FRE1_YEAST
ID FRE1_YEAST Reviewed; 686 AA.
AC P32791; D6VYL5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Ferric/cupric reductase transmembrane component 1 {ECO:0000305};
DE EC=1.16.1.9 {ECO:0000269|PubMed:11120744, ECO:0000269|PubMed:1431884, ECO:0000269|PubMed:15288128, ECO:0000269|PubMed:8662826, ECO:0000269|PubMed:8662973};
DE AltName: Full=Ferric-chelate reductase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=FRE1; OrderedLocusNames=YLR214W; ORFNames=L8167.2;
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=F113;
RX PubMed=1570306; DOI=10.1073/pnas.89.9.3869;
RA Dancis A., Roman D.G., Anderson G.J., Hinnebusch A.G., Klausner R.D.;
RT "Ferric reductase of Saccharomyces cerevisiae: molecular characterization,
RT role in iron uptake, and transcriptional control by iron.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3869-3873(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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, CATALYTIC ACTIVITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1431884; DOI=10.1016/0162-0134(92)84070-4;
RA Anderson G.J., Lesuisse E., Dancis A., Roman D.G., Labbe P., Klausner R.D.;
RT "Ferric iron reduction and iron assimilation in Saccharomyces cerevisiae.";
RL J. Inorg. Biochem. 47:249-255(1992).
RN [5]
RP INDUCTION.
RX PubMed=7720713; DOI=10.1002/j.1460-2075.1995.tb07106.x;
RA Yamaguchi-Iwai Y., Dancis A., Klausner R.D.;
RT "AFT1: a mediator of iron regulated transcriptional control in
RT Saccharomyces cerevisiae.";
RL EMBO J. 14:1231-1239(1995).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=7814363; DOI=10.1074/jbc.270.1.128;
RA Hassett R., Kosman D.J.;
RT "Evidence for Cu(II) reduction as a component of copper uptake by
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:128-134(1995).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8662826; DOI=10.1074/jbc.271.23.13578;
RA Lesuisse E., Casteras-Simon M., Labbe P.;
RT "Evidence for the Saccharomyces cerevisiae ferrireductase system being a
RT multicomponent electron transport chain.";
RL J. Biol. Chem. 271:13578-13583(1996).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=8662973; DOI=10.1074/jbc.271.24.14240;
RA Shatwell K.P., Dancis A., Cross A.R., Klausner R.D., Segal A.W.;
RT "The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome b
RT similar to that of NADPH oxidase.";
RL J. Biol. Chem. 271:14240-14244(1996).
RN [9]
RP HEME BINDING, AND MUTAGENESIS OF HIS-294; HIS-308; HIS-364 AND HIS-378.
RX PubMed=8940093; DOI=10.1074/jbc.271.49.31021;
RA Finegold A.A., Shatwell K.P., Segal A.W., Klausner R.D., Dancis A.;
RT "Intramembrane bis-heme motif for transmembrane electron transport
RT conserved in a yeast iron reductase and the human NADPH oxidase.";
RL J. Biol. Chem. 271:31021-31024(1996).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=9153234; DOI=10.1074/jbc.272.21.13786;
RA Georgatsou E., Mavrogiannis L.A., Fragiadakis G.S., Alexandraki D.;
RT "The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are
RT regulated by the copper-modulated Mac1p activator.";
RL J. Biol. Chem. 272:13786-13792(1997).
RN [11]
RP INDUCTION.
RX PubMed=9200812;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<621::aid-yea121>3.0.co;2-u;
RA Casas C., Aldea M., Espinet C., Gallego C., Gil R., Herrero E.;
RT "The AFT1 transcriptional factor is differentially required for expression
RT of high-affinity iron uptake genes in Saccharomyces cerevisiae.";
RL Yeast 13:621-637(1997).
RN [12]
RP INDUCTION.
RX PubMed=9726978; DOI=10.1074/jbc.273.37.23716;
RA Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RT "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:23716-23721(1998).
RN [13]
RP ERRATUM OF PUBMED:9726978.
RA Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RL J. Biol. Chem. 273:30056-30056(1998).
RN [14]
RP INDUCTION.
RX PubMed=10341420;
RX DOI=10.1002/(sici)1097-0061(199905)15:7<573::aid-yea404>3.0.co;2-7;
RA Georgatsou E., Alexandraki D.;
RT "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu
RT reductase related genes.";
RL Yeast 15:573-584(1999).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11120744; DOI=10.1074/jbc.m010065200;
RA Yun C.-W., Bauler M., Moore R.E., Klebba P.E., Philpott C.C.;
RT "The role of the FRE family of plasma membrane reductases in the uptake of
RT siderophore-iron in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:10218-10223(2001).
RN [16]
RP FUNCTION.
RX PubMed=12954629; DOI=10.1074/jbc.m307019200;
RA Shi X., Stoj C., Romeo A., Kosman D.J., Zhu Z.;
RT "Fre1p Cu2+ reduction and Fet3p Cu1+ oxidation modulate copper toxicity in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:50309-50315(2003).
RN [17]
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 [18]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=15288128; DOI=10.1016/j.freeradbiomed.2004.05.031;
RA Shinyashiki M., Pan C.J., Lopez B.E., Fukuto J.M.;
RT "Inhibition of the yeast metal reductase heme protein fre1 by nitric oxide
RT (NO): a model for inhibition of NADPH oxidase by NO.";
RL Free Radic. Biol. Med. 37:713-723(2004).
RN [19]
RP BIOTECHNOLOGY.
RX PubMed=16000801; DOI=10.1128/aem.71.7.3882-3888.2005;
RA Ramalho P.A., Paiva S., Cavaco-Paulo A., Casal M., Cardoso M.H.,
RA Ramalho M.T.;
RT "Azo reductase activity of intact Saccharomyces cerevisiae cells is
RT dependent on the Fre1p component of plasma membrane ferric reductase.";
RL Appl. Environ. Microbiol. 71:3882-3888(2005).
RN [20]
RP INDUCTION BY AFT1.
RX PubMed=16024809; DOI=10.1128/mcb.25.15.6760-6771.2005;
RA Courel M., Lallet S., Camadro J.-M., Blaiseau P.-L.;
RT "Direct activation of genes involved in intracellular iron use by the yeast
RT iron-responsive transcription factor Aft2 without its paralog Aft1.";
RL Mol. Cell. Biol. 25:6760-6771(2005).
RN [21]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17507646; DOI=10.1091/mbc.e07-03-0274;
RA Aronova S., Wedaman K., Anderson S., Yates J.R. III, Powers T.;
RT "Probing the membrane environment of the TOR kinases reveals functional
RT interactions between TORC1, actin, and membrane trafficking in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 18:2779-2794(2007).
CC -!- FUNCTION: Metalloreductase responsible for reducing extracellular iron
CC and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-
CC salts and Fe(3+) bound to catecholate or hydroxamate siderophores.
CC Fe(3+) is reduced to Fe(2+), which then dissociates from the
CC siderophore and can be imported by the high-affinity Fe(2+) transport
CC complex in the plasma membrane. Also participates in Cu(2+) reduction
CC and Cu(+) uptake. {ECO:0000269|PubMed:11120744,
CC ECO:0000269|PubMed:12954629, ECO:0000269|PubMed:1431884,
CC ECO:0000269|PubMed:1570306, ECO:0000269|PubMed:7814363,
CC ECO:0000269|PubMed:8662826, ECO:0000269|PubMed:8662973,
CC ECO:0000269|PubMed:9153234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC Evidence={ECO:0000269|PubMed:11120744, ECO:0000269|PubMed:1431884,
CC ECO:0000269|PubMed:15288128, ECO:0000269|PubMed:8662826,
CC ECO:0000269|PubMed:8662973};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8662973};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:8940093};
CC -!- ACTIVITY REGULATION: Inhibited by nitric oxide (NO).
CC {ECO:0000269|PubMed:15288128}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1431884,
CC ECO:0000269|PubMed:15288128, ECO:0000269|PubMed:17507646,
CC ECO:0000269|PubMed:8662826}; Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is repressed by the addition of iron
CC (PubMed:1570306, PubMed:1431884). Induced by transcription factor MAC1
CC upon copper deprivation (PubMed:7814363, PubMed:9153234,
CC PubMed:9726978, PubMed:10341420). Induced by transcription factor AFT1
CC upon iron deprivation (PubMed:7720713, PubMed:9200812, PubMed:9726978,
CC PubMed:10341420, PubMed:16024809). {ECO:0000269|PubMed:10341420,
CC ECO:0000269|PubMed:1431884, ECO:0000269|PubMed:1570306,
CC ECO:0000269|PubMed:16024809, ECO:0000269|PubMed:7720713,
CC ECO:0000269|PubMed:7814363, ECO:0000269|PubMed:9153234,
CC ECO:0000269|PubMed:9200812, ECO:0000269|PubMed:9726978}.
CC -!- BIOTECHNOLOGY: Responsible for the reduction of the azo bond of azo
CC dyes, making yeasts efficient azo dye decolorizers.
CC {ECO:0000269|PubMed:16000801}.
CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; M86908; AAA34608.1; -; Genomic_DNA.
DR EMBL; U14913; AAB67424.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09531.1; -; Genomic_DNA.
DR PIR; S30075; S30075.
DR RefSeq; NP_013315.1; NM_001182101.1.
DR AlphaFoldDB; P32791; -.
DR SMR; P32791; -.
DR BioGRID; 31482; 79.
DR DIP; DIP-5349N; -.
DR IntAct; P32791; 1.
DR MINT; P32791; -.
DR STRING; 4932.YLR214W; -.
DR TCDB; 5.B.1.5.1; the phagocyte (gp91(phox)) nadph oxidase family.
DR MaxQB; P32791; -.
DR PaxDb; P32791; -.
DR PRIDE; P32791; -.
DR EnsemblFungi; YLR214W_mRNA; YLR214W; YLR214W.
DR GeneID; 850911; -.
DR KEGG; sce:YLR214W; -.
DR SGD; S000004204; FRE1.
DR VEuPathDB; FungiDB:YLR214W; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000176303; -.
DR HOGENOM; CLU_010365_4_0_1; -.
DR InParanoid; P32791; -.
DR OMA; IRNNPFI; -.
DR BioCyc; MetaCyc:YLR214W-MON; -.
DR BioCyc; YEAST:YLR214W-MON; -.
DR PRO; PR:P32791; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32791; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0015677; P:copper ion import; IDA:SGD.
DR GO; GO:0006826; P:iron ion transport; IDA:SGD.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Copper transport; Electron transport; FAD;
KW Flavoprotein; Glycoprotein; Heme; Ion transport; Iron; Iron transport;
KW Membrane; Metal-binding; NADP; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..686
FT /note="Ferric/cupric reductase transmembrane component 1"
FT /id="PRO_0000010137"
FT TOPO_DOM 23..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..378
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..401
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 258..398
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000255"
FT DOMAIN 399..522
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 294
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:8940093"
FT BINDING 308
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:8940093"
FT BINDING 364
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:8940093"
FT BINDING 378
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:8940093"
FT BINDING 462..468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 514..517
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 652..653
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 294
FT /note="H->A: Impairs heme binding."
FT /evidence="ECO:0000269|PubMed:8940093"
FT MUTAGEN 308
FT /note="H->A: Impairs heme binding."
FT /evidence="ECO:0000269|PubMed:8940093"
FT MUTAGEN 364
FT /note="H->A: Impairs heme binding."
FT /evidence="ECO:0000269|PubMed:8940093"
FT MUTAGEN 378
FT /note="H->A: Impairs heme binding."
FT /evidence="ECO:0000269|PubMed:8940093"
SQ SEQUENCE 686 AA; 78854 MW; 7F6BB3B93A95D6A3 CRC64;
MVRTRVLFCL FISFFATVQS SATLISTSCI SQAALYQFGC SSKSKSCYCK NINWLGSVTA
CAYENSKSNK TLDSALMKLA SQCSSIKVYT LEDMKNIYLN ASNYLRAPEK SDKKTVVSQP
LMANETAYHY YYEENYGIHL NLMRSQWCAW GLVFFWVAVL TAATILNILK RVFGKNIMAN
SVKKSLIYPS VYKDYNERTF YLWKRLPFNF TTRGKGLVVL IFVILTILSL SFGHNIKLPH
PYDRPRWRRS MAFVSRRADL MAIALFPVVY LFGIRNNPFI PITGLSFSTF NFYHKWSAYV
CFMLAVVHSI VMTASGVKRG VFQSLVRKFY FRWGIVATIL MSIIIFQSEK VFRNRGYEIF
LLIHKAMNIM FIIAMYYHCH TLGWMGWIWS MAGILCFDRF CRIVRIIMNG GLKTATLSTT
DDSNVIKISV KKPKFFKYQV GAFAYMYFLS PKSAWFYSFQ SHPFTVLSER HRDPNNPDQL
TMYVKANKGI TRVLLSKVLS APNHTVDCKI FLEGPYGVTV PHIAKLKRNL VGVAAGLGVA
AIYPHFVECL RLPSTDQLQH KFYWIVNDLS HLKWFENELQ WLKEKSCEVS VIYTGSSVED
TNSDESTKGF DDKEESEITV ECLNKRPDLK ELVRSEIKLS ELENNNITFY SCGPATFNDD
FRNAVVQGID SSLKIDVELE EESFTW
