TUP1_YEAST
ID TUP1_YEAST Reviewed; 713 AA.
AC P16649; D6VR85; P17995; P18323;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=General transcriptional corepressor TUP1;
DE AltName: Full=Flocculation suppressor protein;
DE AltName: Full=Glucose repression regulatory protein TUP1;
DE AltName: Full=Repressor AER2;
GN Name=TUP1; Synonyms=AAR1, AER2, AMM1, CYC9, FLK1, SFL2, UMR7;
GN OrderedLocusNames=YCR084C; ORFNames=YCR84C;
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], AND FUNCTION.
RX PubMed=2247069; DOI=10.1128/mcb.10.12.6500-6511.1990;
RA Williams F.E., Trumbly R.J.;
RT "Characterization of TUP1, a mediator of glucose repression in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 10:6500-6511(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1900249; DOI=10.1016/0378-1119(91)90047-f;
RA Zhang M., Rosenblum-Vos L.S., Lowry C.V., Boakye K., Zitomer R.S.;
RT "A yeast protein with homology to the beta-subunit of G proteins is
RT involved in control of heme-regulated and catabolite-repressed genes.";
RL Gene 97:153-161(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44774 / DBY747;
RX PubMed=2197185; DOI=10.1016/0378-1119(90)90210-i;
RA Fujita A., Matsumoto S., Kuhara S., Misumi Y., Kobayashi H.;
RT "Cloning of the yeast SFL2 gene: its disruption results in pleiotropic
RT phenotypes characteristic for tup1 mutants.";
RL Gene 89:93-99(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 SIMILARITY TO BETA SUBUNIT OF G-PROTEINS.
RX PubMed=1901558; DOI=10.1016/0378-1119(91)90118-u;
RA Kearsley S.;
RT "The SFL2 (TUP1?) protein of Saccharomyces cerevisiae contains a repeating
RT motif homologous to beta subunits of G proteins.";
RL Gene 98:147-148(1991).
RN [7]
RP INTERACTION WITH MATALPHA2.
RX PubMed=7995523; DOI=10.1101/gad.8.23.2857;
RA Komachi K., Redd M.J., Johnson A.D.;
RT "The WD repeats of Tup1 interact with the homeo domain protein alpha 2.";
RL Genes Dev. 8:2857-2867(1994).
RN [8]
RP INTERACTION WITH HISTONE H3 AND HISTONE H4.
RX PubMed=8675011; DOI=10.1101/gad.10.10.1247;
RA Edmondson D.G., Smith M.M., Roth S.Y.;
RT "Repression domain of the yeast global repressor Tup1 interacts directly
RT with histones H3 and H4.";
RL Genes Dev. 10:1247-1259(1996).
RN [9]
RP SUBUNIT.
RX PubMed=8943325; DOI=10.1128/mcb.16.12.6707;
RA Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.;
RT "The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four
RT Tup1 subunits.";
RL Mol. Cell. Biol. 16:6707-6714(1996).
RN [10]
RP INTERACTION WITH RFX1.
RX PubMed=9741624; DOI=10.1016/s0092-8674(00)81601-3;
RA Huang M., Zhou Z., Elledge S.J.;
RT "The DNA replication and damage checkpoint pathways induce transcription by
RT inhibition of the Crt1 repressor.";
RL Cell 94:595-605(1998).
RN [11]
RP INTERACTION WITH CYC8 AND RPD3, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
RX PubMed=11069890; DOI=10.1101/gad.829100;
RA Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W.,
RA Stillman D.J., Roth S.Y.;
RT "Ssn6-Tup1 interacts with class I histone deacetylases required for
RT repression.";
RL Genes Dev. 14:2737-2744(2000).
RN [12]
RP INTERACTION WITH PGD1, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
RX PubMed=10722672; DOI=10.1074/jbc.275.12.8397;
RA Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.;
RT "Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II
RT holoenzyme.";
RL J. Biol. Chem. 275:8397-8403(2000).
RN [13]
RP FUNCTION OF THE CYC8-TUP1 COMPLEX.
RX PubMed=11230135; DOI=10.1093/emboj/20.5.1123;
RA Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.;
RT "Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in
RT response to osmotic stress.";
RL EMBO J. 20:1123-1133(2001).
RN [14]
RP INTERACTION WITH SKO1.
RX PubMed=11500510; DOI=10.1074/jbc.m105755200;
RA Pascual-Ahuir A., Posas F., Serrano R., Proft M.;
RT "Multiple levels of control regulate the yeast cAMP-response element-
RT binding protein repressor Sko1p in response to stress.";
RL J. Biol. Chem. 276:37373-37378(2001).
RN [15]
RP INTERACTION WITH HDA1 AND HDA2, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
RX PubMed=11172717; DOI=10.1016/s1097-2765(01)00160-5;
RA Wu J., Suka N., Carlson M., Grunstein M.;
RT "TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene
RT activity in yeast.";
RL Mol. Cell 7:117-126(2001).
RN [16]
RP FUNCTION OF THE CYC8-TUP1 COMPLEX.
RX PubMed=11784848; DOI=10.1128/mcb.22.3.693-703.2002;
RA Davie J.K., Trumbly R.J., Dent S.Y.;
RT "Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo.";
RL Mol. Cell. Biol. 22:693-703(2002).
RN [17]
RP FUNCTION OF THE CYC8-TUP1 COMPLEX.
RX PubMed=14665463; DOI=10.1128/ec.2.6.1288-1303.2003;
RA Mennella T.A., Klinkenberg L.G., Zitomer R.S.;
RT "Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent
RT exclusion of TATA binding protein.";
RL Eukaryot. Cell 2:1288-1303(2003).
RN [18]
RP INTERACTION WITH HOS1; HOS2 AND RPD3.
RX PubMed=14525981; DOI=10.1074/jbc.m309753200;
RA Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.;
RT "Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.";
RL J. Biol. Chem. 278:50158-50162(2003).
RN [19]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [20]
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 [21]
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 [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY
RP 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 [24]
RP IDENTIFICATION BY MASS 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 [25]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 282-713.
RX PubMed=10856245; DOI=10.1093/emboj/19.12.3016;
RA Sprague E.R., Redd M.J., Johnson A.D., Wolberger C.;
RT "Structure of the C-terminal domain of Tup1, a corepressor of transcription
RT in yeast.";
RL EMBO J. 19:3016-3027(2000).
CC -!- FUNCTION: Acts as component of the CYC8-TUP1 corepressor complex which
CC is involved in the repression of many genes in a wide variety of
CC physiological processes including heme-regulated and catabolite
CC repressed genes. May also be involved in the derepression of at least
CC some target genes. The complex is recruited to target genes by
CC interaction with DNA-bound transcriptional repressors, like MATALPHA2,
CC MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to
CC produce a repressive chromatin structure, interacts with hypoacetylated
CC N-terminal tails of histones H3 and H4 that have been programmed for
CC repression by the action of histone deacetylases and interferes
CC directly with the transcriptional machinery by associating with the RNA
CC polymerase II mediator complex. {ECO:0000269|PubMed:10722672,
CC ECO:0000269|PubMed:11069890, ECO:0000269|PubMed:11172717,
CC ECO:0000269|PubMed:11230135, ECO:0000269|PubMed:11784848,
CC ECO:0000269|PubMed:14665463, ECO:0000269|PubMed:2247069}.
CC -!- SUBUNIT: Associates with CYC8/SSN6 to form the CYC8-TUP1 (or TUP1-SSN6)
CC corepressor complex that is composed of 4 copies of TUP1 and one copy
CC of CYC8. Interacts with histone H3, histone H4, MATALPHA2, RFX1, SKO1,
CC PGD1, HDA1, HDA2, HOS1, HOS2 AND RPD3. {ECO:0000269|PubMed:10722672,
CC ECO:0000269|PubMed:11069890, ECO:0000269|PubMed:11172717,
CC ECO:0000269|PubMed:11500510, ECO:0000269|PubMed:14525981,
CC ECO:0000269|PubMed:7995523, ECO:0000269|PubMed:8675011,
CC ECO:0000269|PubMed:8943325, ECO:0000269|PubMed:9741624}.
CC -!- INTERACTION:
CC P16649; P14922: CYC8; NbExp=6; IntAct=EBI-19654, EBI-18215;
CC P16649; P40356: PGD1; NbExp=3; IntAct=EBI-19654, EBI-13268;
CC P16649; P48743: RFX1; NbExp=2; IntAct=EBI-19654, EBI-15036;
CC P16649; P32561: RPD3; NbExp=2; IntAct=EBI-19654, EBI-15864;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat TUP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M31733; AAA35182.1; -; Genomic_DNA.
DR EMBL; M35861; AAA34413.1; -; Genomic_DNA.
DR EMBL; X16365; CAA34411.1; ALT_INIT; Genomic_DNA.
DR EMBL; X59720; CAA42259.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07554.1; -; Genomic_DNA.
DR PIR; JN0133; JN0133.
DR RefSeq; NP_010007.1; NM_001178790.1.
DR PDB; 1ERJ; X-ray; 2.30 A; A/B/C=282-388, A/B/C=432-713.
DR PDB; 3VP8; X-ray; 1.91 A; A/B/C/D=1-92.
DR PDB; 3VP9; X-ray; 1.80 A; A/B=1-92.
DR PDBsum; 1ERJ; -.
DR PDBsum; 3VP8; -.
DR PDBsum; 3VP9; -.
DR AlphaFoldDB; P16649; -.
DR SMR; P16649; -.
DR BioGRID; 31057; 112.
DR ComplexPortal; CPX-1663; CYP8-TUP1 corepressor complex.
DR DIP; DIP-512N; -.
DR IntAct; P16649; 27.
DR MINT; P16649; -.
DR STRING; 4932.YCR084C; -.
DR iPTMnet; P16649; -.
DR MaxQB; P16649; -.
DR PaxDb; P16649; -.
DR PRIDE; P16649; -.
DR EnsemblFungi; YCR084C_mRNA; YCR084C; YCR084C.
DR GeneID; 850445; -.
DR KEGG; sce:YCR084C; -.
DR SGD; S000000680; TUP1.
DR VEuPathDB; FungiDB:YCR084C; -.
DR eggNOG; KOG0266; Eukaryota.
DR GeneTree; ENSGT00960000189238; -.
DR HOGENOM; CLU_000288_57_23_1; -.
DR InParanoid; P16649; -.
DR OMA; DYYILYN; -.
DR BioCyc; YEAST:G3O-29380-MON; -.
DR EvolutionaryTrace; P16649; -.
DR PRO; PR:P16649; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P16649; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0017053; C:transcription repressor complex; IPI:SGD.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:SGD.
DR GO; GO:0036033; F:mediator complex binding; IDA:SGD.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD.
DR GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IMP:SGD.
DR GO; GO:0043486; P:histone exchange; IMP:SGD.
DR GO; GO:0006972; P:hyperosmotic response; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:1900192; P:positive regulation of single-species biofilm formation; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0060256; P:regulation of flocculation; IMP:SGD.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013890; Tscrpt_rep_Tup1_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08581; Tup_N; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..713
FT /note="General transcriptional corepressor TUP1"
FT /id="PRO_0000051312"
FT REPEAT 342..371
FT /note="WD 1"
FT REPEAT 441..471
FT /note="WD 2"
FT REPEAT 483..513
FT /note="WD 3"
FT REPEAT 524..555
FT /note="WD 4"
FT REPEAT 574..604
FT /note="WD 5"
FT REPEAT 628..658
FT /note="WD 6"
FT REPEAT 670..706
FT /note="WD 7"
FT REGION 124..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 75
FT /note="E -> A (in Ref. 1; AAA35182)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="R -> Q (in Ref. 1; AAA35182)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="P -> S (in Ref. 1; AAA35182 and 2; AAA34413)"
FT /evidence="ECO:0000305"
FT TURN 19..26
FT /evidence="ECO:0007829|PDB:3VP9"
FT HELIX 27..84
FT /evidence="ECO:0007829|PDB:3VP9"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1ERJ"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:1ERJ"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:1ERJ"
FT TURN 472..475
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 497..504
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:1ERJ"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 551..555
FT /evidence="ECO:0007829|PDB:1ERJ"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 588..595
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 598..604
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:1ERJ"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 644..649
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 652..658
FT /evidence="ECO:0007829|PDB:1ERJ"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 675..680
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 691..697
FT /evidence="ECO:0007829|PDB:1ERJ"
FT STRAND 700..709
FT /evidence="ECO:0007829|PDB:1ERJ"
SQ SEQUENCE 713 AA; 78308 MW; 444104AAD63CB944 CRC64;
MTASVSNTQN KLNELLDAIR QEFLQVSQEA NTYRLQNQKD YDFKMNQQLA EMQQIRNTVY
ELELTHRKMK DAYEEEIKHL KLGLEQRDHQ IASLTVQQQR QQQQQQQVQQ HLQQQQQQLA
AASASVPVAQ QPPATTSATA TPAANTTTGS PSAFPVQASR PNLVGSQLPT TTLPVVSSNA
QQQLPQQQLQ QQQLQQQQPP PQVSVAPLSN TAINGSPTSK ETTTLPSVKA PESTLKETEP
ENNNTSKIND TGSATTATTT TATETEIKPK EEDATPASLH QDHYLVPYNQ RANHSKPIPP
FLLDLDSQSV PDALKKQTND YYILYNPALP REIDVELHKS LDHTSVVCCV KFSNDGEYLA
TGCNKTTQVY RVSDGSLVAR LSDDSAANNH RNSITENNTT TSTDNNTMTT TTTTTITTTA
MTSAAELAKD VENLNTSSSP SSDLYIRSVC FSPDGKFLAT GAEDRLIRIW DIENRKIVMI
LQGHEQDIYS LDYFPSGDKL VSGSGDRTVR IWDLRTGQCS LTLSIEDGVT TVAVSPGDGK
YIAAGSLDRA VRVWDSETGF LVERLDSENE SGTGHKDSVY SVVFTRDGQS VVSGSLDRSV
KLWNLQNANN KSDSKTPNSG TCEVTYIGHK DFVLSVATTQ NDEYILSGSK DRGVLFWDKK
SGNPLLMLQG HRNSVISVAV ANGSPLGPEY NVFATGSGDC KARIWKYKKI APN
