A; A/B/C/D/E=1-377.
DR PDB; 2ZWH; Fiber; 3.30 A; A=3-377.
DR PDB; 3B5U; EM; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-377.
DR PDB; 3BUZ; X-ray; 2.81 A; B=3-377.
DR PDB; 3CJB; X-ray; 3.21 A; A=1-377.
DR PDB; 3CJC; X-ray; 3.90 A; A=1-377.
DR PDB; 3DAW; X-ray; 2.55 A; A=1-377.
DR PDB; 3FFK; X-ray; 3.00 A; B/E=1-377.
DR PDB; 3G37; EM; -; O/P/Q/R/S/T/U/V/W/X/Y/Z=3-377.
DR PDB; 3HBT; X-ray; 2.70 A; A=3-377.
DR PDB; 3J4K; EM; 8.00 A; A/B/C/D/E=3-377.
DR PDB; 3J8A; EM; 3.70 A; A/B/C/D/E=3-377.
DR PDB; 3J8I; EM; 4.70 A; D/E/F/G/H=1-377.
DR PDB; 3J8J; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K=1-377.
DR PDB; 3J8K; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J=1-377.
DR PDB; 3JBI; EM; 8.50 A; A/B=3-377.
DR PDB; 3JBJ; EM; 7.60 A; A/B=3-377.
DR PDB; 3JBK; EM; 8.20 A; A/B=3-377.
DR PDB; 3M1F; X-ray; 2.89 A; A=3-377.
DR PDB; 3M3N; X-ray; 7.00 A; A/B=3-377.
DR PDB; 3M6G; X-ray; 2.00 A; A/B=3-373.
DR PDB; 3MFP; EM; -; A=3-377.
DR PDB; 3MN5; X-ray; 1.50 A; A=3-377.
DR PDB; 3SJH; X-ray; 1.75 A; A=3-377.
DR PDB; 3TPQ; X-ray; 3.45 A; A/B/C/D/E=3-377.
DR PDB; 3TU5; X-ray; 3.00 A; A=1-377.
DR PDB; 3U8X; X-ray; 2.00 A; A/C=3-377.
DR PDB; 3U9Z; X-ray; 2.09 A; A=3-377.
DR PDB; 3UE5; X-ray; 2.76 A; A=3-377.
DR PDB; 4A7F; EM; 7.70 A; A/D/E/F/I=3-377.
DR PDB; 4A7H; EM; 7.80 A; A/D/E/F/G=3-377.
DR PDB; 4A7L; EM; 8.10 A; A/D/E/F/I=3-377.
DR PDB; 4A7N; EM; 8.90 A; A/B/C/D/E=3-377.
DR PDB; 4B1V; X-ray; 1.75 A; A/B=2-377.
DR PDB; 4B1W; X-ray; 1.95 A; B=2-377.
DR PDB; 4B1X; X-ray; 1.80 A; B=2-377.
DR PDB; 4B1Y; X-ray; 1.29 A; B=2-377.
DR PDB; 4B1Z; X-ray; 3.30 A; A/B/C/D/E/F=2-377.
DR PDB; 4EAH; X-ray; 3.40 A; D/F/G/H=1-377.
DR PDB; 4GY2; X-ray; 2.71 A; B=3-377.
DR PDB; 4H03; X-ray; 1.75 A; B=3-377.
DR PDB; 4H0T; X-ray; 2.20 A; B=3-377.
DR PDB; 4H0V; X-ray; 2.03 A; B=3-377.
DR PDB; 4H0X; X-ray; 2.33 A; B=3-377.
DR PDB; 4H0Y; X-ray; 1.94 A; B=3-377.
DR PDB; 4K41; X-ray; 1.40 A; A=3-377.
DR PDB; 4K42; X-ray; 2.90 A; A/B/C/D=3-377.
DR PDB; 4K43; X-ray; 2.90 A; A/B=3-377.
DR PDB; 4PKG; X-ray; 1.80 A; A=1-377.
DR PDB; 4PKH; X-ray; 2.15 A; A/D/F/I=1-377.
DR PDB; 4PKI; X-ray; 2.30 A; A=1-377.
DR PDB; 4PL8; X-ray; 2.00 A; A/B=3-377.
DR PDB; 4V0U; X-ray; 7.88 A; A/B/C/L/M=3-377.
DR PDB; 4WYB; X-ray; 3.49 A; A/C/E/G/I/K/M/O/Q/S/U/X=1-377.
DR PDB; 4Z94; X-ray; 2.40 A; A=1-377.
DR PDB; 5H53; EM; 5.20 A; D/E=3-377.
DR PDB; 5JLF; EM; 3.60 A; A/B/C/D/E=3-377.
DR PDB; 5KG8; EM; 9.10 A; B/C/D=3-377.
DR PDB; 5MVA; EM; 27.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W=3-377.
DR PDB; 5MVY; EM; 28.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W=3-377.
DR PDB; 5ONV; EM; 4.10 A; A/B/C/D/E=3-377.
DR PDB; 5OOC; EM; 3.60 A; A/B/C/D/E=3-377.
DR PDB; 5OOD; EM; 3.70 A; A/B/C/D/E=3-377.
DR PDB; 5OOE; EM; 3.60 A; A/B/C/D/E=3-377.
DR PDB; 5OOF; EM; 3.40 A; A/B/C/D/E=3-377.
DR PDB; 5UBO; X-ray; 2.39 A; A=1-377.
DR PDB; 5YEE; X-ray; 1.81 A; B=1-377.
DR PDB; 5YPU; X-ray; 2.00 A; A/C=7-374.
DR PDB; 5ZZA; X-ray; 1.53 A; A=5-377.
DR PDB; 5ZZB; X-ray; 2.30 A; B/D=7-377.
DR PDB; 6AV9; EM; 3.90 A; A/B/C=1-377.
DR PDB; 6AVB; EM; 3.90 A; A/B/C=1-377.
DR PDB; 6BIH; EM; 6.00 A; C=1-377.
DR PDB; 6BNO; EM; 5.50 A; A/B/C/D/E/F/G/H=1-373.
DR PDB; 6BNP; EM; 4.60 A; A/B/C/D/E/F/G/H=1-373.
DR PDB; 6BNQ; EM; 5.50 A; A/B/C/D/E/F/G/H=1-373.
DR PDB; 6BNU; EM; 7.50 A; A/B/C/D/E/F/G/H=1-373.
DR PDB; 6BNV; EM; 4.60 A; A/B/C/D/E/F/G/H=1-373.
DR PDB; 6BNW; EM; 5.50 A; A/B/C/D/E/F/G/H=1-373.
DR PDB; 6C1D; EM; 3.20 A; A/B/C/D/E=3-377.
DR PDB; 6C1G; EM; 3.80 A; A/B/C/D/E=3-377.
DR PDB; 6C1H; EM; 3.90 A; A/B/C/D/E=3-377.
DR PDB; 6FHL; EM; 3.30 A; A/B/C/D/E=3-377.
DR PDB; 6FM2; X-ray; 2.80 A; A=3-377.
DR PDB; 6GVC; X-ray; 2.60 A; A/B/C/D=1-377.
DR PDB; 6JBK; X-ray; 2.45 A; A/C/E/G=1-377.
DR PDB; 6JCU; X-ray; 2.30 A; A/C=1-377.
DR PDB; 6JH8; X-ray; 2.15 A; A=1-377.
DR PDB; 6JH9; X-ray; 1.74 A; A=1-377.
DR PDB; 6KN7; EM; 6.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=3-377.
DR PDB; 6KN8; EM; 4.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=3-377.
DR PDB; 6MGO; X-ray; 2.20 A; A=1-377.
DR PDB; 6NAS; X-ray; 2.90 A; A=3-377.
DR PDB; 6NBE; X-ray; 2.00 A; A=3-377.
DR PDB; 6QRI; X-ray; 2.40 A; A/B=1-377.
DR PDB; 6RSW; X-ray; 1.95 A; A=3-377.
DR PDB; 6T1Y; EM; 3.30 A; A/B/C/D/E=3-377.
DR PDB; 6T20; EM; 3.70 A; A/B/C/D/E=3-377.
DR PDB; 6T23; EM; 3.10 A; A/B/C/D/E=3-377.
DR PDB; 6T24; EM; 3.70 A; A/B/C/D/E=3-377.
DR PDB; 6T25; EM; 3.60 A; A/B/C/D/E=3-377.
DR PDB; 6U96; EM; 3.80 A; A/B/C/D/E=1-377.
DR PDB; 6UBY; EM; 7.50 A; A/B/C/D/E/F/G/H=1-377.
DR PDB; 6UC0; EM; 7.50 A; A/B/C/D/E/F/G=1-377.
DR PDB; 6UC4; EM; 9.20 A; A/B/C/D/E/F/G/H/J/K/L=1-377.
DR PDB; 6VAO; EM; 3.40 A; A/B/C/D/E=1-377.
DR PDB; 6VAU; EM; 3.50 A; A/B/C/D/E=1-377.
DR PDB; 6VEC; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K=1-377.
DR PDB; 6W17; EM; 3.90 A; I/J/K/L=1-377.
DR PDB; 6W7V; X-ray; 1.70 A; A=1-377.
DR PDB; 6WVT; EM; 3.56 A; B/D/E/F/H/I=1-377.
DR PDB; 6YP9; X-ray; 2.56 A; A=3-377.
DR PDB; 7AD9; EM; 3.50 A; B/D/F/H/I=1-377.
DR PDB; 7AHN; EM; 2.90 A; A/B/C/D/E=1-377.
DR PDB; 7AHQ; EM; 3.60 A; A/B/C/D/E=1-377.
DR PDB; 7C2F; X-ray; 2.03 A; A/C=3-377.
DR PDB; 7C2G; X-ray; 1.71 A; A=1-377.
DR PDB; 7C2H; X-ray; 2.35 A; A=1-377.
DR PDB; 7CCC; X-ray; 3.20 A; A/E=1-377.
DR PDB; 7NXV; X-ray; 2.55 A; A/D=3-377.
DR PDB; 7NZM; EM; 3.96 A; A=3-377.
DR PDB; 7P1G; EM; 3.20 A; A/B/C/D/E=1-377.
DR PDB; 7PLT; EM; 3.30 A; C=1-377.
DR PDB; 7PLU; EM; 3.20 A; C/F/G=1-377.
DR PDB; 7PLV; EM; 3.50 A; C=1-377.
DR PDB; 7PLW; EM; 3.50 A; C=1-377.
DR PDB; 7PLX; EM; 3.60 A; C=1-377.
DR PDB; 7PLY; EM; 3.20 A; C=1-377.
DR PDB; 7PLZ; EM; 3.20 A; C/F/G=1-377.
DR PDB; 7PM0; EM; 3.60 A; C=1-377.
DR PDB; 7PM1; EM; 3.50 A; C=1-377.
DR PDB; 7PM2; EM; 3.60 A; C=1-377.
DR PDB; 7PM3; EM; 3.10 A; B/C/D=1-377.
DR PDB; 7PM5; EM; 3.10 A; C=1-377.
DR PDB; 7PM6; EM; 3.00 A; C/F/G=1-377.
DR PDB; 7PM7; EM; 3.50 A; C=1-377.
DR PDB; 7PM8; EM; 3.50 A; C=1-377.
DR PDB; 7PM9; EM; 3.70 A; C=1-377.
DR PDB; 7PMA; EM; 3.60 A; C=1-377.
DR PDB; 7PMB; EM; 3.60 A; C=1-377.
DR PDB; 7PMC; EM; 3.70 A; C=1-377.
DR PDB; 7PMD; EM; 2.90 A; C=1-377.
DR PDB; 7PME; EM; 2.90 A; C/F/G=1-377.
DR PDB; 7PMF; EM; 3.40 A; C=1-377.
DR PDB; 7PMG; EM; 3.30 A; C=1-377.
DR PDB; 7PMH; EM; 3.40 A; C=1-377.
DR PDB; 7PMI; EM; 3.30 A; C=1-377.
DR PDB; 7PMJ; EM; 3.40 A; C=1-377.
DR PDB; 7PML; EM; 3.30 A; C=1-377.
DR PDBsum; 1ATN; -.
DR PDBsum; 1EQY; -.
DR PDBsum; 1ESV; -.
DR PDBsum; 1H1V; -.
DR PDBsum; 1IJJ; -.
DR PDBsum; 1J6Z; -.
DR PDBsum; 1KXP; -.
DR PDBsum; 1LCU; -.
DR PDBsum; 1LOT; -.
DR PDBsum; 1M8Q; -.
DR PDBsum; 1MA9; -.
DR PDBsum; 1MVW; -.
DR PDBsum; 1NWK; -.
DR PDBsum; 1O18; -.
DR PDBsum; 1O19; -.
DR PDBsum; 1O1A; -.
DR PDBsum; 1O1B; -.
DR PDBsum; 1O1C; -.
DR PDBsum; 1O1D; -.
DR PDBsum; 1O1E; -.
DR PDBsum; 1O1F; -.
DR PDBsum; 1O1G; -.
DR PDBsum; 1P8Z; -.
DR PDBsum; 1QZ5; -.
DR PDBsum; 1QZ6; -.
DR PDBsum; 1RDW; -.
DR PDBsum; 1RFQ; -.
DR PDBsum; 1RGI; -.
DR PDBsum; 1S22; -.
DR PDBsum; 1SQK; -.
DR PDBsum; 1T44; -.
DR PDBsum; 1WUA; -.
DR PDBsum; 1Y64; -.
DR PDBsum; 1YXQ; -.
DR PDBsum; 2A3Z; -.
DR PDBsum; 2A40; -.
DR PDBsum; 2A41; -.
DR PDBsum; 2A42; -.
DR PDBsum; 2A5X; -.
DR PDBsum; 2ASM; -.
DR PDBsum; 2ASO; -.
DR PDBsum; 2ASP; -.
DR PDBsum; 2D1K; -.
DR PDBsum; 2FF3; -.
DR PDBsum; 2FF6; -.
DR PDBsum; 2FXU; -.
DR PDBsum; 2GWJ; -.
DR PDBsum; 2GWK; -.
DR PDBsum; 2HMP; -.
DR PDBsum; 2PAV; -.
DR PDBsum; 2PBD; -.
DR PDBsum; 2Q0R; -.
DR PDBsum; 2Q0U; -.
DR PDBsum; 2Q1N; -.
DR PDBsum; 2Q31; -.
DR PDBsum; 2Q36; -.
DR PDBsum; 2Q97; -.
DR PDBsum; 2V51; -.
DR PDBsum; 2V52; -.
DR PDBsum; 2VCP; -.
DR PDBsum; 2VYP; -.
DR PDBsum; 2W49; -.
DR PDBsum; 2W4U; -.
DR PDBsum; 2Y83; -.
DR PDBsum; 2YJE; -.
DR PDBsum; 2YJF; -.
DR PDBsum; 2ZWH; -.
DR PDBsum; 3B5U; -.
DR PDBsum; 3BUZ; -.
DR PDBsum; 3CJB; -.
DR PDBsum; 3CJC; -.
DR PDBsum; 3DAW; -.
DR PDBsum; 3FFK; -.
DR PDBsum; 3G37; -.
DR PDBsum; 3HBT; -.
DR PDBsum; 3J4K; -.
DR PDBsum; 3J8A; -.
DR PDBsum; 3J8I; -.
DR PDBsum; 3J8J; -.
DR PDBsum; 3J8K; -.
DR PDBsum; 3JBI; -.
DR PDBsum; 3JBJ; -.
DR PDBsum; 3JBK; -.
DR PDBsum; 3M1F; -.
DR PDBsum; 3M3N; -.
DR PDBsum; 3M6G; -.
DR PDBsum; 3MFP; -.
DR PDBsum; 3MN5; -.
DR PDBsum; 3SJH; -.
DR PDBsum; 3TPQ; -.
DR PDBsum; 3TU5; -.
DR PDBsum; 3U8X; -.
DR PDBsum; 3U9Z; -.
DR PDBsum; 3UE5; -.
DR PDBsum; 4A7F; -.
DR PDBsum; 4A7H; -.
DR PDBsum; 4A7L; -.
DR PDBsum; 4A7N; -.
DR PDBsum; 4B1V; -.
DR PDBsum; 4B1W; -.
DR PDBsum; 4B1X; -.
DR PDBsum; 4B1Y; -.
DR PDBsum; 4B1Z; -.
DR PDBsum; 4EAH; -.
DR PDBsum; 4GY2; -.
DR PDBsum; 4H03; -.
DR PDBsum; 4H0T; -.
DR PDBsum; 4H0V; -.
DR PDBsum; 4H0X; -.
DR PDBsum; 4H0Y; -.
DR PDBsum; 4K41; -.
DR PDBsum; 4K42; -.
DR PDBsum; 4K43; -.
DR PDBsum; 4PKG; -.
DR PDBsum; 4PKH; -.
DR PDBsum; 4PKI; -.
DR PDBsum; 4PL8; -.
DR PDBsum; 4V0U; -.
DR PDBsum; 4WYB; -.
DR PDBsum; 4Z94; -.
DR PDBsum; 5H53; -.
DR PDBsum; 5JLF; -.
DR PDBsum; 5KG8; -.
DR PDBsum; 5MVA; -.
DR PDBsum; 5MVY; -.
DR PDBsum; 5ONV; -.
DR PDBsum; 5OOC; -.
DR PDBsum; 5OOD; -.
DR PDBsum; 5OOE; -.
DR PDBsum; 5OOF; -.
DR PDBsum; 5UBO; -.
DR PDBsum; 5YEE; -.
DR PDBsum; 5YPU; -.
DR PDBsum; 5ZZA; -.
DR PDBsum; 5ZZB; -.
DR PDBsum; 6AV9; -.
DR PDBsum; 6AVB; -.
DR PDBsum; 6BIH; -.
DR PDBsum; 6BNO; -.
DR PDBsum; 6BNP; -.
DR PDBsum; 6BNQ; -.
DR PDBsum; 6BNU; -.
DR PDBsum; 6BNV; -.
DR PDBsum; 6BNW; -.
DR PDBsum; 6C1D; -.
DR PDBsum; 6C1G; -.
DR PDBsum; 6C1H; -.
DR PDBsum; 6FHL; -.
DR PDBsum; 6FM2; -.
DR PDBsum; 6GVC; -.
DR PDBsum; 6JBK; -.
DR PDBsum; 6JCU; -.
DR PDBsum; 6JH8; -.
DR PDBsum; 6JH9; -.
DR PDBsum; 6KN7; -.
DR PDBsum; 6KN8; -.
DR PDBsum; 6MGO; -.
DR PDBsum; 6NAS; -.
DR PDBsum; 6NBE; -.
DR PDBsum; 6QRI; -.
DR PDBsum; 6RSW; -.
DR PDBsum; 6T1Y; -.
DR PDBsum; 6T20; -.
DR PDBsum; 6T23; -.
DR PDBsum; 6T24; -.
DR PDBsum; 6T25; -.
DR PDBsum; 6U96; -.
DR PDBsum; 6UBY; -.
DR PDBsum; 6UC0; -.
DR PDBsum; 6UC4; -.
DR PDBsum; 6VAO; -.
DR PDBsum; 6VAU; -.
DR PDBsum; 6VEC; -.
DR PDBsum; 6W17; -.
DR PDBsum; 6W7V; -.
DR PDBsum; 6WVT; -.
DR PDBsum; 6YP9; -.
DR PDBsum; 7AD9; -.
DR PDBsum; 7AHN; -.
DR PDBsum; 7AHQ; -.
DR PDBsum; 7C2F; -.
DR PDBsum; 7C2G; -.
DR PDBsum; 7C2H; -.
DR PDBsum; 7CCC; -.
DR PDBsum; 7NXV; -.
DR PDBsum; 7NZM; -.
DR PDBsum; 7P1G; -.
DR PDBsum; 7PLT; -.
DR PDBsum; 7PLU; -.
DR PDBsum; 7PLV; -.
DR PDBsum; 7PLW; -.
DR PDBsum; 7PLX; -.
DR PDBsum; 7PLY; -.
DR PDBsum; 7PLZ; -.
DR PDBsum; 7PM0; -.
DR PDBsum; 7PM1; -.
DR PDBsum; 7PM2; -.
DR PDBsum; 7PM3; -.
DR PDBsum; 7PM5; -.
DR PDBsum; 7PM6; -.
DR PDBsum; 7PM7; -.
DR PDBsum; 7PM8; -.
DR PDBsum; 7PM9; -.
DR PDBsum; 7PMA; -.
DR PDBsum; 7PMB; -.
DR PDBsum; 7PMC; -.
DR PDBsum; 7PMD; -.
DR PDBsum; 7PME; -.
DR PDBsum; 7PMF; -.
DR PDBsum; 7PMG; -.
DR PDBsum; 7PMH; -.
DR PDBsum; 7PMI; -.
DR PDBsum; 7PMJ; -.
DR PDBsum; 7PML; -.
DR AlphaFoldDB; P68135; -.
DR SMR; P68135; -.
DR DIP; DIP-29021N; -.
DR ELM; P68135; -.
DR IntAct; P68135; 88.
DR MINT; P68135; -.
DR STRING; 9986.ENSOCUP00000006542; -.
DR BindingDB; P68135; -.
DR ChEMBL; CHEMBL4523260; -.
DR CarbonylDB; P68135; -.
DR iPTMnet; P68135; -.
DR MetOSite; P68135; -.
DR eggNOG; KOG0676; Eukaryota.
DR InParanoid; P68135; -.
DR SABIO-RK; P68135; -.
DR EvolutionaryTrace; P68135; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005884; C:actin filament; IDA:CAFA.
DR GO; GO:0032432; C:actin filament bundle; IDA:CAFA.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0031941; C:filamentous actin; IDA:CAFA.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; ISS:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
DR GO; GO:0140660; F:cytoskeletal motor activator activity; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0031432; F:titin binding; IPI:CAFA.
DR GO; GO:0005523; F:tropomyosin binding; IPI:CAFA.
DR GO; GO:0031013; F:troponin I binding; IPI:CAFA.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:CAFA.
DR GO; GO:0030041; P:actin filament polymerization; IDA:CAFA.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:UniProtKB.
DR IDEAL; IID50082; -.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; ATP-binding; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Methylation; Muscle protein;
KW Nucleotide-binding; Oxidation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..377
FT /note="Actin, alpha skeletal muscle, intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442811"
FT CHAIN 3..377
FT /note="Actin, alpha skeletal muscle"
FT /evidence="ECO:0000269|PubMed:1150665,
FT ECO:0000269|PubMed:499690"
FT /id="PRO_0000442812"
FT REGION 112..125
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000269|PubMed:8449927"
FT REGION 360..372
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000269|PubMed:8449927"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 3
FT /note="N-acetylaspartate; in Actin, alpha skeletal muscle"
FT /evidence="ECO:0000269|PubMed:1150665"
FT MOD_RES 46
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68134"
FT MOD_RES 49
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68134"
FT MOD_RES 63
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|PubMed:1150665,
FT ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279,
FT ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690,
FT ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68133"
FT MOD_RES 179
FT /note="ADP-ribosylarginine; by SpvB"
FT /evidence="ECO:0000305|PubMed:16905096"
FT TURN 4..8
FT /evidence="ECO:0007829|PDB:1ATN"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1WUA"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4B1Y"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2FXU"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4PKG"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4H0T"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7PLV"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:4B1Y"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4K41"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7PM8"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2ZWH"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:4B1Y"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2PBD"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6JH9"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1IJJ"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:2PBD"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:4B1Y"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:4B1Y"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:2Q0U"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:4B1Y"
SQ 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
