(data stored in SCRATCH zone)

SWISSPROT: ACT1_DICDI

ID   ACT1_DICDI              Reviewed;         376 AA.
AC   P07830; P02577; P07827; Q23856; Q23875; Q23877; Q23879; Q23880;
AC   Q54H30; Q7KWV6; Q94466;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAY-2019, entry version 146.
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; Mycetozoa; Dictyostelids; 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
RT   discoideum and analysis of variability in the protein coding
RT   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;
RA   Knecht D.A., Cohen S.M., Loomis W.F., Lodish H.F.;
RT   "Developmental regulation of Dictyostelium discoideum actin gene
RT   fusions 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.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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;
RP   ACT14 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
RT   Dictyostelium 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
RT   discoideum.";
RL   Cell 31:375-382(1982).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 (ACT6 AND ACT8).
RX   PubMed=6286214;
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
RT   single major actin.";
RL   Nature 284:475-477(1980).
RN   [11]
RP   PROTEIN SEQUENCE OF 120-133.
RX   PubMed=2211676;
RA   Frankel S., Condeelis J., Leinwand L.;
RT   "Expression of actin in Escherichia coli. Aggregation, solubilization,
RT   and functional analysis.";
RL   J. Biol. Chem. 265:17980-17987(1990).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 289-376 (ACT2; ACT5; ACT8
RP   AND 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
RT   determined by 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
RT   cells and localization of the phosphorylation site to tyrosine-53
RT   adjacent to the 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
RP   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
RP   ATP.
RX   PubMed=12732734; DOI=10.1073/pnas.0832273100;
RA   Vorobiev S., Strokopytov B., Drubin D.G., Frieden C., Ono S.,
RA   Condeelis J., Rubenstein P.A., Almo S.C.;
RT   "The structure of nonvertebrate actin: implications for the ATP
RT   hydrolytic mechanism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5760-5765(2003).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells. Multiple isoforms are involved in various
CC       cellular functions such as cytoskeleton structure, cell mobility,
CC       chromosome movement and muscle contraction.
CC   -!- INTERACTION:
CC       P06396:GSN (xeno); NbExp=4; IntAct=EBI-7195234, EBI-351506;
CC       P07737:PFN1 (xeno); NbExp=3; IntAct=EBI-7195234, EBI-713780;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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   SMR; P07830; -.
DR   DIP; DIP-40989N; -.
DR   IntAct; P07830; 3.
DR   MINT; P07830; -.
DR   STRING; 44689.DDB0220456; -.
DR   iPTMnet; P07830; -.
DR   SWISS-2DPAGE; P07830; -.
DR   PaxDb; P07830; -.
DR   PRIDE; P07830; -.
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   eggNOG; COG5277; LUCA.
DR   InParanoid; P07830; -.
DR   KO; K10355; -.
DR   OMA; KCDESIC; -.
DR   PhylomeDB; P07830; -.
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   Proteomes; UP000002195; Unassembled WGS sequence.
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: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:0005811; C:lipid droplet; HDA: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: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   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
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;
DR   PRODOM; Q54H30.
DR   SWISS-2DPAGE; Q54H30.
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:6892652}.
FT   CHAIN         2    376       Major actin.
FT                                /FTId=PRO_0000088926.
FT   MOD_RES      54     54       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:7498488}.
FT   CONFLICT     31     31       V -> L (in Ref. 6; CAA23479).
FT                                {ECO:0000305}.
FT   CONFLICT     32     32       F -> S (in Ref. 1; CAA27032).
FT                                {ECO:0000305}.
FT   CONFLICT     41     41       H -> Y (in Ref. 6; CAA23479).
FT                                {ECO:0000305}.
FT   CONFLICT     57     57       D -> E (in Ref. 1; CAA27032).
FT                                {ECO:0000305}.
FT   CONFLICT    109    109       A -> G (in Ref. 1; CAA27032).
FT                                {ECO:0000305}.
FT   CONFLICT    140    140       V -> A (in Ref. 1; CAA27032).
FT                                {ECO:0000305}.
FT   CONFLICT    145    145       A -> E (in Ref. 5; AAA74186).
FT                                {ECO:0000305}.
FT   CONFLICT    226    226       A -> Q (in Ref. 10; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    228    228       M -> I (in Ref. 5; AAA74186).
FT                                {ECO:0000305}.
FT   CONFLICT    229    229       Q -> A (in Ref. 10; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    313    313       R -> G (in Ref. 12; AAA51619/AAA33148/
FT                                AAA33157). {ECO:0000305}.
FT   CONFLICT    357    357       W -> L (in Ref. 12; AAA33152).
FT                                {ECO:0000305}.
FT   STRAND        4      6       {ECO:0000244|PDB:1C0F}.
FT   STRAND        9     13       {ECO:0000244|PDB:3CIP}.
FT   STRAND       15     22       {ECO:0000244|PDB:3CIP}.
FT   STRAND       25     27       {ECO:0000244|PDB:1C0G}.
FT   STRAND       29     33       {ECO:0000244|PDB:3CIP}.
FT   STRAND       36     40       {ECO:0000244|PDB:3CIP}.
FT   STRAND       43     45       {ECO:0000244|PDB:3A5O}.
FT   HELIX        57     61       {ECO:0000244|PDB:3CIP}.
FT   TURN         62     65       {ECO:0000244|PDB:3CIP}.
FT   STRAND       66     69       {ECO:0000244|PDB:3CIP}.
FT   STRAND       71     73       {ECO:0000244|PDB:1C0G}.
FT   HELIX        80     92       {ECO:0000244|PDB:3CIP}.
FT   TURN         93     95       {ECO:0000244|PDB:1NLV}.
FT   HELIX        99    101       {ECO:0000244|PDB:3CIP}.
FT   STRAND      104    108       {ECO:0000244|PDB:3CIP}.
FT   HELIX       114    126       {ECO:0000244|PDB:3CIP}.
FT   STRAND      131    137       {ECO:0000244|PDB:3CIP}.
FT   HELIX       138    145       {ECO:0000244|PDB:3CIP}.
FT   STRAND      149    156       {ECO:0000244|PDB:3CIP}.
FT   STRAND      161    167       {ECO:0000244|PDB:3CIP}.
FT   HELIX       173    175       {ECO:0000244|PDB:3CIP}.
FT   STRAND      177    180       {ECO:0000244|PDB:3CIP}.
FT   HELIX       183    196       {ECO:0000244|PDB:3CIP}.
FT   HELIX       204    217       {ECO:0000244|PDB:3CIP}.
FT   HELIX       224    233       {ECO:0000244|PDB:3CIP}.
FT   STRAND      235    237       {ECO:0000244|PDB:1NLV}.
FT   STRAND      239    242       {ECO:0000244|PDB:3CIP}.
FT   STRAND      244    246       {ECO:0000244|PDB:1NLV}.
FT   STRAND      248    251       {ECO:0000244|PDB:3CIP}.
FT   HELIX       254    263       {ECO:0000244|PDB:3CIP}.
FT   HELIX       265    268       {ECO:0000244|PDB:3CIP}.
FT   HELIX       275    284       {ECO:0000244|PDB:3CIP}.
FT   HELIX       288    290       {ECO:0000244|PDB:3CIP}.
FT   HELIX       291    295       {ECO:0000244|PDB:3CIP}.
FT   STRAND      298    302       {ECO:0000244|PDB:3CIP}.
FT   HELIX       303    305       {ECO:0000244|PDB:3CIP}.
FT   HELIX       310    321       {ECO:0000244|PDB:3CIP}.
FT   HELIX       336    338       {ECO:0000244|PDB:3CIP}.
FT   HELIX       339    349       {ECO:0000244|PDB:3CIP}.
FT   HELIX       353    355       {ECO:0000244|PDB:3CIP}.
FT   STRAND      357    359       {ECO:0000244|PDB:3CIP}.
FT   HELIX       360    366       {ECO:0000244|PDB:3CIP}.
FT   HELIX       368    370       {ECO:0000244|PDB:3CIP}.
FT   HELIX       371    374       {ECO:0000244|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
//

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