FET3_YEAST
ID FET3_YEAST Reviewed; 636 AA.
AC P38993; D6VZN2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Iron transport multicopper oxidase FET3;
DE EC=1.16.3.1 {ECO:0000269|PubMed:16230618};
DE Flags: Precursor;
GN Name=FET3; OrderedLocusNames=YMR058W; ORFNames=YM9796.11;
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, AND INDUCTION.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8293473; DOI=10.1016/0092-8674(94)90346-8;
RA Askwith C., Eide D., van Ho A., Bernard P.S., Li L., Davis-Kaplan S.,
RA Sipe D.M., Kaplan J.;
RT "The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for
RT ferrous iron uptake.";
RL Cell 76:403-410(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7836366; DOI=10.1074/jbc.270.3.1098;
RA de Silva D.M., Askwith C.C., Eide D., Kaplan J.;
RT "The FET3 gene product required for high affinity iron transport in yeast
RT is a cell surface ferroxidase.";
RL J. Biol. Chem. 270:1098-1101(1995).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9162052; DOI=10.1074/jbc.272.22.14208;
RA de Silva D., Davis-Kaplan S., Fergestad J., Kaplan J.;
RT "Purification and characterization of Fet3 protein, a yeast homologue of
RT ceruloplasmin.";
RL J. Biol. Chem. 272:14208-14213(1997).
RN [6]
RP EPR SPECTROSCOPY.
RA Kosman D.J., Hassett R., Yuan D.S., McCracken J.;
RT "Spectroscopic characterization of the Cu(II) sites in the Fet3 protein,
RT the multinuclear copper oxidase from yeast required for high affinity iron
RT uptake.";
RL J. Am. Chem. Soc. 120:4037-4038(1998).
RN [7]
RP ENZYME KINETICS, ABSORPTION SPECTROSCOPY, AND EPR SPECTROSCOPY.
RX PubMed=9722559; DOI=10.1074/jbc.273.36.23274;
RA Hassett R., Yuan D.S., Kosman D.J.;
RT "Spectral and kinetic properties of the Fet3 protein from Saccharomyces
RT cerevisiae, a multinuclear copper ferroxidase enzyme.";
RL J. Biol. Chem. 273:23274-23282(1998).
RN [8]
RP ABSORPTION SPECTROSCOPY, CIRCULAR DICHROISM ANALYSIS, MAGNETIC CIRCULAR
RP DICHROISM, EPR SPECTROSCOPY, AND RESONANCE RAMAN SPECTROSCOPY.
RX PubMed=11389633; DOI=10.1021/ja003975s;
RA Machonkin T.E., Quintanar L., Palmer A.E., Hassett R., Severance S.,
RA Kosman D.J., Solomon E.I.;
RT "Spectroscopy and reactivity of the type 1 copper site in Fet3p from
RT Saccharomyces cerevisiae: correlation of structure with reactivity in the
RT multicopper oxidases.";
RL J. Am. Chem. Soc. 123:5507-5517(2001).
RN [9]
RP CIRCULAR DICHROISM ANALYSIS, MAGNETIC CIRCULAR DICHROISM, AND EPR
RP SPECTROSCOPY OF MUTANTS.
RX PubMed=12009907; DOI=10.1021/bi011979j;
RA Palmer A.E., Quintanar L., Severance S., Wang T.P., Kosman D.J.,
RA Solomon E.I.;
RT "Spectroscopic characterization and O(2) reactivity of the trinuclear Cu
RT cluster of mutants of the multicopper oxidase Fet3p.";
RL Biochemistry 41:6438-6448(2002).
RN [10]
RP MUTAGENESIS OF COPPER LIGANDS, ABSORPTION SPECTROSCOPY, AND EPR
RP SPECTROSCOPY.
RX PubMed=10694398; DOI=10.1021/bi992334a;
RA Blackburn N.J., Ralle M., Hassett R., Kosman D.J.;
RT "Spectroscopic analysis of the trinuclear cluster in the Fet3 protein from
RT yeast, a multinuclear copper oxidase.";
RL Biochemistry 39:2316-2324(2000).
RN [11]
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 [12]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=16522632; DOI=10.1074/jbc.m512042200;
RA Singh A., Severance S., Kaur N., Wiltsie W., Kosman D.J.;
RT "Assembly, activation, and trafficking of the Fet3p.Ftr1p high affinity
RT iron permease complex in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 281:13355-13364(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP IDENTIFICATION BY 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 [15] {ECO:0007744|PDB:1ZPU}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-555 IN COMPLEX WITH COPPER,
RP CATALYTIC ACTIVITY, AND GLYCOSYLATION AT ASN-27; ASN-77; ASN-88; ASN-113;
RP ASN-194; ASN-198; ASN-244; ASN-292; ASN-300; ASN-359 AND ASN-381.
RX PubMed=16230618; DOI=10.1073/pnas.0506227102;
RA Taylor A.B., Stoj C.S., Ziegler L., Kosman D.J., Hart P.J.;
RT "The copper-iron connection in biology: structure of the metallo-oxidase
RT Fet3p.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15459-15464(2005).
CC -!- FUNCTION: Iron transport multicopper ferroxidase required for Fe(2+)
CC ion high affinity uptake. Required to oxidize Fe(2+) to Fe(3+), which
CC is then transported into the cell via the ferric iron permease FTR1.
CC Essential component of copper-dependent iron transport.
CC {ECO:0000269|PubMed:7836366, ECO:0000269|PubMed:8293473}.
CC -!- CATALYTIC ACTIVITY: [Iron transport multicopper oxidase FET3]:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000269|PubMed:16230618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC Evidence={ECO:0000269|PubMed:16230618};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:16230618};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000269|PubMed:16230618};
CC -!- INTERACTION:
CC P38993; P40088: FTR1; NbExp=6; IntAct=EBI-6876, EBI-7138;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16522632,
CC ECO:0000269|PubMed:7836366, ECO:0000269|PubMed:9162052}; Single-pass
CC type I membrane protein; Extracellular side
CC {ECO:0000269|PubMed:16522632, ECO:0000269|PubMed:7836366}.
CC -!- INDUCTION: By iron deprivation. Repressed by iron excess.
CC {ECO:0000269|PubMed:8293473}.
CC -!- MISCELLANEOUS: Present with 1050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; L25090; AAA64929.1; -; Genomic_DNA.
DR EMBL; Z49703; CAA89768.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09956.1; -; Genomic_DNA.
DR PIR; A55428; A55428.
DR RefSeq; NP_013774.1; NM_001182556.1.
DR PDB; 1ZPU; X-ray; 2.80 A; A/B/C/D/E/F=22-555.
DR PDBsum; 1ZPU; -.
DR AlphaFoldDB; P38993; -.
DR SMR; P38993; -.
DR BioGRID; 35233; 123.
DR ComplexPortal; CPX-868; FET3-FTR1 high affinity iron permease complex.
DR DIP; DIP-5314N; -.
DR IntAct; P38993; 10.
DR MINT; P38993; -.
DR STRING; 4932.YMR058W; -.
DR TCDB; 2.A.108.1.1; the iron/lead transporter (ilt) family.
DR iPTMnet; P38993; -.
DR MaxQB; P38993; -.
DR PaxDb; P38993; -.
DR PRIDE; P38993; -.
DR EnsemblFungi; YMR058W_mRNA; YMR058W; YMR058W.
DR GeneID; 855080; -.
DR KEGG; sce:YMR058W; -.
DR SGD; S000004662; FET3.
DR VEuPathDB; FungiDB:YMR058W; -.
DR eggNOG; KOG1263; Eukaryota.
DR GeneTree; ENSGT00940000176768; -.
DR HOGENOM; CLU_006504_7_3_1; -.
DR InParanoid; P38993; -.
DR OMA; VHYDDTM; -.
DR BioCyc; YEAST:YMR058W-MON; -.
DR SABIO-RK; P38993; -.
DR EvolutionaryTrace; P38993; -.
DR PRO; PR:P38993; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38993; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0033573; C:high-affinity iron permease complex; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:1901684; P:arsenate ion transmembrane transport; IGI:SGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0098706; P:iron ion import across cell outer membrane; IDA:ComplexPortal.
DR GO; GO:0034755; P:iron ion transmembrane transport; IMP:SGD.
DR GO; GO:0033215; P:reductive iron assimilation; IMP:SGD.
DR GO; GO:0046688; P:response to copper ion; IMP:SGD.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Glycoprotein; Ion transport; Iron;
KW Iron transport; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..636
FT /note="Iron transport multicopper oxidase FET3"
FT /id="PRO_0000002959"
FT TOPO_DOM 22..559
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16522632"
FT TRANSMEM 560..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16522632"
FT DOMAIN 32..146
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 157..301
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 362..502
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 128
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 413
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 416
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 418
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 483
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 484
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 485
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT BINDING 489
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16230618,
FT ECO:0007744|PDB:1ZPU"
FT STRAND 23..35
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1ZPU"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 336..347
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 487..491
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 502..507
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:1ZPU"
FT HELIX 515..523
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:1ZPU"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:1ZPU"
SQ SEQUENCE 636 AA; 72360 MW; 71CB4352B87746E6 CRC64;
MTNALLSIAV LLFSMLSLAQ AETHTFNWTT GWDYRNVDGL KSRPVITCNG QFPWPDITVN
KGDRVQIYLT NGMNNTNTSM HFHGLFQNGT ASMDGVPFLT QCPIAPGSTM LYNFTVDYNV
GTYWYHSHTD GQYEDGMKGL FIIKDDSFPY DYDEELSLSL SEWYHDLVTD LTKSFMSVYN
PTGAEPIPQN LIVNNTMNLT WEVQPDTTYL LRIVNVGGFV SQYFWIEDHE MTVVEIDGIT
TEKNVTDMLY ITVAQRYTVL VHTKNDTDKN FAIMQKFDDT MLDVIPSDLQ LNATSYMVYN
KTAALPTQNY VDSIDNFLDD FYLQPYEKEA IYGEPDHVIT VDVVMDNLKN GVNYAFFNNI
TYTAPKVPTL MTVLSSGDQA NNSEIYGSNT HTFILEKDEI VEIVLNNQDT GTHPFHLHGH
AFQTIQRDRT YDDALGEVPH SFDPDNHPAF PEYPMRRDTL YVRPQSNFVI RFKADNPGVW
FFHCHIEWHL LQGLGLVLVE DPFGIQDAHS QQLSENHLEV CQSCSVATEG NAAANTLDLT
DLTGENVQHA FIPTGFTKKG IIAMTFSCFA GILGIITIAI YGMMDMEDAT EKVIRDLHVD
PEVLLNEVDE NEERQVNEDR HSTEKHQFLT KAKRFF
