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Major actin (Actin A1) (Actin A12) (Actin A8) (Actin III) (Actin M6) (Actin-1) (Actin-11) (Actin-12) (Actin-13) (Actin-14) (Actin-15) (Actin-16) (Actin-19) (Actin-2) (Actin-2-sub 1) (Actin-20) (Actin-21) (Actin-3a) (Actin-4) (Actin-5) (Actin-6) (Actin-7) (Actin-8) (Actin-9) (Actin-IEL1)

 ACT1_DICDI              Reviewed;         376 AA.
P07830; P02577; P07827; Q23856; Q23875; Q23877; Q23879; Q23880;
Q54H30; Q7KWV6; Q94466;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
07-JUN-2017, entry version 136.
RecName: Full=Major actin;
AltName: Full=Actin A1;
AltName: Full=Actin A12;
AltName: Full=Actin A8;
AltName: Full=Actin III;
AltName: Full=Actin M6;
AltName: Full=Actin-1;
AltName: Full=Actin-11;
AltName: Full=Actin-12;
AltName: Full=Actin-13;
AltName: Full=Actin-14;
AltName: Full=Actin-15;
AltName: Full=Actin-16;
AltName: Full=Actin-19;
AltName: Full=Actin-2;
AltName: Full=Actin-2-sub 1;
AltName: Full=Actin-20;
AltName: Full=Actin-21;
AltName: Full=Actin-3a;
AltName: Full=Actin-4;
AltName: Full=Actin-5;
AltName: Full=Actin-6;
AltName: Full=Actin-7;
AltName: Full=Actin-8;
AltName: Full=Actin-9;
AltName: Full=Actin-IEL1;
Name=act1; Synonyms=act1a; ORFNames=DDB_G0289553;
and
Name=act2; Synonyms=act2-1; ORFNames=DDB_G0274133;
and
Name=act4; ORFNames=DDB_G0289005;
and
Name=act5; ORFNames=DDB_G0289663;
and
Name=act6; ORFNames=DDB_G0274135;
and
Name=act7; ORFNames=DDB_G0280545;
and
Name=act8; Synonyms=actA8; ORFNames=DDB_G0269234;
and
Name=act9; ORFNames=DDB_G0274601;
and
Name=act11; ORFNames=DDB_G0288879;
and
Name=act12; ORFNames=DDB_G0274129;
and
Name=act13; ORFNames=DDB_G0274599;
and
Name=act14; Synonyms=actB1; ORFNames=DDB_G0274137;
and
Name=act15; Synonyms=actA1; ORFNames=DDB_G0272520;
and
Name=act16; Synonyms=actM6; ORFNames=DDB_G0272248;
and
Name=act19; ORFNames=DDB_G0274727;
and
Name=act20; ORFNames=DDB_G0274285;
and
Name=act21; ORFNames=DDB_G0274561;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ACT8 AND ACT12).
PubMed=3003365; DOI=10.1016/0022-2836(85)90108-1;
Romans P., Firtel R.A.;
"Organization of the actin multigene family of Dictyostelium
discoideum and analysis of variability in the protein coding
regions.";
J. Mol. Biol. 186:321-335(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3025622; DOI=10.1128/MCB.6.11.3973;
Knecht D.A., Cohen S.M., Loomis W.F., Lodish H.F.;
"Developmental regulation of Dictyostelium discoideum actin gene
fusions carried on low-copy and high-copy transformation vectors.";
Mol. Cell. Biol. 6:3973-3983(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-260 (ACT15).
STRAIN=79A;
Zhou S.;
"A new Dictyostelium discoideum actin gene.";
Prog. Inorg. Biochem. Biophys. 15:372-376(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-68 (ACT2; ACT5; ACT7;
ACT14 AND ACT16).
PubMed=293714; DOI=10.1073/pnas.76.12.6206;
Firtel R.A., Timm R., Kimmel A.R., McKeown M.;
"Unusual nucleotide sequences at the 5' end of actin genes in
Dictyostelium discoideum.";
Proc. Natl. Acad. Sci. U.S.A. 76:6206-6210(1979).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9 (ACT8).
PubMed=6894715; DOI=10.1016/0092-8674(81)90105-7;
McKeown M., Firtel R.A.;
"Differential expression and 5' end mapping of actin genes in
Dictyostelium.";
Cell 24:799-807(1981).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-9 (ACT4).
PubMed=6297763; DOI=10.1016/0092-8674(82)90131-3;
Tsang A.S., Mahbubani H.M., Williams J.G.;
"Cell-type-specific actin mRNA populations in Dictyostelium
discoideum.";
Cell 31:375-382(1982).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 (ACT6 AND ACT8).
PubMed=6286214;
McKeown M., Firtel R.A.;
"Actin multigene family of Dictyostelium.";
Cold Spring Harb. Symp. Quant. Biol. 46:495-505(1982).
[10]
PROTEIN SEQUENCE OF 2-376.
PubMed=6892652; DOI=10.1038/284475a0;
Vandekerckhove J., Weber K.;
"Vegetative Dictyostelium cells containing 17 actin genes express a
single major actin.";
Nature 284:475-477(1980).
[11]
PROTEIN SEQUENCE OF 120-133.
PubMed=2211676;
Frankel S., Condeelis J., Leinwand L.;
"Expression of actin in Escherichia coli. Aggregation, solubilization,
and functional analysis.";
J. Biol. Chem. 265:17980-17987(1990).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 289-376 (ACT2; ACT5; ACT8
AND ACT15).
STRAIN=AX3;
PubMed=6276562; DOI=10.1016/0022-2836(81)90425-3;
McKeown M., Firtel R.A.;
"Evidence for sub-families of actin genes in Dictyostelium as
determined by comparisons of 3' end sequences.";
J. Mol. Biol. 151:593-606(1981).
[13]
PHOSPHORYLATION AT TYR-54.
PubMed=7498488; DOI=10.1016/0014-5793(95)01165-B;
Jungbluth A., Eckerskorn C., Gerisch G., Lottspeich F., Stocker S.,
Schweiger A.;
"Stress-induced tyrosine phosphorylation of actin in Dictyostelium
cells and localization of the phosphorylation site to tyrosine-53
adjacent to the DNase I binding loop.";
FEBS Lett. 375:87-90(1995).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GELSOLIN AND
ATP.
PubMed=8395021; DOI=10.1038/364685a0;
McLaughlin P.J., Gooch J.T., Mannherz H.-G., Weeds A.G.;
"Structure of gelsolin segment 1-actin complex and the mechanism of
filament severing.";
Nature 364:685-692(1993).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GELSOLIN AND
ATP.
PubMed=12732734; DOI=10.1073/pnas.0832273100;
Vorobiev S., Strokopytov B., Drubin D.G., Frieden C., Ono S.,
Condeelis J., Rubenstein P.A., Almo S.C.;
"The structure of nonvertebrate actin: implications for the ATP
hydrolytic mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 100:5760-5765(2003).
-!- FUNCTION: Actins are highly conserved proteins that are involved
in various types of cell motility and are ubiquitously expressed
in all eukaryotic cells. Multiple isoforms are involved in various
cellular functions such as cytoskeleton structure, cell mobility,
chromosome movement and muscle contraction.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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EMBL; X03281; CAA27031.1; -; Genomic_DNA.
EMBL; X03282; CAA27032.1; -; Genomic_DNA.
EMBL; M14146; AAA33145.1; -; Genomic_DNA.
EMBL; AAFI02000005; EAL71967.1; -; Genomic_DNA.
EMBL; AAFI02000008; EAL71184.1; -; Genomic_DNA.
EMBL; AAFI02000008; EAL71276.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL69957.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL69959.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL69960.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL69961.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL70035.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL70173.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL70192.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL70193.1; -; Genomic_DNA.
EMBL; AAFI02000012; EAL70256.1; -; Genomic_DNA.
EMBL; AAFI02000037; EAL67074.1; -; Genomic_DNA.
EMBL; AAFI02000126; EAL62963.1; -; Genomic_DNA.
EMBL; AAFI02000129; EAL62918.1; -; Genomic_DNA.
EMBL; AAFI02000142; EAL62666.1; -; Genomic_DNA.
EMBL; AAFI02000148; EAL62543.1; -; Genomic_DNA.
EMBL; U25660; AAA74186.1; -; Genomic_DNA.
EMBL; V00183; CAA23479.1; -; Genomic_DNA.
EMBL; V00186; CAA23482.1; -; Genomic_DNA.
EMBL; V00188; CAA23484.1; -; mRNA.
EMBL; J01267; AAA33147.1; -; Genomic_DNA.
EMBL; J01273; AAA33151.1; -; Genomic_DNA.
EMBL; J01274; AAA33153.1; -; Genomic_DNA.
EMBL; J01276; AAA51618.1; -; Genomic_DNA.
EMBL; J01279; AAA33146.1; -; Genomic_DNA.
EMBL; J01265; AAA33158.1; -; mRNA.
EMBL; J01270; AAA33159.1; -; mRNA.
EMBL; J01272; AAA33160.1; -; Genomic_DNA.
EMBL; K02954; AAA33148.1; -; Genomic_DNA.
EMBL; K02958; AAA33152.1; -; Genomic_DNA.
EMBL; K02960; AAA51619.1; -; Genomic_DNA.
EMBL; J01278; AAA33157.1; -; mRNA.
PIR; A25084; A25084.
PIR; A39239; A39239.
PIR; A93223; ATDO.
PIR; B23412; B23412.
RefSeq; XP_636088.1; XM_630996.1.
RefSeq; XP_636169.1; XM_631077.1.
RefSeq; XP_636425.1; XM_631333.1.
RefSeq; XP_636507.1; XM_631415.1.
RefSeq; XP_641146.1; XM_636054.1.
RefSeq; XP_643986.1; XM_638894.1.
RefSeq; XP_643988.1; XM_638896.1.
RefSeq; XP_643989.1; XM_638897.1.
RefSeq; XP_643990.1; XM_638898.1.
RefSeq; XP_644132.1; XM_639040.1.
RefSeq; XP_644146.1; XM_639054.1.
RefSeq; XP_644157.1; XM_639065.1.
RefSeq; XP_644244.1; XM_639152.1.
RefSeq; XP_644246.1; XM_639154.1.
RefSeq; XP_645099.1; XM_640007.1.
RefSeq; XP_645262.1; XM_640170.1.
RefSeq; XP_646688.1; XM_641596.1.
PDB; 1C0F; X-ray; 2.40 A; A=2-376.
PDB; 1C0G; X-ray; 2.00 A; A=2-376.
PDB; 1DEJ; X-ray; 2.40 A; A=2-376.
PDB; 1NLV; X-ray; 1.80 A; A=2-376.
PDB; 1NM1; X-ray; 1.80 A; A=2-376.
PDB; 1NMD; X-ray; 1.90 A; A=2-376.
PDB; 3A5L; X-ray; 2.40 A; C=2-376.
PDB; 3A5M; X-ray; 2.40 A; C=2-376.
PDB; 3A5N; X-ray; 2.36 A; C=2-376.
PDB; 3A5O; X-ray; 2.40 A; C=2-376.
PDB; 3CHW; X-ray; 2.30 A; A=2-376.
PDB; 3CI5; X-ray; 1.70 A; A=2-376.
PDB; 3CIP; X-ray; 1.60 A; A=2-376.
PDBsum; 1C0F; -.
PDBsum; 1C0G; -.
PDBsum; 1DEJ; -.
PDBsum; 1NLV; -.
PDBsum; 1NM1; -.
PDBsum; 1NMD; -.
PDBsum; 3A5L; -.
PDBsum; 3A5M; -.
PDBsum; 3A5N; -.
PDBsum; 3A5O; -.
PDBsum; 3CHW; -.
PDBsum; 3CI5; -.
PDBsum; 3CIP; -.
ProteinModelPortal; P07830; -.
SMR; P07830; -.
DIP; DIP-40989N; -.
MINT; MINT-121645; -.
STRING; 44689.DDB0220456; -.
iPTMnet; P07830; -.
SWISS-2DPAGE; P07830; -.
PaxDb; P07830; -.
PRIDE; P07830; -.
EnsemblProtists; EAL62543; EAL62543; DDB_G0289663.
EnsemblProtists; EAL62666; EAL62666; DDB_G0289553.
EnsemblProtists; EAL62918; EAL62918; DDB_G0289005.
EnsemblProtists; EAL62963; EAL62963; DDB_G0288879.
EnsemblProtists; EAL67074; EAL67074; DDB_G0280545.
EnsemblProtists; EAL69957; EAL69957; DDB_G0274129.
EnsemblProtists; EAL69959; EAL69959; DDB_G0274133.
EnsemblProtists; EAL69960; EAL69960; DDB_G0274135.
EnsemblProtists; EAL69961; EAL69961; DDB_G0274137.
EnsemblProtists; EAL70035; EAL70035; DDB_G0274285.
EnsemblProtists; EAL70173; EAL70173; DDB_G0274561.
EnsemblProtists; EAL70192; EAL70192; DDB_G0274599.
EnsemblProtists; EAL70193; EAL70193; DDB_G0274601.
EnsemblProtists; EAL70256; EAL70256; DDB_G0274727.
EnsemblProtists; EAL71184; EAL71184; DDB_G0272520.
EnsemblProtists; EAL71276; EAL71276; DDB_G0272248.
EnsemblProtists; EAL71967; EAL71967; DDB_G0269234.
GeneID; 8617663; -.
GeneID; 8618428; -.
GeneID; 8618493; -.
GeneID; 8619412; -.
GeneID; 8619414; -.
GeneID; 8619415; -.
GeneID; 8619416; -.
GeneID; 8619562; -.
GeneID; 8619575; -.
GeneID; 8619586; -.
GeneID; 8619672; -.
GeneID; 8619674; -.
GeneID; 8622703; -.
GeneID; 8626890; -.
GeneID; 8626916; -.
GeneID; 8627198; -.
GeneID; 8627300; -.
KEGG; ddi:DDB_G0269234; -.
KEGG; ddi:DDB_G0272248; -.
KEGG; ddi:DDB_G0272520; -.
KEGG; ddi:DDB_G0274129; -.
KEGG; ddi:DDB_G0274133; -.
KEGG; ddi:DDB_G0274135; -.
KEGG; ddi:DDB_G0274137; -.
KEGG; ddi:DDB_G0274285; -.
KEGG; ddi:DDB_G0274561; -.
KEGG; ddi:DDB_G0274599; -.
KEGG; ddi:DDB_G0274601; -.
KEGG; ddi:DDB_G0274727; -.
KEGG; ddi:DDB_G0280545; -.
KEGG; ddi:DDB_G0288879; -.
KEGG; ddi:DDB_G0289005; -.
KEGG; ddi:DDB_G0289553; -.
KEGG; ddi:DDB_G0289663; -.
dictyBase; DDB_G0289553; act1.
dictyBase; DDB_G0288879; act11.
dictyBase; DDB_G0274129; act12.
dictyBase; DDB_G0274599; act13.
dictyBase; DDB_G0274137; act14.
dictyBase; DDB_G0272520; act15.
dictyBase; DDB_G0272248; act16.
dictyBase; DDB_G0274727; act19.
dictyBase; DDB_G0274133; act2.
dictyBase; DDB_G0274285; act20.
dictyBase; DDB_G0274561; act21.
dictyBase; DDB_G0289005; act4.
dictyBase; DDB_G0289663; act5.
dictyBase; DDB_G0274135; act6.
dictyBase; DDB_G0280545; act7.
dictyBase; DDB_G0269234; act8.
dictyBase; DDB_G0274601; act9.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
InParanoid; P07830; -.
KO; K10355; -.
OMA; ANGIHET; -.
PhylomeDB; P07830; -.
EvolutionaryTrace; P07830; -.
PRO; PR:P07830; -.
Proteomes; UP000002195; Chromosome 1.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Chromosome 3.
Proteomes; UP000002195; Chromosome 5.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
GO; GO:0005884; C:actin filament; IDA:dictyBase.
GO; GO:0031252; C:cell leading edge; TAS:dictyBase.
GO; GO:0060187; C:cell pole; IDA:dictyBase.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
GO; GO:0032009; C:early phagosome; IDA:dictyBase.
GO; GO:0061836; C:intranuclear rod; IDA:dictyBase.
GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
GO; GO:0032010; C:phagolysosome; IDA:dictyBase.
GO; GO:0031143; C:pseudopodium; TAS:dictyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017022; F:myosin binding; IDA:dictyBase.
GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:dictyBase.
GO; GO:0000902; P:cell morphogenesis; TAS:dictyBase.
GO; GO:0006935; P:chemotaxis; TAS:dictyBase.
GO; GO:0006897; P:endocytosis; TAS:dictyBase.
GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
GO; GO:0000281; P:mitotic cytokinesis; TAS:dictyBase.
GO; GO:0006909; P:phagocytosis; IEP:dictyBase.
GO; GO:0042331; P:phototaxis; TAS:dictyBase.
GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
GO; GO:0016192; P:vesicle-mediated transport; TAS:dictyBase.
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; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6892652}.
CHAIN 2 376 Major actin.
/FTId=PRO_0000088926.
MOD_RES 54 54 Phosphotyrosine.
{ECO:0000269|PubMed:7498488}.
CONFLICT 31 31 V -> L (in Ref. 6; CAA23479).
{ECO:0000305}.
CONFLICT 32 32 F -> S (in Ref. 1; CAA27032).
{ECO:0000305}.
CONFLICT 41 41 H -> Y (in Ref. 6; CAA23479).
{ECO:0000305}.
CONFLICT 57 57 D -> E (in Ref. 1; CAA27032).
{ECO:0000305}.
CONFLICT 109 109 A -> G (in Ref. 1; CAA27032).
{ECO:0000305}.
CONFLICT 140 140 V -> A (in Ref. 1; CAA27032).
{ECO:0000305}.
CONFLICT 145 145 A -> E (in Ref. 5; AAA74186).
{ECO:0000305}.
CONFLICT 226 226 A -> Q (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 228 228 M -> I (in Ref. 5; AAA74186).
{ECO:0000305}.
CONFLICT 229 229 Q -> A (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 313 313 R -> G (in Ref. 12; AAA51619/AAA33148/
AAA33157). {ECO:0000305}.
CONFLICT 357 357 W -> L (in Ref. 12; AAA33152).
{ECO:0000305}.
STRAND 4 6 {ECO:0000244|PDB:1C0F}.
STRAND 9 13 {ECO:0000244|PDB:3CIP}.
STRAND 15 22 {ECO:0000244|PDB:3CIP}.
STRAND 25 27 {ECO:0000244|PDB:1C0G}.
STRAND 29 33 {ECO:0000244|PDB:3CIP}.
STRAND 36 40 {ECO:0000244|PDB:3CIP}.
STRAND 43 45 {ECO:0000244|PDB:3A5O}.
HELIX 57 61 {ECO:0000244|PDB:3CIP}.
TURN 62 65 {ECO:0000244|PDB:3CIP}.
STRAND 66 69 {ECO:0000244|PDB:3CIP}.
STRAND 71 73 {ECO:0000244|PDB:1C0G}.
HELIX 80 92 {ECO:0000244|PDB:3CIP}.
TURN 93 95 {ECO:0000244|PDB:1NLV}.
HELIX 99 101 {ECO:0000244|PDB:3CIP}.
STRAND 104 108 {ECO:0000244|PDB:3CIP}.
HELIX 114 126 {ECO:0000244|PDB:3CIP}.
STRAND 131 137 {ECO:0000244|PDB:3CIP}.
HELIX 138 145 {ECO:0000244|PDB:3CIP}.
STRAND 149 156 {ECO:0000244|PDB:3CIP}.
STRAND 161 167 {ECO:0000244|PDB:3CIP}.
HELIX 173 175 {ECO:0000244|PDB:3CIP}.
STRAND 177 180 {ECO:0000244|PDB:3CIP}.
HELIX 183 196 {ECO:0000244|PDB:3CIP}.
HELIX 204 217 {ECO:0000244|PDB:3CIP}.
HELIX 224 233 {ECO:0000244|PDB:3CIP}.
STRAND 235 237 {ECO:0000244|PDB:1NLV}.
STRAND 239 242 {ECO:0000244|PDB:3CIP}.
STRAND 244 246 {ECO:0000244|PDB:1NLV}.
STRAND 248 251 {ECO:0000244|PDB:3CIP}.
HELIX 254 263 {ECO:0000244|PDB:3CIP}.
HELIX 265 268 {ECO:0000244|PDB:3CIP}.
HELIX 275 284 {ECO:0000244|PDB:3CIP}.
HELIX 288 290 {ECO:0000244|PDB:3CIP}.
HELIX 291 295 {ECO:0000244|PDB:3CIP}.
STRAND 298 302 {ECO:0000244|PDB:3CIP}.
HELIX 303 305 {ECO:0000244|PDB:3CIP}.
HELIX 310 321 {ECO:0000244|PDB:3CIP}.
HELIX 336 338 {ECO:0000244|PDB:3CIP}.
HELIX 339 349 {ECO:0000244|PDB:3CIP}.
HELIX 353 355 {ECO:0000244|PDB:3CIP}.
STRAND 357 359 {ECO:0000244|PDB:3CIP}.
HELIX 360 366 {ECO:0000244|PDB:3CIP}.
HELIX 368 370 {ECO:0000244|PDB:3CIP}.
HELIX 371 374 {ECO:0000244|PDB:3CIP}.
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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