ACT1_DICDI
ID ACT1_DICDI Reviewed; 376 AA.
AC P07830; P02577; P07827; Q23856; Q23875; Q23877; Q23879; Q23880; Q54H30;
AC Q7KWV6; Q94466;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Major actin;
DE AltName: Full=Actin A1;
DE AltName: Full=Actin A12;
DE AltName: Full=Actin A8;
DE AltName: Full=Actin III;
DE AltName: Full=Actin M6;
DE AltName: Full=Actin-1;
DE AltName: Full=Actin-11;
DE AltName: Full=Actin-12;
DE AltName: Full=Actin-13;
DE AltName: Full=Actin-14;
DE AltName: Full=Actin-15;
DE AltName: Full=Actin-16;
DE AltName: Full=Actin-19;
DE AltName: Full=Actin-2;
DE AltName: Full=Actin-2-sub 1;
DE AltName: Full=Actin-20;
DE AltName: Full=Actin-21;
DE AltName: Full=Actin-3a;
DE AltName: Full=Actin-4;
DE AltName: Full=Actin-5;
DE AltName: Full=Actin-6;
DE AltName: Full=Actin-7;
DE AltName: Full=Actin-8;
DE AltName: Full=Actin-9;
DE AltName: Full=Actin-IEL1;
GN Name=act1; Synonyms=act1a; ORFNames=DDB_G0289553;
GN and
GN Name=act2; Synonyms=act2-1; ORFNames=DDB_G0274133;
GN and
GN Name=act4; ORFNames=DDB_G0289005;
GN and
GN Name=act5; ORFNames=DDB_G0289663;
GN and
GN Name=act6; ORFNames=DDB_G0274135;
GN and
GN Name=act7; ORFNames=DDB_G0280545;
GN and
GN Name=act8; Synonyms=actA8; ORFNames=DDB_G0269234;
GN and
GN Name=act9; ORFNames=DDB_G0274601;
GN and
GN Name=act11; ORFNames=DDB_G0288879;
GN and
GN Name=act12; ORFNames=DDB_G0274129;
GN and
GN Name=act13; ORFNames=DDB_G0274599;
GN and
GN Name=act14; Synonyms=actB1; ORFNames=DDB_G0274137;
GN and
GN Name=act15; Synonyms=actA1; ORFNames=DDB_G0272520;
GN and
GN Name=act16; Synonyms=actM6; ORFNames=DDB_G0272248;
GN and
GN Name=act19; ORFNames=DDB_G0274727;
GN and
GN Name=act20; ORFNames=DDB_G0274285;
GN and
GN Name=act21; ORFNames=DDB_G0274561;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ACT8 AND ACT12).
RX PubMed=3003365; DOI=10.1016/0022-2836(85)90108-1;
RA Romans P., Firtel R.A.;
RT "Organization of the actin multigene family of Dictyostelium discoideum and
RT analysis of variability in the protein coding regions.";
RL J. Mol. Biol. 186:321-335(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3025622; DOI=10.1128/mcb.6.11.3973-3983.1986;
RA Knecht D.A., Cohen S.M., Loomis W.F., Lodish H.F.;
RT "Developmental regulation of Dictyostelium discoideum actin gene fusions
RT carried on low-copy and high-copy transformation vectors.";
RL Mol. Cell. Biol. 6:3973-3983(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-260 (ACT15).
RC STRAIN=79A;
RA Zhou S.;
RT "A new Dictyostelium discoideum actin gene.";
RL Prog. Inorg. Biochem. Biophys. 15:372-376(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-68 (ACT2; ACT5; ACT7; ACT14
RP AND ACT16).
RX PubMed=293714; DOI=10.1073/pnas.76.12.6206;
RA Firtel R.A., Timm R., Kimmel A.R., McKeown M.;
RT "Unusual nucleotide sequences at the 5' end of actin genes in Dictyostelium
RT discoideum.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:6206-6210(1979).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9 (ACT8).
RX PubMed=6894715; DOI=10.1016/0092-8674(81)90105-7;
RA McKeown M., Firtel R.A.;
RT "Differential expression and 5' end mapping of actin genes in
RT Dictyostelium.";
RL Cell 24:799-807(1981).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-9 (ACT4).
RX PubMed=6297763; DOI=10.1016/0092-8674(82)90131-3;
RA Tsang A.S., Mahbubani H.M., Williams J.G.;
RT "Cell-type-specific actin mRNA populations in Dictyostelium discoideum.";
RL Cell 31:375-382(1982).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 (ACT6 AND ACT8).
RX PubMed=6286214; DOI=10.1101/sqb.1982.046.01.046;
RA McKeown M., Firtel R.A.;
RT "Actin multigene family of Dictyostelium.";
RL Cold Spring Harb. Symp. Quant. Biol. 46:495-505(1982).
RN [10]
RP PROTEIN SEQUENCE OF 2-376.
RX PubMed=6892652; DOI=10.1038/284475a0;
RA Vandekerckhove J., Weber K.;
RT "Vegetative Dictyostelium cells containing 17 actin genes express a single
RT major actin.";
RL Nature 284:475-477(1980).
RN [11]
RP PROTEIN SEQUENCE OF 120-133.
RX PubMed=2211676; DOI=10.1016/s0021-9258(18)38260-7;
RA Frankel S., Condeelis J., Leinwand L.;
RT "Expression of actin in Escherichia coli. Aggregation, solubilization, and
RT functional analysis.";
RL J. Biol. Chem. 265:17980-17987(1990).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 289-376 (ACT2; ACT5; ACT8 AND
RP ACT15).
RC STRAIN=AX3;
RX PubMed=6276562; DOI=10.1016/0022-2836(81)90425-3;
RA McKeown M., Firtel R.A.;
RT "Evidence for sub-families of actin genes in Dictyostelium as determined by
RT comparisons of 3' end sequences.";
RL J. Mol. Biol. 151:593-606(1981).
RN [13]
RP PHOSPHORYLATION AT TYR-54.
RX PubMed=7498488; DOI=10.1016/0014-5793(95)01165-b;
RA Jungbluth A., Eckerskorn C., Gerisch G., Lottspeich F., Stocker S.,
RA Schweiger A.;
RT "Stress-induced tyrosine phosphorylation of actin in Dictyostelium cells
RT and localization of the phosphorylation site to tyrosine-53 adjacent to the
RT DNase I binding loop.";
RL FEBS Lett. 375:87-90(1995).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GELSOLIN AND ATP.
RX PubMed=8395021; DOI=10.1038/364685a0;
RA McLaughlin P.J., Gooch J.T., Mannherz H.-G., Weeds A.G.;
RT "Structure of gelsolin segment 1-actin complex and the mechanism of
RT filament severing.";
RL Nature 364:685-692(1993).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GELSOLIN AND ATP.
RX PubMed=12732734; DOI=10.1073/pnas.0832273100;
RA Vorobiev S., Strokopytov B., Drubin D.G., Frieden C., Ono S., Condeelis J.,
RA Rubenstein P.A., Almo S.C.;
RT "The structure of nonvertebrate actin: implications for the ATP hydrolytic
RT mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5760-5765(2003).
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. Multiple isoforms are involved in various cellular
CC functions such as cytoskeleton structure, cell mobility, chromosome
CC movement and muscle contraction.
CC -!- INTERACTION:
CC P07830; P06396: GSN; Xeno; NbExp=4; IntAct=EBI-7195234, EBI-351506;
CC P07830; P07737: PFN1; Xeno; NbExp=3; IntAct=EBI-7195234, EBI-713780;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; X03281; CAA27031.1; -; Genomic_DNA.
DR EMBL; X03282; CAA27032.1; -; Genomic_DNA.
DR EMBL; M14146; AAA33145.1; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71967.1; -; Genomic_DNA.
DR EMBL; AAFI02000008; EAL71184.1; -; Genomic_DNA.
DR EMBL; AAFI02000008; EAL71276.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL69957.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL69959.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL69960.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL69961.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL70035.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL70173.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL70192.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL70193.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL70256.1; -; Genomic_DNA.
DR EMBL; AAFI02000037; EAL67074.1; -; Genomic_DNA.
DR EMBL; AAFI02000126; EAL62963.1; -; Genomic_DNA.
DR EMBL; AAFI02000129; EAL62918.1; -; Genomic_DNA.
DR EMBL; AAFI02000142; EAL62666.1; -; Genomic_DNA.
DR EMBL; AAFI02000148; EAL62543.1; -; Genomic_DNA.
DR EMBL; U25660; AAA74186.1; -; Genomic_DNA.
DR EMBL; V00183; CAA23479.1; -; Genomic_DNA.
DR EMBL; V00186; CAA23482.1; -; Genomic_DNA.
DR EMBL; V00188; CAA23484.1; -; mRNA.
DR EMBL; J01267; AAA33147.1; -; Genomic_DNA.
DR EMBL; J01273; AAA33151.1; -; Genomic_DNA.
DR EMBL; J01274; AAA33153.1; -; Genomic_DNA.
DR EMBL; J01276; AAA51618.1; -; Genomic_DNA.
DR EMBL; J01279; AAA33146.1; -; Genomic_DNA.
DR EMBL; J01265; AAA33158.1; -; mRNA.
DR EMBL; J01270; AAA33159.1; -; mRNA.
DR EMBL; J01272; AAA33160.1; -; Genomic_DNA.
DR EMBL; K02954; AAA33148.1; -; Genomic_DNA.
DR EMBL; K02958; AAA33152.1; -; Genomic_DNA.
DR EMBL; K02960; AAA51619.1; -; Genomic_DNA.
DR EMBL; J01278; AAA33157.1; -; mRNA.
DR PIR; A25084; A25084.
DR PIR; A39239; A39239.
DR PIR; A93223; ATDO.
DR PIR; B23412; B23412.
DR RefSeq; XP_636088.1; XM_630996.1.
DR RefSeq; XP_636169.1; XM_631077.1.
DR RefSeq; XP_636425.1; XM_631333.1.
DR RefSeq; XP_636507.1; XM_631415.1.
DR RefSeq; XP_641146.1; XM_636054.1.
DR RefSeq; XP_643986.1; XM_638894.1.
DR RefSeq; XP_643988.1; XM_638896.1.
DR RefSeq; XP_643989.1; XM_638897.1.
DR RefSeq; XP_643990.1; XM_638898.1.
DR RefSeq; XP_644132.1; XM_639040.1.
DR RefSeq; XP_644146.1; XM_639054.1.
DR RefSeq; XP_644157.1; XM_639065.1.
DR RefSeq; XP_644244.1; XM_639152.1.
DR RefSeq; XP_644246.1; XM_639154.1.
DR RefSeq; XP_645099.1; XM_640007.1.
DR RefSeq; XP_645262.1; XM_640170.1.
DR RefSeq; XP_646688.1; XM_641596.1.
DR PDB; 1C0F; X-ray; 2.40 A; A=2-376.
DR PDB; 1C0G; X-ray; 2.00 A; A=2-376.
DR PDB; 1DEJ; X-ray; 2.40 A; A=2-376.
DR PDB; 1NLV; X-ray; 1.80 A; A=2-376.
DR PDB; 1NM1; X-ray; 1.80 A; A=2-376.
DR PDB; 1NMD; X-ray; 1.90 A; A=2-376.
DR PDB; 3A5L; X-ray; 2.40 A; C=2-376.
DR PDB; 3A5M; X-ray; 2.40 A; C=2-376.
DR PDB; 3A5N; X-ray; 2.36 A; C=2-376.
DR PDB; 3A5O; X-ray; 2.40 A; C=2-376.
DR PDB; 3CHW; X-ray; 2.30 A; A=2-376.
DR PDB; 3CI5; X-ray; 1.70 A; A=2-376.
DR PDB; 3CIP; X-ray; 1.60 A; A=2-376.
DR PDBsum; 1C0F; -.
DR PDBsum; 1C0G; -.
DR PDBsum; 1DEJ; -.
DR PDBsum; 1NLV; -.
DR PDBsum; 1NM1; -.
DR PDBsum; 1NMD; -.
DR PDBsum; 3A5L; -.
DR PDBsum; 3A5M; -.
DR PDBsum; 3A5N; -.
DR PDBsum; 3A5O; -.
DR PDBsum; 3CHW; -.
DR PDBsum; 3CI5; -.
DR PDBsum; 3CIP; -.
DR AlphaFoldDB; P07830; -.
DR SMR; P07830; -.
DR DIP; DIP-40989N; -.
DR IntAct; P07830; 3.
DR MINT; P07830; -.
DR STRING; 44689.DDB0185015; -.
DR iPTMnet; P07830; -.
DR SWISS-2DPAGE; P07830; -.
DR PaxDb; P07830; -.
DR ABCD; P07830; 1 sequenced antibody.
DR EnsemblProtists; EAL62543; EAL62543; DDB_G0289663.
DR EnsemblProtists; EAL62666; EAL62666; DDB_G0289553.
DR EnsemblProtists; EAL62918; EAL62918; DDB_G0289005.
DR EnsemblProtists; EAL62963; EAL62963; DDB_G0288879.
DR EnsemblProtists; EAL67074; EAL67074; DDB_G0280545.
DR EnsemblProtists; EAL69957; EAL69957; DDB_G0274129.
DR EnsemblProtists; EAL69959; EAL69959; DDB_G0274133.
DR EnsemblProtists; EAL69960; EAL69960; DDB_G0274135.
DR EnsemblProtists; EAL69961; EAL69961; DDB_G0274137.
DR EnsemblProtists; EAL70035; EAL70035; DDB_G0274285.
DR EnsemblProtists; EAL70173; EAL70173; DDB_G0274561.
DR EnsemblProtists; EAL70192; EAL70192; DDB_G0274599.
DR EnsemblProtists; EAL70193; EAL70193; DDB_G0274601.
DR EnsemblProtists; EAL70256; EAL70256; DDB_G0274727.
DR EnsemblProtists; EAL71184; EAL71184; DDB_G0272520.
DR EnsemblProtists; EAL71276; EAL71276; DDB_G0272248.
DR EnsemblProtists; EAL71967; EAL71967; DDB_G0269234.
DR GeneID; 8617663; -.
DR GeneID; 8618428; -.
DR GeneID; 8618493; -.
DR GeneID; 8619412; -.
DR GeneID; 8619414; -.
DR GeneID; 8619415; -.
DR GeneID; 8619416; -.
DR GeneID; 8619562; -.
DR GeneID; 8619575; -.
DR GeneID; 8619586; -.
DR GeneID; 8619672; -.
DR GeneID; 8619674; -.
DR GeneID; 8622703; -.
DR GeneID; 8626890; -.
DR GeneID; 8626916; -.
DR GeneID; 8627198; -.
DR GeneID; 8627300; -.
DR KEGG; ddi:DDB_G0269234; -.
DR KEGG; ddi:DDB_G0272248; -.
DR KEGG; ddi:DDB_G0272520; -.
DR KEGG; ddi:DDB_G0274129; -.
DR KEGG; ddi:DDB_G0274133; -.
DR KEGG; ddi:DDB_G0274135; -.
DR KEGG; ddi:DDB_G0274137; -.
DR KEGG; ddi:DDB_G0274285; -.
DR KEGG; ddi:DDB_G0274561; -.
DR KEGG; ddi:DDB_G0274599; -.
DR KEGG; ddi:DDB_G0274601; -.
DR KEGG; ddi:DDB_G0274727; -.
DR KEGG; ddi:DDB_G0280545; -.
DR KEGG; ddi:DDB_G0288879; -.
DR KEGG; ddi:DDB_G0289005; -.
DR KEGG; ddi:DDB_G0289553; -.
DR KEGG; ddi:DDB_G0289663; -.
DR dictyBase; DDB_G0289553; act1.
DR dictyBase; DDB_G0288879; act11.
DR dictyBase; DDB_G0274129; act12.
DR dictyBase; DDB_G0274599; act13.
DR dictyBase; DDB_G0274137; act14.
DR dictyBase; DDB_G0272520; act15.
DR dictyBase; DDB_G0272248; act16.
DR dictyBase; DDB_G0274727; act19.
DR dictyBase; DDB_G0274133; act2.
DR dictyBase; DDB_G0274285; act20.
DR dictyBase; DDB_G0274561; act21.
DR dictyBase; DDB_G0289005; act4.
DR dictyBase; DDB_G0289663; act5.
DR dictyBase; DDB_G0274135; act6.
DR dictyBase; DDB_G0280545; act7.
DR dictyBase; DDB_G0269234; act8.
DR dictyBase; DDB_G0274601; act9.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P07830; -.
DR OMA; STFQQKE; -.
DR PhylomeDB; P07830; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-196025; Formation of annular gap junctions.
DR Reactome; R-DDI-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DDI-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-DDI-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR EvolutionaryTrace; P07830; -.
DR PRO; PR:P07830; -.
DR Proteomes; UP000002195; Chromosome 1.
DR Proteomes; UP000002195; Chromosome 2.
DR Proteomes; UP000002195; Chromosome 3.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005884; C:actin filament; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0060187; C:cell pole; IDA:dictyBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR GO; GO:0061836; C:intranuclear rod; IDA:dictyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:dictyBase.
DR GO; GO:0061851; C:leading edge of lamellipodium; IDA:dictyBase.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0032010; C:phagolysosome; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; TAS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IDA:dictyBase.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; TAS:dictyBase.
DR GO; GO:0006935; P:chemotaxis; TAS:dictyBase.
DR GO; GO:0006897; P:endocytosis; TAS:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; TAS:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IEP:dictyBase.
DR GO; GO:0042331; P:phototaxis; TAS:dictyBase.
DR GO; GO:0001778; P:plasma membrane repair; IDA:dictyBase.
DR GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:dictyBase.
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; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6892652"
FT CHAIN 2..376
FT /note="Major actin"
FT /id="PRO_0000088926"
FT MOD_RES 54
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:7498488"
FT CONFLICT 31
FT /note="V -> L (in Ref. 6; CAA23479)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="F -> S (in Ref. 1; CAA27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="H -> Y (in Ref. 6; CAA23479)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="D -> E (in Ref. 1; CAA27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="A -> G (in Ref. 1; CAA27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="V -> A (in Ref. 1; CAA27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="A -> E (in Ref. 5; AAA74186)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> Q (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="M -> I (in Ref. 5; AAA74186)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Q -> A (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="R -> G (in Ref. 12; AAA51619/AAA33148/AAA33157)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="W -> L (in Ref. 12; AAA33152)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1C0F"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1C0G"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3A5O"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:3CIP"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1C0G"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:3CIP"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1NLV"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1NLV"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1NLV"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3CIP"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:3CIP"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:3CIP"
SQ SEQUENCE 376 AA; 41733 MW; 3610737F3B525123 CRC64;
MDGEDVQALV IDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HTGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYM MKILTERGYS FTTTAEREIV RDIKEKLAYV ALDFEAEMQT AASSSALEKS
YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESAGIHETTY NSIMKCDVDI RKDLYGNVVL
SGGTTMFPGI ADRMNKELTA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
EEYDESGPSI VHRKCF
