ACEA_YEAST
ID ACEA_YEAST Reviewed; 557 AA.
AC P28240; D3DLX0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:1551398};
DE Short=ICL {ECO:0000305};
DE EC=4.1.3.1 {ECO:0000269|PubMed:1551398, ECO:0000269|PubMed:23159490, ECO:0000269|PubMed:3059712, ECO:0000269|PubMed:4259654};
DE AltName: Full=Methylisocitrate lyase {ECO:0000303|PubMed:4259654};
DE Short=MICA {ECO:0000305};
DE EC=4.1.3.30 {ECO:0000269|PubMed:3059712, ECO:0000269|PubMed:4259654};
DE AltName: Full=Threo-D(S)-isocitrate glyoxylate-lyase {ECO:0000305};
GN Name=ICL1 {ECO:0000303|PubMed:1551398};
GN OrderedLocusNames=YER065C {ECO:0000312|SGD:S000000867};
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=1551398; DOI=10.1111/j.1432-1033.1992.tb16720.x;
RA Fernandez E., Moreno F., Rodicio R.;
RT "The ICL1 gene from Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 204:983-990(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=DBY939;
RX PubMed=8319292; DOI=10.1007/bf00312621;
RA Schoeler A., Schueller H.-J.;
RT "Structure and regulation of the isocitrate lyase gene ICL1 from the yeast
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 23:375-381(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=4259654; DOI=10.1016/0003-9861(72)90118-x;
RA McFadden B.A., Rose I.A., Williams J.O.;
RT "Production of pyruvate and succinate by action of isocitrate lyase on
RT alpha-methylisocitrate.";
RL Arch. Biochem. Biophys. 148:84-88(1972).
RN [6]
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=3076186; DOI=10.1099/00221287-134-9-2499;
RA Lopez-Boado Y.S., Herrero P., Fernandez M.-T., Fernandez R., Moreno F.;
RT "Glucose-stimulated phosphorylation of yeast isocitrate lyase in vivo.";
RL J. Gen. Microbiol. 134:2499-2505(1988).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=3059712; DOI=10.1002/yea.320040105;
RA Lopez-Boado Y.S., Herrero P., Fernandez M.-T., Fernandez R., Moreno F.;
RT "Purification of isocitrate lyase from Saccharomyces cerevisiae.";
RL Yeast 4:41-46(1988).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8870676; DOI=10.1042/bj3190255;
RA Taylor K.M., Kaplan C.P., Gao X., Baker A.;
RT "Localization and targeting of isocitrate lyases in Saccharomyces
RT cerevisiae.";
RL Biochem. J. 319:255-262(1996).
RN [9]
RP MUTAGENESIS OF THR-53.
RX PubMed=8641464; DOI=10.1016/0014-5793(96)00344-4;
RA Ordiz I., Herrero P., Rodicio R., Moreno F.;
RT "Glucose-induced inactivation of isocitrate lyase in Saccharomyces
RT cerevisiae is mediated by the cAMP-dependent protein kinase catalytic
RT subunits Tpk1 and Tpk2.";
RL FEBS Lett. 385:43-46(1996).
RN [10]
RP MUTAGENESIS OF LYS-216 AND MET-220.
RX PubMed=8923733;
RX DOI=10.1002/(sici)1097-0061(199610)12:13<1285::aid-yea5>3.0.co;2-b;
RA Heinisch J.J., Valdes E., Alvarez J., Rodicio R.;
RT "Molecular genetics of ICL2, encoding a non-functional isocitrate lyase in
RT Saccharomyces cerevisiae.";
RL Yeast 12:1285-1295(1996).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=9370278; DOI=10.1016/s0378-1119(97)00311-9;
RA Chaves R.S., Herrero P., Ordiz I., Angeles del Brio M., Moreno F.;
RT "Isocitrate lyase localisation in Saccharomyces cerevisiae cells.";
RL Gene 198:165-169(1997).
RN [12]
RP INDUCTION.
RX PubMed=9425123; DOI=10.1042/bj3290383;
RA Ordiz I., Herrero P., Rodicio R., Gancedo J.M., Moreno F.;
RT "A 27 kDa protein binds to a positive and a negative regulatory sequence in
RT the promoter of the ICL1 gene from Saccharomyces cerevisiae.";
RL Biochem. J. 329:383-388(1998).
RN [13]
RP INDUCTION.
RX PubMed=10540293; DOI=10.1046/j.1365-2958.1999.01588.x;
RA Rahner A., Hiesinger M., Schueller H.-J.;
RT "Deregulation of gluconeogenic structural genes by variants of the
RT transcriptional activator Cat8p of the yeast Saccharomyces cerevisiae.";
RL Mol. Microbiol. 34:146-156(1999).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11452311; DOI=10.1038/35083594;
RA Lorenz M.C., Fink G.R.;
RT "The glyoxylate cycle is required for fungal virulence.";
RL Nature 412:83-86(2001).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17651441; DOI=10.1111/j.1742-4658.2007.05959.x;
RA Sarry J.E., Chen S., Collum R.P., Liang S., Peng M., Lang A., Naumann B.,
RA Dzierszinski F., Yuan C.X., Hippler M., Rea P.A.;
RT "Analysis of the vacuolar luminal proteome of Saccharomyces cerevisiae.";
RL FEBS J. 274:4287-4305(2007).
RN [16]
RP INDUCTION.
RX PubMed=17428308; DOI=10.1111/j.1567-1364.2007.00236.x;
RA Belinchon M.M., Gancedo J.M.;
RT "Glucose controls multiple processes in Saccharomyces cerevisiae through
RT diverse combinations of signaling pathways.";
RL FEMS Yeast Res. 7:808-818(2007).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=20457600; DOI=10.1074/jbc.m109.075143;
RA Brown C.R., Hung G.C., Dunton D., Chiang H.L.;
RT "The TOR complex 1 is distributed in endosomes and in retrograde vesicles
RT that form from the vacuole membrane and plays an important role in the
RT vacuole import and degradation pathway.";
RL J. Biol. Chem. 285:23359-23370(2010).
RN [18]
RP DISRUPTION PHENOTYPE.
RX PubMed=21246628; DOI=10.1002/yea.1828;
RA Lee Y.J., Jang J.W., Kim K.J., Maeng P.J.;
RT "TCA cycle-independent acetate metabolism via the glyoxylate cycle in
RT Saccharomyces cerevisiae.";
RL Yeast 28:153-166(2011).
RN [19]
RP FUNCTION.
RX PubMed=22876324; DOI=10.1371/journal.pone.0042475;
RA Chen Y., Siewers V., Nielsen J.;
RT "Profiling of cytosolic and peroxisomal acetyl-CoA metabolism in
RT Saccharomyces cerevisiae.";
RL PLoS ONE 7:E42475-E42475(2012).
RN [20]
RP CATALYTIC ACTIVITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23159490; DOI=10.1016/j.bbamcr.2012.11.008;
RA Casatta N., Porro A., Orlandi I., Brambilla L., Vai M.;
RT "Lack of Sir2 increases acetate consumption and decreases extracellular
RT pro-aging factors.";
RL Biochim. Biophys. Acta 1833:593-601(2013).
RN [21]
RP DISRUPTION PHENOTYPE.
RX PubMed=24062879; DOI=10.1155/2013/802870;
RA Orlandi I., Ronzulli R., Casatta N., Vai M.;
RT "Ethanol and acetate acting as carbon/energy sources negatively affect
RT yeast chronological aging.";
RL Oxid. Med. Cell. Longev. 2013:802870-802870(2013).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=24665361; DOI=10.3402/jev.v3.23497;
RA Giardina B.J., Stein K., Chiang H.L.;
RT "The endocytosis gene END3 is essential for the glucose-induced rapid
RT decline of small vesicles in the extracellular fraction in Saccharomyces
RT cerevisiae.";
RL J. Extracell. Vesicles 3:0-0(2014).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=24520859; DOI=10.1186/1477-5956-12-9;
RA Giardina B.J., Stanley B.A., Chiang H.L.;
RT "Glucose induces rapid changes in the secretome of Saccharomyces
RT cerevisiae.";
RL Proteome Sci. 12:9-9(2014).
CC -!- FUNCTION: Catalyzes the formation of succinate and glyoxylate from
CC isocitrate, a key step of the glyoxylate cycle, which operates as an
CC anaplerotic route for replenishing the tricarboxylic acid cycle.
CC Required for growth on ethanol or acetate, but dispensable when
CC fermentable carbon sources are available. Acts also on 2-
CC methylisocitrate. {ECO:0000269|PubMed:11452311,
CC ECO:0000269|PubMed:1551398, ECO:0000269|PubMed:22876324,
CC ECO:0000269|PubMed:23159490, ECO:0000269|PubMed:3059712,
CC ECO:0000269|PubMed:4259654}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:1551398,
CC ECO:0000269|PubMed:23159490, ECO:0000269|PubMed:3059712,
CC ECO:0000269|PubMed:4259654};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC Evidence={ECO:0000269|PubMed:3059712, ECO:0000269|PubMed:4259654};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WKK7};
CC -!- ACTIVITY REGULATION: Phosphorylated and inactivated after addition of
CC glucose to the cell culture (repressing conditions).
CC {ECO:0000269|PubMed:3076186}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for threo-D(S)-isocitrate (at pH 7.0)
CC {ECO:0000269|PubMed:3059712, ECO:0000269|PubMed:4259654};
CC KM=0.6 mM for threo-D(S)-2-methylisocitrate (at pH 7.0 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:3059712, ECO:0000269|PubMed:4259654};
CC Note=The Vmax with threo-D(S)-isocitrate as substrate is 5-fold
CC higher than with threo-D(S)-2-methylisocitrate as substrate.
CC {ECO:0000269|PubMed:3059712, ECO:0000269|PubMed:4259654};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:3059712,
CC ECO:0000269|PubMed:4259654};
CC Temperature dependence:
CC Thermostable for 60 minutes up to 50 degrees Celsius.
CC {ECO:0000269|PubMed:3059712, ECO:0000269|PubMed:4259654};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000305|PubMed:3059712,
CC ECO:0000305|PubMed:4259654}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:3059712}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20457600,
CC ECO:0000269|PubMed:8870676, ECO:0000269|PubMed:9370278}. Secreted,
CC extracellular space, extracellular matrix {ECO:0000269|PubMed:24520859,
CC ECO:0000269|PubMed:24665361}. Vacuole {ECO:0000269|PubMed:17651441,
CC ECO:0000269|PubMed:20457600}. Note=Localizes in extracellular vesicles
CC during growth on lown glucose. When glucose is added to glucose-starved
CC wild-type cells, levels of extracellular ICL1 get reduced. Targeted to
CC the vacuole for degradation in 3-day-starved cells.
CC {ECO:0000269|PubMed:20457600, ECO:0000269|PubMed:24520859,
CC ECO:0000269|PubMed:24665361}.
CC -!- INDUCTION: Repressed by glucose and induced by ethanol via the
CC transcriptional activator CAT8. The promoter sequence located between
CC -397 and -388 contains an upstream activating sequence (UAS)element
CC whereas the sequence located between -261 and -242 contains an upstream
CC repressing sequence (URS) element. {ECO:0000269|PubMed:10540293,
CC ECO:0000269|PubMed:17428308, ECO:0000269|PubMed:3076186,
CC ECO:0000269|PubMed:8319292, ECO:0000269|PubMed:9425123}.
CC -!- PTM: Phosphorylated in response to elevated glucose levels, leading
CC first to reversible inactivation of the enzyme (short-term
CC inactivation), and at a later stage to proteolytic degradation of the
CC protein (long-term inactivation). {ECO:0000269|PubMed:3076186}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth when acetate or ethanol are the
CC sole carbon source. Leads to reduced chronological lifespan.
CC {ECO:0000269|PubMed:11452311, ECO:0000269|PubMed:1551398,
CC ECO:0000269|PubMed:21246628, ECO:0000269|PubMed:23159490,
CC ECO:0000269|PubMed:24062879}.
CC -!- MISCELLANEOUS: Yeast isocitrate lyase is the only eukaryotic member of
CC this family that is located in the cytoplasm, instead of being targeted
CC to the peroxisome or the glyoxysome. {ECO:0000269|PubMed:9370278}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; X61271; CAA43575.1; -; Genomic_DNA.
DR EMBL; X65554; CAA46523.1; -; Genomic_DNA.
DR EMBL; U18813; AAB64601.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07724.1; -; Genomic_DNA.
DR PIR; S22386; WZBYI.
DR RefSeq; NP_010987.3; NM_001178956.3.
DR PDB; 7EBC; X-ray; 2.30 A; A/B/C/D=1-557.
DR PDBsum; 7EBC; -.
DR AlphaFoldDB; P28240; -.
DR SMR; P28240; -.
DR BioGRID; 36807; 82.
DR DIP; DIP-1663N; -.
DR IntAct; P28240; 2.
DR MINT; P28240; -.
DR STRING; 4932.YER065C; -.
DR MaxQB; P28240; -.
DR PaxDb; P28240; -.
DR PRIDE; P28240; -.
DR EnsemblFungi; YER065C_mRNA; YER065C; YER065C.
DR GeneID; 856794; -.
DR KEGG; sce:YER065C; -.
DR SGD; S000000867; ICL1.
DR VEuPathDB; FungiDB:YER065C; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; P28240; -.
DR OMA; LEKDWAE; -.
DR BioCyc; YEAST:YER065C-MON; -.
DR SABIO-RK; P28240; -.
DR UniPathway; UPA00703; UER00719.
DR PRO; PR:P28240; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P28240; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IMP:SGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631; PTHR21631; 1.
DR Pfam; PF00463; ICL; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01346; isocit_lyase; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Extracellular matrix; Glyoxylate bypass; Lyase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Secreted;
KW Tricarboxylic acid cycle; Vacuole.
FT CHAIN 1..557
FT /note="Isocitrate lyase"
FT /id="PRO_0000068799"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 218..219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 437..441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MUTAGEN 53
FT /note="T->A: Abolishes short-term enzyme inactivation by
FT glucose addition."
FT /evidence="ECO:0000269|PubMed:8641464"
FT MUTAGEN 216
FT /note="K->R: Reduces activity by 45%; when associated with
FT L-220."
FT /evidence="ECO:0000269|PubMed:8923733"
FT MUTAGEN 220
FT /note="M->L: Reduces activity by 45%; when associated with
FT R-216."
FT /evidence="ECO:0000269|PubMed:8923733"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 60..78
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:7EBC"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 131..154
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:7EBC"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 415..426
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:7EBC"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:7EBC"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 473..492
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 494..500
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 502..508
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 515..519
FT /evidence="ECO:0007829|PDB:7EBC"
FT HELIX 521..531
FT /evidence="ECO:0007829|PDB:7EBC"
SQ SEQUENCE 557 AA; 62409 MW; 15CC5A169CCEBE8B CRC64;
MPIPVGNTKN DFAALQAKLD ADAAEIEKWW SDSRWSKTKR NYSARDIAVR RGTFPPIEYP
SSVMARKLFK VLEKHHNEGT VSKTFGALDP VQISQMAKYL DTIYISGWQC SSTASTSNEP
GPDLADYPMD TVPNKVEHLF KAQLFHDRKQ LEARSKAKSQ EELDEMGAPI DYLTPIVADA
DAGHGGLTAV FKLTKMFIER GAAGIHMEDQ TSTNKKCGHM AGRCVIPVQE HVNRLVTIRM
CADIMHSDLI VVARTDSEAA TLISSTIDTR DHYFIVGATN PNIEPFAEVL NDAIMSGASG
QELADIEQKW CRDAGLKLFH EAVIDEIERS ALSNKQELIK KFTSKVGPLT ETSHREAKKL
AKEILGHEIF FDWELPRVRE GLYRYRGGTQ CSIMRARAFA PYADLVWMES NYPDFQQAKE
FAEGVKEKFP DQWLAYNLSP SFNWPKAMSV DEQHTFIQRL GDLGYIWQFI TLAGLHTNAL
AVHNFSRDFA KDGMKAYAQN VQQREMDDGV DVLKHQKWSG AEYIDGLLKL AQGGVSATAA
MGTGVTEDQF KENGVKK
