FUS3_YEAST
ID FUS3_YEAST Reviewed; 353 AA.
AC P16892; D6VPY4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Mitogen-activated protein kinase FUS3;
DE Short=MAP kinase FUS3;
DE EC=2.7.11.24;
GN Name=FUS3; Synonyms=DAC2; OrderedLocusNames=YBL016W;
GN ORFNames=YBL03.21, YBL0303;
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=2406028; DOI=10.1016/0092-8674(90)90668-5;
RA Elion E.A., Grisafi P.L., Fink G.R.;
RT "FUS3 encodes a cdc2+/CDC28-related kinase required for the transition from
RT mitosis into conjugation.";
RL Cell 60:649-664(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1465115; DOI=10.1007/bf00279392;
RA Fujimura H.A.;
RT "The DAC2/FUS3 protein kinase is not essential for transcriptional
RT activation of the mating pheromone response pathway in Saccharomyces
RT cerevisiae.";
RL Mol. Gen. Genet. 235:450-452(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441754; DOI=10.1002/yea.320080910;
RA van Dyck L., Purnelle B., Skala J., Goffeau A.;
RT "An 11.4 kb DNA segment on the left arm of yeast chromosome II carries the
RT carboxypeptidase Y sorting gene PEP1, as well as ACH1, FUS3 and a putative
RT ARS.";
RL Yeast 8:769-776(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP PHOSPHORYLATION AT THR-180 AND TYR-182.
RX PubMed=1628831; DOI=10.1101/gad.6.7.1280;
RA Gartner A., Nasmyth K., Ammerer G.;
RT "Signal transduction in Saccharomyces cerevisiae requires tyrosine and
RT threonine phosphorylation of FUS3 and KSS1.";
RL Genes Dev. 6:1280-1292(1992).
RN [8]
RP FUNCTION, AND REGULATION OF STE12 ACTIVITY.
RX PubMed=9393860; DOI=10.1016/s0092-8674(00)80454-7;
RA Madhani H.D., Styles C.A., Fink G.R.;
RT "MAP kinases with distinct inhibitory functions impart signaling
RT specificity during yeast differentiation.";
RL Cell 91:673-684(1997).
RN [9]
RP FUNCTION, AND COMPLEX WITH DIG1; DIG2 AND STE12.
RX PubMed=9094309; DOI=10.1016/s0960-9822(06)00118-7;
RA Tedford K., Kim S., Sa D., Stevens K., Tyers M.;
RT "Regulation of the mating pheromone and invasive growth responses in yeast
RT by two MAP kinase substrates.";
RL Curr. Biol. 7:228-238(1997).
RN [10]
RP FUNCTION, AND REGULATION OF KSS1 ACTIVITY.
RX PubMed=11583629; DOI=10.1016/s1097-2765(01)00322-7;
RA Sabbagh W. Jr., Flatauer L.J., Bardwell A.J., Bardwell L.;
RT "Specificity of MAP kinase signaling in yeast differentiation involves
RT transient versus sustained MAPK activation.";
RL Mol. Cell 8:683-691(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=11781566; DOI=10.1038/ncb1201-1051;
RA van Drogen F., Stucke V.M., Jorritsma G., Peter M.;
RT "MAP kinase dynamics in response to pheromones in budding yeast.";
RL Nat. Cell Biol. 3:1051-1059(2001).
RN [12]
RP FUNCTION, AND REGULATION OF STE12 PROMOTER SELECTIVITY.
RX PubMed=12732146; DOI=10.1016/s0092-8674(03)00301-5;
RA Zeitlinger J., Simon I., Harbison C.T., Hannett N.M., Volkert T.L.,
RA Fink G.R., Young R.A.;
RT "Program-specific distribution of a transcription factor dependent on
RT partner transcription factor and MAPK signaling.";
RL Cell 113:395-404(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
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 [16]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-345, 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).
CC -!- FUNCTION: Together with closely related KSS1, FUS3 is the final kinase
CC in the signal transduction cascade regulating activation/repression of
CC the mating and filamentation pathways, induced by pheromone and
CC nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates
CC the mating but suppresses the filamentation pathway, whereas activated
CC KSS1 activates both pathways. Pheromone-activated FUS3 functions by
CC inhibiting the binding of the transcriptional activator STE12 to
CC filamentation specific genes while inducing its binding to and activity
CC at mating specific genes. Non-activated FUS3 has a repressive effect on
CC STE12 transcriptional activity. KSS1 can partially compensate for the
CC lack of FUS3 but mating efficiency is reduced and the filamentation
CC program is partially activated upon pheromone signaling. FUS3
CC phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.
CC {ECO:0000269|PubMed:11583629, ECO:0000269|PubMed:12732146,
CC ECO:0000269|PubMed:9094309, ECO:0000269|PubMed:9393860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC phosphorylation after pheromone treatment.
CC -!- SUBUNIT: In the nucleus, FUS3 forms a complex with DIG1, DIG2 and
CC STE12. The interaction of FUS3 with STE12 depends on the presence of
CC both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after
CC pheromone treatment. During its activation and phosphorylation, FUS3
CC forms a membrane-associated complex with the scaffold protein STE5, the
CC MAPKK STE7, the MAPKKK STE11, and the G-protein beta subunit GBB/STE4;
CC interacting directly with STE7 and STE5.
CC -!- INTERACTION:
CC P16892; P33306: BCK2; NbExp=2; IntAct=EBI-7193, EBI-3480;
CC P16892; P16892: FUS3; NbExp=2; IntAct=EBI-7193, EBI-7193;
CC P16892; P23561: STE11; NbExp=6; IntAct=EBI-7193, EBI-18259;
CC P16892; P32917: STE5; NbExp=11; IntAct=EBI-7193, EBI-18373;
CC P16892; P06784: STE7; NbExp=15; IntAct=EBI-7193, EBI-18389;
CC P16892; P32830: TIM12; NbExp=2; IntAct=EBI-7193, EBI-11303;
CC P16892; A7TJH8: Kpol_1061p54; Xeno; NbExp=2; IntAct=EBI-7193, EBI-8783719;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11781566}. Cytoplasm
CC {ECO:0000269|PubMed:11781566}. Periplasm {ECO:0000269|PubMed:11781566}.
CC Note=FUS3 shuttles rapidly between the cytoplasm and the nucleus
CC independent of pheromone treatment or FUS3 phosphorylation level.
CC Activated FUS3 translocates rapidly to the nucleus.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-180 and Tyr-182 by STE7 in response
CC to pheromone induction, which activates the enzyme. Activated FUS3
CC initiates a feedback signal, down-regulating phosphorylation of both,
CC FUS3 and KSS1. {ECO:0000269|PubMed:1628831}.
CC -!- MISCELLANEOUS: Present with 8480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; M31132; AAA34613.1; -; Genomic_DNA.
DR EMBL; X69572; CAA49292.1; -; Genomic_DNA.
DR EMBL; X68577; CAA48569.1; -; Genomic_DNA.
DR EMBL; Z35777; CAA84835.1; -; Genomic_DNA.
DR EMBL; AY693096; AAT93115.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07104.1; -; Genomic_DNA.
DR PIR; S28548; S28548.
DR RefSeq; NP_009537.1; NM_001178256.1.
DR PDB; 2B9F; X-ray; 1.80 A; A=1-353.
DR PDB; 2B9H; X-ray; 1.55 A; A=1-353.
DR PDB; 2B9I; X-ray; 2.50 A; A=1-353.
DR PDB; 2B9J; X-ray; 2.30 A; A=1-353.
DR PDB; 2F49; X-ray; 1.90 A; A/B=1-353.
DR PDB; 2F9G; X-ray; 2.10 A; A=1-353.
DR PDB; 2FA2; X-ray; 2.85 A; A/B=1-353.
DR PDBsum; 2B9F; -.
DR PDBsum; 2B9H; -.
DR PDBsum; 2B9I; -.
DR PDBsum; 2B9J; -.
DR PDBsum; 2F49; -.
DR PDBsum; 2F9G; -.
DR PDBsum; 2FA2; -.
DR AlphaFoldDB; P16892; -.
DR SMR; P16892; -.
DR BioGRID; 32682; 430.
DR DIP; DIP-714N; -.
DR ELM; P16892; -.
DR IntAct; P16892; 35.
DR MINT; P16892; -.
DR STRING; 4932.YBL016W; -.
DR iPTMnet; P16892; -.
DR MaxQB; P16892; -.
DR PaxDb; P16892; -.
DR PRIDE; P16892; -.
DR EnsemblFungi; YBL016W_mRNA; YBL016W; YBL016W.
DR GeneID; 852265; -.
DR KEGG; sce:YBL016W; -.
DR SGD; S000000112; FUS3.
DR VEuPathDB; FungiDB:YBL016W; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P16892; -.
DR OMA; IFHPHPP; -.
DR BioCyc; YEAST:G3O-28920-MON; -.
DR BRENDA; 2.7.11.24; 984.
DR Reactome; R-SCE-110056; MAPK3 (ERK1) activation.
DR Reactome; R-SCE-111995; phospho-PLA2 pathway.
DR Reactome; R-SCE-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-SCE-112411; MAPK1 (ERK2) activation.
DR Reactome; R-SCE-170968; Frs2-mediated activation.
DR Reactome; R-SCE-198753; ERK/MAPK targets.
DR Reactome; R-SCE-202670; ERKs are inactivated.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SCE-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-SCE-437239; Recycling pathway of L1.
DR Reactome; R-SCE-445144; Signal transduction by L1.
DR Reactome; R-SCE-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-SCE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-SCE-5674135; MAP2K and MAPK activation.
DR Reactome; R-SCE-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9634635; Estrogen-stimulated signaling through PRKCZ.
DR EvolutionaryTrace; P16892; -.
DR PRO; PR:P16892; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P16892; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004707; F:MAP kinase activity; IDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IPI:SGD.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:SGD.
DR GO; GO:0071507; P:pheromone response MAPK cascade; IDA:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IDA:SGD.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR DisProt; DP02784; -.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Conjugation;
KW Cytoplasm; Isopeptide bond; Kinase; Mitosis; Nucleotide-binding; Nucleus;
KW Periplasm; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..353
FT /note="Mitogen-activated protein kinase FUS3"
FT /id="PRO_0000186326"
FT DOMAIN 13..309
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 180..182
FT /note="TXY"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:1628831"
FT MOD_RES 182
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:1628831"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 334
FT /note="Y -> H (in Ref. 1; AAA34613)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:2F49"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:2B9H"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:2B9H"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2B9H"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:2B9H"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2B9H"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2B9F"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2B9H"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 111..130
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2B9H"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2B9H"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2B9F"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2F49"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 202..218
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:2B9H"
FT TURN 245..250
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2B9H"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:2B9H"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:2B9H"
SQ SEQUENCE 353 AA; 40772 MW; 5117980D20A1E7E2 CRC64;
MPKRIVYNIS SDFQLKSLLG EGAYGVVCSA THKPTGEIVA IKKIEPFDKP LFALRTLREI
KILKHFKHEN IITIFNIQRP DSFENFNEVY IIQELMQTDL HRVISTQMLS DDHIQYFIYQ
TLRAVKVLHG SNVIHRDLKP SNLLINSNCD LKVCDFGLAR IIDESAADNS EPTGQQSGMT
EYVATRWYRA PEVMLTSAKY SRAMDVWSCG CILAELFLRR PIFPGRDYRH QLLLIFGIIG
TPHSDNDLRC IESPRAREYI KSLPMYPAAP LEKMFPRVNP KGIDLLQRML VFDPAKRITA
KEALEHPYLQ TYHDPNDEPE GEPIPPSFFE FDHYKEALTT KDLKKLIWNE IFS
