CP51_YEAST
ID CP51_YEAST Reviewed; 530 AA.
AC P10614; D3DKV1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Lanosterol 14-alpha demethylase CYP51 {ECO:0000303|PubMed:369554};
DE EC=1.14.14.154 {ECO:0000269|PubMed:105731, ECO:0000269|PubMed:369554};
DE AltName: Full=Cytochrome P450 51 {ECO:0000305};
DE AltName: Full=Cytochrome P450-14DM {ECO:0000303|PubMed:3046615};
DE AltName: Full=Cytochrome P450-LIA1 {ECO:0000303|PubMed:3322742};
DE Short=CYPLI {ECO:0000303|PubMed:3322742};
DE AltName: Full=Ergosterol biosynthetic protein 11 {ECO:0000303|PubMed:1730736};
DE AltName: Full=Sterol 14-alpha demethylase {ECO:0000305};
GN Name=ERG11 {ECO:0000303|PubMed:1730736}; Synonyms=CYP51;
GN OrderedLocusNames=YHR007C;
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=3322742; DOI=10.1089/dna.1987.6.529;
RA Kalb V.F., Woods C.W., Turi T.G., Dey C.R., Sutter T.R., Loper J.C.;
RT "Primary structure of the P450 lanosterol demethylase gene from
RT Saccharomyces cerevisiae.";
RL DNA 6:529-537(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3046615; DOI=10.1016/s0006-291x(88)81087-8;
RA Ishida N., Aoyama Y., Hatanaka R., Oyama Y., Imajo S., Ishiguro M.,
RA Oshima T., Nakazato H., Noguchi T., Maitra U.S., Mohan V.P., Sprinson D.B.,
RA Yoshida Y.;
RT "A single amino acid substitution converts cytochrome P450(14DM) to an
RT inactive form, cytochrome P450SG1: complete primary structures deduced from
RT cloned DNAS.";
RL Biochem. Biophys. Res. Commun. 155:317-323(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-530.
RX PubMed=3542713; DOI=10.1016/0378-1119(86)90021-1;
RA Kalb V.F., Loper J.C., Dey C.R., Woods C.W., Sutter T.R.;
RT "Isolation of a cytochrome P-450 structural gene from Saccharomyces
RT cerevisiae.";
RL Gene 45:237-245(1986).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=369554; DOI=10.1016/s0006-291x(78)80005-9;
RA Ohba M., Sato R., Yoshida Y., Nishino T., Katsuki H.;
RT "Involvement of cytochrome P-450 and a cyanide-sensitive enzyme in
RT different steps of lanosterol demethylation by yeast microsomes.";
RL Biochem. Biophys. Res. Commun. 85:21-27(1978).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=105731; DOI=10.1016/s0006-291x(78)80006-0;
RA Aoyama Y., Yoshida Y.;
RT "The 14alpha-demethylation of lanosterol by a reconstituted cytochrome P-
RT 450 system from yeast microsomes.";
RL Biochem. Biophys. Res. Commun. 85:28-34(1978).
RN [8]
RP INDUCTION.
RX PubMed=1730736; DOI=10.1016/s0021-9258(18)46051-6;
RA Turi T.G., Loper J.C.;
RT "Multiple regulatory elements control expression of the gene encoding the
RT Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-demethylase
RT (ERG11).";
RL J. Biol. Chem. 267:2046-2056(1992).
RN [9]
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 [10]
RP FUNCTION, AND INTERACTION WITH ERG28.
RX PubMed=15995173; DOI=10.1194/jlr.m500153-jlr200;
RA Mo C., Bard M.;
RT "Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex.";
RL J. Lipid Res. 46:1991-1998(2005).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
RP 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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-353 AND LYS-454, AND
RP IDENTIFICATION BY 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 [14]
RP REVIEW ON ERGOSTEROL BIOSYNTHESIS.
RX PubMed=32679672; DOI=10.3390/genes11070795;
RA Jorda T., Puig S.;
RT "Regulation of ergosterol biosynthesis in Saccharomyces cerevisiae.";
RL Genes (Basel) 11:0-0(2020).
RN [15] {ECO:0007744|PDB:4LXJ, ECO:0007744|PDB:5EQB}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH HEME, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=24613931; DOI=10.1073/pnas.1324245111;
RA Monk B.C., Tomasiak T.M., Keniya M.V., Huschmann F.U., Tyndall J.D.,
RA O'Connell J.D. III, Cannon R.D., McDonald J.G., Rodriguez A.,
RA Finer-Moore J.S., Stroud R.M.;
RT "Architecture of a single membrane spanning cytochrome P450 suggests
RT constraints that orient the catalytic domain relative to a bilayer.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3865-3870(2014).
CC -!- FUNCTION: Lanosterol 14-alpha demethylase; part of the third module of
CC ergosterol biosynthesis pathway that includes the late steps of the
CC pathway (PubMed:369554, PubMed:105731). ERG11 catalyzes C14-
CC demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-
CC triene-3-beta-ol, which is critical for ergosterol biosynthesis
CC (PubMed:369554, PubMed:105731). The third module or late pathway
CC involves the ergosterol synthesis itself through consecutive reactions
CC that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly,
CC the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl
CC pyrophosphate moieties to form squalene, which is the precursor of all
CC steroids. Squalene synthase is crucial for balancing the incorporation
CC of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene
CC synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the
CC stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is
CC considered to be a rate-limiting enzyme in steroid biosynthesis. Then,
CC the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3
CC oxidosqualene to lanosterol, a reaction that forms the sterol core. In
CC the next steps, lanosterol is transformed to zymosterol through a
CC complex process involving various demethylation, reduction and
CC desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also
CC known as CYP51) catalyzes C14-demethylation of lanosterol to produce
CC 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for
CC ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15
CC double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-
CC dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is
CC substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which
CC ERG25 catalyzes the three-step monooxygenation required for the
CC demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes
CC the oxidative decarboxylation that results in a reduction of the 3-
CC beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is
CC responsible for the reduction of the keto group on the C-3. ERG28 has a
CC role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the
CC endoplasmic reticulum and ERG29 regulates the activity of the iron-
CC containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-
CC methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-
CC methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol
CC isomerase ERG2 catalyzes the reaction which results in unsaturation at
CC C-7 in the B ring of sterols and thus converts fecosterol to episterol.
CC The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5
CC double bond in the B ring to produce 5-dehydroepisterol. The C-22
CC sterol desaturase ERG5 further converts 5-dehydroepisterol into
CC ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double
CC bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-
CC 3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce
CC ergosterol (PubMed:32679672). {ECO:0000269|PubMed:105731,
CC ECO:0000269|PubMed:369554, ECO:0000303|PubMed:32679672}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4
CC H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154;
CC Evidence={ECO:0000269|PubMed:105731, ECO:0000269|PubMed:369554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287;
CC Evidence={ECO:0000269|PubMed:105731, ECO:0000269|PubMed:369554};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:24613931};
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 1/6. {ECO:0000269|PubMed:105731,
CC ECO:0000269|PubMed:369554}.
CC -!- SUBUNIT: Interacts with ERG28. {ECO:0000269|PubMed:15995173}.
CC -!- INTERACTION:
CC P10614; P53045: ERG25; NbExp=3; IntAct=EBI-5127, EBI-6506;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000269|PubMed:16847258,
CC ECO:0000269|PubMed:24613931}.
CC -!- INDUCTION: Expression is increased during growth on glucose, in the
CC presence of heme, and during oxygen limiting growth conditions and,
CC unexpectedly, during anaerobic growth (PubMed:1730736). Two upstream
CC activating sequences, UASl and UASZ, and an upstream repressor element,
CC URS1, plus a second possible or cryptic repressor element, URSP, are
CC present in promoter (PubMed:1730736). HAP1 participates in activation
CC from UASl but not from UAS2, whereas the ROXl repressor represses
CC expressio of ERG11 (PubMed:1730736). {ECO:0000269|PubMed:1730736}.
CC -!- MISCELLANEOUS: It is the main target for antifungal compounds of the
CC triazole family like ketoconazole which inhibits by coordinating the
CC iron atom at the sixth ligand position. {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 73200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M18109; AAA34379.1; -; Genomic_DNA.
DR EMBL; M15663; AAA34837.1; -; Genomic_DNA.
DR EMBL; M21483; AAA34546.1; -; Genomic_DNA.
DR EMBL; M21484; AAA34547.1; -; Genomic_DNA.
DR EMBL; U10555; AAB68433.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06695.1; -; Genomic_DNA.
DR PIR; A27491; A27491.
DR RefSeq; NP_011871.1; NM_001179137.1.
DR PDB; 4LXJ; X-ray; 1.90 A; A=1-530.
DR PDB; 5EQB; X-ray; 2.19 A; A=1-530.
DR PDBsum; 4LXJ; -.
DR PDBsum; 5EQB; -.
DR AlphaFoldDB; P10614; -.
DR SMR; P10614; -.
DR BioGRID; 36434; 493.
DR DIP; DIP-7886N; -.
DR IntAct; P10614; 73.
DR MINT; P10614; -.
DR STRING; 4932.YHR007C; -.
DR DrugBank; DB06890; (2R)-2-PHENYL-N-PYRIDIN-4-YLBUTANAMIDE.
DR DrugBank; DB07568; (2S)-2-[(2,1,3-BENZOTHIADIAZOL-4-YLSULFONYL)AMINO]-2-PHENYL-N-PYRIDIN-4-YLACETAMIDE.
DR DrugBank; DB07572; 3-{[(4-methylphenyl)sulfonyl]amino}propyl pyridin-4-ylcarbamate.
DR DrugBank; DB07635; 4,4'-Dihydroxybenzophenone.
DR DrugBank; DB07569; CIS-4-METHYL-N-[(1S)-3-(METHYLSULFANYL)-1-(PYRIDIN-4-YLCARBAMOYL)PROPYL]CYCLOHEXANECARBOXAMIDE.
DR DrugBank; DB07560; N-[(1S)-2-methyl-1-(pyridin-4-ylcarbamoyl)propyl]cyclohexanecarboxamide.
DR iPTMnet; P10614; -.
DR MaxQB; P10614; -.
DR PaxDb; P10614; -.
DR PRIDE; P10614; -.
DR TopDownProteomics; P10614; -.
DR EnsemblFungi; YHR007C_mRNA; YHR007C; YHR007C.
DR GeneID; 856398; -.
DR KEGG; sce:YHR007C; -.
DR SGD; S000001049; ERG11.
DR VEuPathDB; FungiDB:YHR007C; -.
DR eggNOG; KOG0684; Eukaryota.
DR GeneTree; ENSGT00930000151026; -.
DR HOGENOM; CLU_001570_15_0_1; -.
DR InParanoid; P10614; -.
DR OMA; AWTLIEL; -.
DR BioCyc; MetaCyc:YHR007C-MON; -.
DR BioCyc; YEAST:YHR007C-MON; -.
DR BRENDA; 1.14.14.154; 984.
DR Reactome; R-SCE-191273; Cholesterol biosynthesis.
DR Reactome; R-SCE-211976; Endogenous sterols.
DR UniPathway; UPA00770; UER00754.
DR PRO; PR:P10614; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P10614; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008398; F:sterol 14-demethylase activity; IDA:SGD.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:SGD.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Heme; Iron; Isopeptide bond;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..530
FT /note="Lanosterol 14-alpha demethylase CYP51"
FT /id="PRO_0000052012"
FT TOPO_DOM 1..20
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16847258,
FT ECO:0000269|PubMed:24613931"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16847258,
FT ECO:0000269|PubMed:24613931"
FT TOPO_DOM 42..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258,
FT ECO:0000269|PubMed:24613931"
FT BINDING 126
FT /ligand="lanosterol"
FT /ligand_id="ChEBI:CHEBI:16521"
FT /evidence="ECO:0000269|PubMed:24613931,
FT ECO:0007744|PDB:4LXJ"
FT BINDING 314
FT /ligand="itraconazole"
FT /ligand_id="ChEBI:CHEBI:6076"
FT /evidence="ECO:0000269|PubMed:24613931,
FT ECO:0007744|PDB:5EQB"
FT BINDING 470
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:24613931,
FT ECO:0007744|PDB:4LXJ, ECO:0007744|PDB:5EQB"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 433
FT /note="K -> N (in Ref. 2; AAA34546/AAA34547)"
FT /evidence="ECO:0000305"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 27..49
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4LXJ"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:4LXJ"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 160..180
FT /evidence="ECO:0007829|PDB:4LXJ"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:4LXJ"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 249..274
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 301..331
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:4LXJ"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:4LXJ"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4LXJ"
FT HELIX 473..490
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:4LXJ"
FT STRAND 518..525
FT /evidence="ECO:0007829|PDB:4LXJ"
SQ SEQUENCE 530 AA; 60720 MW; 646960BBA0E17979 CRC64;
MSATKSIVGE ALEYVNIGLS HFLALPLAQR ISLIIIIPFI YNIVWQLLYS LRKDRPPLVF
YWIPWVGSAV VYGMKPYEFF EECQKKYGDI FSFVLLGRVM TVYLGPKGHE FVFNAKLADV
SAEAAYAHLT TPVFGKGVIY DCPNSRLMEQ KKFVKGALTK EAFKSYVPLI AEEVYKYFRD
SKNFRLNERT TGTIDVMVTQ PEMTIFTASR SLLGKEMRAK LDTDFAYLYS DLDKGFTPIN
FVFPNLPLEH YRKRDHAQKA ISGTYMSLIK ERRKNNDIQD RDLIDSLMKN STYKDGVKMT
DQEIANLLIG VLMGGQHTSA ATSAWILLHL AERPDVQQEL YEEQMRVLDG GKKELTYDLL
QEMPLLNQTI KETLRMHHPL HSLFRKVMKD MHVPNTSYVI PAGYHVLVSP GYTHLRDEYF
PNAHQFNIHR WNKDSASSYS VGEEVDYGFG AISKGVSSPY LPFGGGRHRC IGEHFAYCQL
GVLMSIFIRT LKWHYPEGKT VPPPDFTSMV TLPTGPAKII WEKRNPEQKI
