EXG1_CANAL
ID EXG1_CANAL Reviewed; 438 AA.
AC P29717; A0A1D8PCW5; Q5AI63; Q5AIZ3; Q9URL8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 5.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glucan 1,3-beta-glucosidase;
DE EC=2.4.1.- {ECO:0000269|PubMed:10469155};
DE EC=3.2.1.58 {ECO:0000269|PubMed:10469155, ECO:0000269|PubMed:20875088, ECO:0000269|PubMed:21713010};
DE AltName: Full=Exo-1,3-beta-glucanase {ECO:0000303|PubMed:8436950};
DE Flags: Precursor;
GN Name=XOG1; Synonyms=EXG, EXG1, XOG; OrderedLocusNames=CAALFM_C102990CA;
GN ORFNames=Ca49C10.05, CaO19.10507, CaO19.2990;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 39-73.
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RX PubMed=8436950; DOI=10.1099/00221287-139-2-325;
RA Chambers R.S., Broughton M.J., Cannon R.D., Carne A., Emerson G.W.,
RA Sullivan P.A.;
RT "An exo-beta-(1,3)-glucanase of Candida albicans: purification of the
RT enzyme and molecular cloning of the gene.";
RL J. Gen. Microbiol. 139:325-334(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE CAO19.10507).
RC STRAIN=1161;
RA Taylor K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [6]
RP PROTEIN SEQUENCE OF 39-73, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=3153A;
RX PubMed=1789004; DOI=10.1002/yea.320070808;
RA Luna-Arias J.P., Analuz E., Ridruejo J.C., Olivero I., Larriba G.;
RT "The major exoglucanase from Candida albicans: a non-glycosylated secretory
RT monomer related to its counterpart from Saccharomyces cerevisiae.";
RL Yeast 7:833-841(1991).
RN [7]
RP ACTIVE SITE GLU-330.
RX PubMed=9013549; DOI=10.1074/jbc.272.6.3161;
RA MacKenzie L.F., Brooke G.S., Cutfield J.F., Sullivan P.A., Withers S.G.;
RT "Identification of Glu-330 as the catalytic nucleophile of Candida albicans
RT exo-beta-(1,3)-glucanase.";
RL J. Biol. Chem. 272:3161-3167(1997).
RN [8]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10469155; DOI=10.1046/j.1432-1327.1999.00581.x;
RA Stubbs H.J., Brasch D.J., Emerson G.W., Sullivan P.A.;
RT "Hydrolase and transferase activities of the beta-1,3-exoglucanase of
RT Candida albicans.";
RL Eur. J. Biochem. 263:889-895(1999).
RN [9]
RP INDUCTION.
RX PubMed=14731272; DOI=10.1111/j.1365-2958.2003.03879.x;
RA Lee C.M., Nantel A., Jiang L., Whiteway M., Shen S.H.;
RT "The serine/threonine protein phosphatase SIT4 modulates yeast-to-hypha
RT morphogenesis and virulence in Candida albicans.";
RL Mol. Microbiol. 51:691-709(2004).
RN [10]
RP INDUCTION.
RX PubMed=17030998; DOI=10.1128/ec.00186-06;
RA Brown V., Sexton J.A., Johnston M.;
RT "A glucose sensor in Candida albicans.";
RL Eukaryot. Cell 5:1726-1737(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19555771; DOI=10.1016/j.fgb.2009.06.005;
RA Maddi A., Bowman S.M., Free S.J.;
RT "Trifluoromethanesulfonic acid-based proteomic analysis of cell wall and
RT secreted proteins of the ascomycetous fungi Neurospora crassa and Candida
RT albicans.";
RL Fungal Genet. Biol. 46:768-781(2009).
RN [12]
RP INDUCTION.
RX PubMed=20402792; DOI=10.1111/j.1567-1364.2010.00626.x;
RA Li X., Du W., Zhao J., Zhang L., Zhu Z., Jiang L.;
RT "The MAP kinase-activated protein kinase Rck2p regulates cellular responses
RT to cell wall stresses, filamentation and virulence in the human fungal
RT pathogen Candida albicans.";
RL FEMS Yeast Res. 10:441-451(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20167299; DOI=10.1016/j.jprot.2010.02.008;
RA Hernaez M.L., Ximenez-Embun P., Martinez-Gomariz M.,
RA Gutierrez-Blazquez M.D., Nombela C., Gil C.;
RT "Identification of Candida albicans exposed surface proteins in vivo by a
RT rapid proteomic approach.";
RL J. Proteomics 73:1404-1409(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=20392151; DOI=10.3109/13693780903405782;
RA Kelly J., Kavanagh K.;
RT "Proteomic analysis of proteins released from growth-arrested Candida
RT albicans following exposure to caspofungin.";
RL Med. Mycol. 48:598-605(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20641015; DOI=10.1002/yea.1775;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.;
RT "Mass spectrometric analysis of the secretome of Candida albicans.";
RL Yeast 27:661-672(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21622905; DOI=10.1128/ec.05011-11;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA de Koning L.J., Klis F.M.;
RT "Effects of fluconazole on the secretome, the wall proteome, and wall
RT integrity of the clinical fungus Candida albicans.";
RL Eukaryot. Cell 10:1071-1081(2011).
RN [17]
RP INTERACTION WITH ANTIMICROBIAL PEPTIDE LL-37, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND FUNCTION.
RX PubMed=21713010; DOI=10.1371/journal.pone.0021394;
RA Tsai P.W., Yang C.Y., Chang H.T., Lan C.Y.;
RT "Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in
RT Candida albicans adhesion by the human antimicrobial peptide LL-37.";
RL PLoS ONE 6:E21394-E21394(2011).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=22876186; DOI=10.1371/journal.ppat.1002848;
RA Taff H.T., Nett J.E., Zarnowski R., Ross K.M., Sanchez H., Cain M.T.,
RA Hamaker J., Mitchell A.P., Andes D.R.;
RT "A Candida biofilm-induced pathway for matrix glucan delivery: implications
RT for drug resistance.";
RL PLoS Pathog. 8:E1002848-E1002848(2012).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=23243062; DOI=10.1128/ec.00278-12;
RA Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G.,
RA Brul S., de Koning L.J., Klis F.M.;
RT "Surface stress induces a conserved cell wall stress response in the
RT pathogenic fungus Candida albicans.";
RL Eukaryot. Cell 12:254-264(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=23136884; DOI=10.1111/mmi.12087;
RA Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL Mol. Microbiol. 87:132-151(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 45-438, DISULFIDE BOND, AND
RP SUBSTRATE-BINDING.
RX PubMed=10610795; DOI=10.1006/jmbi.1999.3287;
RA Cutfield S.M., Davies G.J., Murshudov G., Anderson B.F., Moody P.C.,
RA Sullivan P.A., Cutfield J.F.;
RT "The structure of the exo-beta-(1,3)-glucanase from Candida albicans in
RT native and bound forms: relationship between a pocket and groove in family
RT 5 glycosyl hydrolases.";
RL J. Mol. Biol. 294:771-783(1999).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 39-438 IN COMPLEX WITH SUBSTRATE,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-182; PHE-267; PHE-296 AND
RP GLU-330.
RX PubMed=20875088; DOI=10.1111/j.1742-4658.2010.07869.x;
RA Patrick W.M., Nakatani Y., Cutfield S.M., Sharpe M.L., Ramsay R.J.,
RA Cutfield J.F.;
RT "Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and
RT the role of the Phe-Phe 'clamp' at the active site entrance.";
RL FEBS J. 277:4549-4561(2010).
CC -!- FUNCTION: Major glucan 1,3-beta-glucosidase required for cell wall
CC integrity. Beta-glucanases participate in the metabolism of beta-
CC glucan, the main structural component of the cell wall. Can also
CC function biosynthetically as a transglycosylase. Functions to deliver
CC glucan from the cell to the extracellular matrix. Does not appear to
CC impact cell wall glucan content of biofilm cells, nor is it necessary
CC for filamentation or biofilm formation. Involved in cell-substrate and
CC cell-cell adhesion. Adhesion to host-cell surfaces is the first
CC critical step during mucosal infection. XOG1 is target of human
CC antimicrobial peptide LL-37 for inhibition of cell adhesion.
CC {ECO:0000269|PubMed:21713010, ECO:0000269|PubMed:22876186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000269|PubMed:10469155,
CC ECO:0000269|PubMed:20875088, ECO:0000269|PubMed:21713010};
CC -!- ACTIVITY REGULATION: Binding of human antimicrobial peptide LL-37
CC decreases the catalytic activity, which leads to the decrease of cell
CC adhesion. {ECO:0000269|PubMed:21713010}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.0 mM for laminaribiose {ECO:0000269|PubMed:10469155};
CC KM=12.7 mM for laminaritriose {ECO:0000269|PubMed:10469155};
CC KM=5.0 mM for laminaritetraose {ECO:0000269|PubMed:10469155};
CC KM=2.6 mM for laminaripentaose {ECO:0000269|PubMed:10469155};
CC KM=2.7 mM for laminarihexaose {ECO:0000269|PubMed:10469155};
CC KM=2.4 mM for laminariheptaose {ECO:0000269|PubMed:10469155};
CC KM=3.9 mM for laminarin {ECO:0000269|PubMed:10469155};
CC KM=17.9 mM for pustulan {ECO:0000269|PubMed:10469155};
CC KM=260 mM for gentiobiose {ECO:0000269|PubMed:10469155};
CC KM=120 mM for gentiotriose {ECO:0000269|PubMed:10469155};
CC KM=70 mM for cellobiose {ECO:0000269|PubMed:10469155};
CC KM=9.4 mM for cellotetraose {ECO:0000269|PubMed:10469155};
CC KM=12.0 mM for cellohexaose {ECO:0000269|PubMed:10469155};
CC KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG)
CC {ECO:0000269|PubMed:10469155};
CC -!- SUBUNIT: Monomer. Interacts with the human antimicrobial peptide LL-37.
CC {ECO:0000269|PubMed:1789004, ECO:0000269|PubMed:20875088,
CC ECO:0000269|PubMed:21713010}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:1789004,
CC ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:20167299,
CC ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}. Note=Is non-
CC covalently attached to the cell wall.
CC -!- INDUCTION: Expression is maximal during the early rapid growth phase
CC and increases during biofilm growth. Induced by caspofungin.
CC Transcripts is also regulated by RCK2, SIT4, and HTG4.
CC {ECO:0000269|PubMed:14731272, ECO:0000269|PubMed:17030998,
CC ECO:0000269|PubMed:20392151, ECO:0000269|PubMed:20402792,
CC ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:22876186}.
CC -!- DISRUPTION PHENOTYPE: Leads to enhanced susceptibility to the commonly
CC used antifungal, fluconazole, during biofilm growth only.
CC {ECO:0000269|PubMed:22876186}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; X56556; CAA39908.1; -; Genomic_DNA.
DR EMBL; AL033497; CAA21969.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW25980.1; -; Genomic_DNA.
DR PIR; A47702; A47702.
DR PIR; T52149; T52149.
DR RefSeq; XP_721488.2; XM_716395.2.
DR PDB; 1CZ1; X-ray; 1.85 A; A=45-438.
DR PDB; 1EQC; X-ray; 1.85 A; A=45-438.
DR PDB; 1EQP; X-ray; 1.90 A; A=45-438.
DR PDB; 2PB1; X-ray; 1.90 A; A=39-438.
DR PDB; 2PBO; X-ray; 1.85 A; A=39-438.
DR PDB; 2PC8; X-ray; 1.80 A; A=39-438.
DR PDB; 2PF0; X-ray; 1.90 A; A=39-438.
DR PDB; 3N9K; X-ray; 1.70 A; A=40-438.
DR PDB; 3O6A; X-ray; 2.00 A; A=40-438.
DR PDB; 4M80; X-ray; 1.86 A; A=40-438.
DR PDB; 4M81; X-ray; 1.86 A; A=40-438.
DR PDB; 4M82; X-ray; 1.59 A; A=40-438.
DR PDBsum; 1CZ1; -.
DR PDBsum; 1EQC; -.
DR PDBsum; 1EQP; -.
DR PDBsum; 2PB1; -.
DR PDBsum; 2PBO; -.
DR PDBsum; 2PC8; -.
DR PDBsum; 2PF0; -.
DR PDBsum; 3N9K; -.
DR PDBsum; 3O6A; -.
DR PDBsum; 4M80; -.
DR PDBsum; 4M81; -.
DR PDBsum; 4M82; -.
DR AlphaFoldDB; P29717; -.
DR SMR; P29717; -.
DR BioGRID; 1219931; 3.
DR STRING; 237561.P29717; -.
DR DrugBank; DB01816; Castanospermine.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EXG5A_CANAL; -.
DR GeneID; 3636837; -.
DR KEGG; cal:CAALFM_C102990CA; -.
DR CGD; CAL0000190583; XOG1.
DR VEuPathDB; FungiDB:C1_02990C_A; -.
DR eggNOG; ENOG502QPYU; Eukaryota.
DR HOGENOM; CLU_004624_0_1_1; -.
DR InParanoid; P29717; -.
DR OMA; YWTWKAE; -.
DR OrthoDB; 896412at2759; -.
DR BRENDA; 3.2.1.58; 1096.
DR SABIO-RK; P29717; -.
DR EvolutionaryTrace; P29717; -.
DR PRO; PR:P29717; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:CGD.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:CGD.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:CGD.
DR GO; GO:0006073; P:cellular glucan metabolic process; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR GO; GO:0044407; P:single-species biofilm formation in or on host organism; IMP:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW Signal; Transferase; Virulence; Zymogen.
FT SIGNAL 1..21
FT /note="Or 25"
FT /evidence="ECO:0000255"
FT PROPEP 22..38
FT /evidence="ECO:0000269|PubMed:1789004,
FT ECO:0000269|PubMed:8436950"
FT /id="PRO_0000007878"
FT CHAIN 39..438
FT /note="Glucan 1,3-beta-glucosidase"
FT /id="PRO_0000007879"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9013549"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20875088"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20875088"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20875088"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20875088"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20875088"
FT DISULFID 313..435
FT /evidence="ECO:0000269|PubMed:10610795"
FT DISULFID 338..364
FT /evidence="ECO:0000269|PubMed:10610795"
FT MUTAGEN 182
FT /note="F->A: Decreases catalytic activity. Impairs
FT catalytic activity; when associated with Ala-296."
FT /evidence="ECO:0000269|PubMed:20875088"
FT MUTAGEN 267
FT /note="F->A: Decreases catalytic activity. Impairs
FT catalytic activity; when associated with Ala-296 or Ser-
FT 330."
FT /evidence="ECO:0000269|PubMed:20875088"
FT MUTAGEN 296
FT /note="F->A: Impairs catalytic activity; when associated
FT with Ala-182."
FT /evidence="ECO:0000269|PubMed:20875088"
FT MUTAGEN 296
FT /note="F->W,I: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:20875088"
FT MUTAGEN 330
FT /note="E->Q: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:20875088"
FT MUTAGEN 330
FT /note="E->S: Impairs catalytic activity; when associated
FT with Ala-267."
FT /evidence="ECO:0000269|PubMed:20875088"
FT CONFLICT 102
FT /note="S -> L (in Ref. 2; CAA21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="F -> S (in Ref. 2; CAA21969)"
FT /evidence="ECO:0000305"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4M82"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 89..112
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4M82"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 238..254
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4M82"
FT TURN 270..275
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 305..321
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:4M82"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 375..393
FT /evidence="ECO:0007829|PDB:4M82"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:4M82"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:4M82"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:4M82"
SQ SEQUENCE 438 AA; 50056 MW; 6FEAEA80C1B0121C CRC64;
MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN NVIRGVNLGG
WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA ASRILQKHWS TWITEQDFKQ
ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ VQYLEKALGW ARKNNIRVWI DLHGAPGSQN
GFDNSGLRDS YNFQNGDNTQ VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK
LKQFFLDGYN SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE
LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR YEGAYDNAPY
IGSCQPMLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF WSWKTENAPE WSFQTLTYNG
LFPQPVTDRQ FPNQCGFH
