ACT_YEAST
ID ACT_YEAST Reviewed; 375 AA.
AC P60010; D6VTJ1; P02579; Q9P3X6; Q9P3X7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Actin;
GN Name=ACT1; Synonyms=ABY1, END7; OrderedLocusNames=YFL039C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6994099; DOI=10.1073/pnas.77.5.2546;
RA Gallwitz D., Sures I.;
RT "Structure of a split yeast gene: complete nucleotide sequence of the actin
RT gene in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2546-2550(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7001447; DOI=10.1073/pnas.77.7.3912;
RA Ng R., Abelson J.;
RT "Isolation and sequence of the gene for actin in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:3912-3916(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-58.
RX PubMed=6096014; DOI=10.1016/0092-8674(84)90468-9;
RA Domdey H., Apostol B., Lin R.J., Newman A., Brody E., Abelson J.;
RT "Lariat structures are in vivo intermediates in yeast pre-mRNA splicing.";
RL Cell 39:611-621(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-57.
RX PubMed=7003553; DOI=10.1093/nar/8.5.1043;
RA Gallwitz D., Seidel R.;
RT "Molecular cloning of the actin gene from yeast Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 8:1043-1059(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Carlsbergensis;
RX PubMed=6286825;
RA Nellen W., Donath C., Moos M., Gallwitz D.;
RT "The nucleotide sequences of the actin genes from Saccharomyces
RT carlsbergensis and Saccharomyces cerevisiae are identical except for their
RT introns.";
RL J. Mol. Appl. Genet. 1:239-244(1981).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-358.
RC STRAIN=ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632, and
RC CBS 1907;
RX PubMed=11491363; DOI=10.1099/00207713-51-4-1593;
RA Daniel H.-M., Sorrell T.C., Meyer W.;
RT "Partial sequence analysis of the actin gene and its potential for studying
RT the phylogeny of Candida species and their teleomorphs.";
RL Int. J. Syst. Evol. Microbiol. 51:1593-1606(2001).
RN [9]
RP ACETYLATION AT MET-1, AND PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=1885608; DOI=10.1016/s0021-9258(18)55376-x;
RA Cook R.K., Sheff D.R., Rubenstein P.A.;
RT "Unusual metabolism of the yeast actin amino terminus.";
RL J. Biol. Chem. 266:16825-16833(1991).
RN [10]
RP PROTEIN SEQUENCE OF 19-25.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [11]
RP MUTAGENESIS.
RX PubMed=1935913; DOI=10.1002/j.1460-2075.1991.tb04965.x;
RA Johannes F.-Z., Gallwitz D.;
RT "Site-directed mutagenesis of the yeast actin gene: a test for actin
RT function in vivo.";
RL EMBO J. 10:3951-3958(1991).
RN [12]
RP INTERACTION WITH YIH1.
RX PubMed=15126500; DOI=10.1074/jbc.m404009200;
RA Sattlegger E., Swanson M.J., Ashcraft E.A., Jennings J.L., Fekete R.A.,
RA Link A.J., Hinnebusch A.G.;
RT "YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and
RT impairs general amino acid control when overexpressed.";
RL J. Biol. Chem. 279:29952-29962(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP INTERACTION WITH YIH1.
RX PubMed=21239490; DOI=10.1074/jbc.m110.171587;
RA Sattlegger E., Barbosa J.A., Moraes M.C., Martins R.M., Hinnebusch A.G.,
RA Castilho B.A.;
RT "Gcn1 and actin binding to Yih1: implications for activation of the eIF2
RT kinase GCN2.";
RL J. Biol. Chem. 286:10341-10355(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND LACK OF METHYLATION AT HIS-73.
RX PubMed=10496983; DOI=10.1006/abbi.1999.1370;
RA Kalhor H.R., Niewmierzycka A., Faull K.F., Yao X., Grade S., Clarke S.,
RA Rubenstein P.A.;
RT "A highly conserved 3-methylhistidine modification is absent in yeast
RT actin.";
RL Arch. Biochem. Biophys. 370:105-111(1999).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [19]
RP SUBUNIT, AND MUTAGENESIS OF ARG-183 AND ARG-335.
RX PubMed=28796488; DOI=10.1021/acschembio.7b00385;
RA Filipuzzi I., Thomas J.R., Pries V., Estoppey D., Salcius M., Studer C.,
RA Schirle M., Hoepfner D.;
RT "Direct Interaction of Chivosazole F with Actin Elicits Cell Responses
RT Similar to Latrunculin A but Distinct from Chondramide.";
RL ACS Chem. Biol. 12:2264-2269(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
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.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix
CC (Probable). Treatments with Lantrunculin A, the microbial peptide
CC Chondramide or the microbial metabolite Chivazole F inhibit actin
CC polymerization (PubMed:28796488). Each actin can bind to 4 others.
CC Interacts with YIH1 (via C-terminus); this interaction occurs in a
CC GCN1-independent manner (PubMed:15126500, PubMed:21239490). Component
CC of the INO80 complex. Component of the SWR1 complex. Component of the
CC NuA4 complex. {ECO:0000269|PubMed:15126500,
CC ECO:0000269|PubMed:21239490, ECO:0000269|PubMed:28796488, ECO:0000305}.
CC -!- INTERACTION:
CC P60010; P60010: ACT1; NbExp=6; IntAct=EBI-2169, EBI-2169;
CC P60010; P46680: AIP1; NbExp=3; IntAct=EBI-2169, EBI-2406;
CC P60010; Q03048: COF1; NbExp=3; IntAct=EBI-2169, EBI-4853;
CC P60010; Q06440: CRN1; NbExp=3; IntAct=EBI-2169, EBI-4950;
CC P60010; P02829: HSP82; NbExp=2; IntAct=EBI-2169, EBI-8659;
CC P60010; Q12446: LAS17; NbExp=4; IntAct=EBI-2169, EBI-10022;
CC P60010; P07274: PFY1; NbExp=4; IntAct=EBI-2169, EBI-13892;
CC P60010; P39743: RVS167; NbExp=4; IntAct=EBI-2169, EBI-14500;
CC P60010; P32599: SAC6; NbExp=4; IntAct=EBI-2169, EBI-6931;
CC P60010; P17555: SRV2; NbExp=7; IntAct=EBI-2169, EBI-4024;
CC P60010; P12612: TCP1; NbExp=3; IntAct=EBI-2169, EBI-19045;
CC P60010; P0A6F5: groEL; Xeno; NbExp=5; IntAct=EBI-2169, EBI-543750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; V01288; CAA24597.1; -; Genomic_DNA.
DR EMBL; V01289; CAA24598.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V01290; CAA24599.1; -; Genomic_DNA.
DR EMBL; L00026; AAA34391.1; -; Genomic_DNA.
DR EMBL; D50617; BAA21512.1; -; Genomic_DNA.
DR EMBL; AJ389075; CAC00716.1; -; Genomic_DNA.
DR EMBL; AJ389076; CAC00717.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12401.1; -; Genomic_DNA.
DR PIR; A03005; ATBY.
DR PIR; JS0702; JS0702.
DR RefSeq; NP_116614.1; NM_001179927.1.
DR PDB; 1YAG; X-ray; 1.90 A; A=1-375.
DR PDB; 1YVN; X-ray; 2.10 A; A=1-375.
DR PDB; 5NBL; X-ray; 2.80 A; C/D=1-375.
DR PDB; 5NBM; X-ray; 3.40 A; C/D=1-375.
DR PDB; 5NBN; X-ray; 4.00 A; C/D=1-375.
DR PDB; 5Y81; EM; 4.70 A; G=1-375.
DR PDBsum; 1YAG; -.
DR PDBsum; 1YVN; -.
DR PDBsum; 5NBL; -.
DR PDBsum; 5NBM; -.
DR PDBsum; 5NBN; -.
DR PDBsum; 5Y81; -.
DR AlphaFoldDB; P60010; -.
DR SMR; P60010; -.
DR BioGRID; 31107; 2326.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR DIP; DIP-310N; -.
DR IntAct; P60010; 238.
DR MINT; P60010; -.
DR STRING; 4932.YFL039C; -.
DR BindingDB; P60010; -.
DR MoonDB; P60010; Predicted.
DR CarbonylDB; P60010; -.
DR iPTMnet; P60010; -.
DR SWISS-2DPAGE; P60010; -.
DR MaxQB; P60010; -.
DR PaxDb; P60010; -.
DR PRIDE; P60010; -.
DR ABCD; P60010; 1 sequenced antibody.
DR EnsemblFungi; YFL039C_mRNA; YFL039C; YFL039C.
DR GeneID; 850504; -.
DR KEGG; sce:YFL039C; -.
DR SGD; S000001855; ACT1.
DR VEuPathDB; FungiDB:YFL039C; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P60010; -.
DR OMA; FHTTAER; -.
DR BioCyc; YEAST:G3O-30423-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-196025; Formation of annular gap junctions.
DR Reactome; R-SCE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SCE-5663213; RHO GTPases Activate WASPs and WAVEs.
DR EvolutionaryTrace; P60010; -.
DR PRO; PR:P60010; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P60010; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005884; C:actin filament; IDA:SGD.
DR GO; GO:0032432; C:actin filament bundle; IDA:SGD.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0031011; C:Ino80 complex; IPI:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IMP:SGD.
DR GO; GO:0009306; P:protein secretion; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
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; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Nucleotide-binding;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..375
FT /note="Actin"
FT /id="PRO_0000089051"
FT SITE 73
FT /note="Not methylated"
FT /evidence="ECO:0000269|PubMed:10496983"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:1885608,
FT ECO:0007744|PubMed:22814378"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT VARIANT 143
FT /note="Y -> F (in strain: CBS 1907)"
FT MUTAGEN 183
FT /note="R->K: No effect on growth kinetics nor on actin
FT cytoskeleton morphology. Resistant to Chivosazole F
FT inhibition of polymerization. Increases penetrance of
FT Latrunculin A inhibition of polymerization. No effect on
FT Chondramide inhibition of polymerization."
FT /evidence="ECO:0000269|PubMed:28796488"
FT MUTAGEN 335
FT /note="R->K: No effect on growth kinetics nor on actin
FT cytoskeleton morphology. Resistant to Chivosazole F and
FT Latrunculin A inhibition of polymerization. No effect on
FT Chondramide inhibition of polymerization."
FT /evidence="ECO:0000269|PubMed:28796488"
FT CONFLICT 178
FT /note="I -> L (in Ref. 2; CAA24598)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="G -> S (in Ref. 2; CAA24598)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:5NBM"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1YAG"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1YVN"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1YVN"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1YVN"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1YAG"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:1YAG"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:1YAG"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5NBM"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 350..354
FT /evidence="ECO:0007829|PDB:1YAG"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1YAG"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:1YAG"
SQ SEQUENCE 375 AA; 41690 MW; 87AC19B0B0BC9E71 CRC64;
MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS
KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPM NPKSNREKMT
QIMFETFNVP AFYVSIQAVL SLYSSGRTTG IVLDSGDGVT HVVPIYAGFS LPHAILRIDL
AGRDLTDYLM KILSERGYSF STTAEREIVR DIKEKLCYVA LDFEQEMQTA AQSSSIEKSY
ELPDGQVITI GNERFRAPEA LFHPSVLGLE SAGIDQTTYN SIMKCDVDVR KELYGNIVMS
GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT TFQQMWISKQ
EYDESGPSIV HHKCF
