FDC1_YEAST
ID FDC1_YEAST Reviewed; 503 AA.
AC Q03034; D6VTF8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ferulic acid decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000303|PubMed:20471595};
DE EC=4.1.1.102 {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:20471595, ECO:0000269|PubMed:25647642, ECO:0000269|PubMed:25862228, ECO:0000269|PubMed:26083754};
DE AltName: Full=Phenacrylate decarboxylase {ECO:0000255|HAMAP-Rule:MF_03196};
GN Name=FDC1 {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000303|PubMed:20471595};
GN OrderedLocusNames=YDR539W {ECO:0000312|SGD:S000002947}; ORFNames=D3703.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=20471595; DOI=10.1016/j.jbiosc.2009.11.011;
RA Mukai N., Masaki K., Fujii T., Kawamukai M., Iefuji H.;
RT "PAD1 and FDC1 are essential for the decarboxylation of phenylacrylic acids
RT in Saccharomyces cerevisiae.";
RL J. Biosci. Bioeng. 109:564-569(2010).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MASS SPECTROMETRY.
RX PubMed=25647642; DOI=10.1021/cb5008103;
RA Lin F., Ferguson K.L., Boyer D.R., Lin X.N., Marsh E.N.;
RT "Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor
RT required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic
RT acid decarboxylase.";
RL ACS Chem. Biol. 10:1137-1144(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), SUBUNIT, MUTAGENESIS OF GLU-285,
RP ACTIVE SITE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25862228; DOI=10.1128/aem.00762-15;
RA Bhuiya M.W., Lee S.G., Jez J.M., Yu O.;
RT "Structure and mechanism of ferulic acid decarboxylase (FDC1) from
RT Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 81:4216-4223(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH PRFMN AND MANGANESE.
RX PubMed=26083754; DOI=10.1038/nature14560;
RA Payne K.A., White M.D., Fisher K., Khara B., Bailey S.S., Parker D.,
RA Rattray N.J., Trivedi D.K., Goodacre R., Beveridge R., Barran P.,
RA Rigby S.E., Scrutton N.S., Hay S., Leys D.;
RT "New cofactor supports alpha,beta-unsaturated acid decarboxylation via 1,3-
RT dipolar cycloaddition.";
RL Nature 522:497-501(2015).
CC -!- FUNCTION: Catalyzes the reversible decarboxylation of aromatic
CC carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid,
CC producing the corresponding vinyl derivatives 4-vinylphenol, 4-
CC vinylguaiacol, and styrene, respectively, which play the role of aroma
CC metabolites (PubMed:20471595, PubMed:25647642). Not essential for
CC ubiquinone synthesis (PubMed:20471595). {ECO:0000255|HAMAP-
CC Rule:MF_03196, ECO:0000269|PubMed:20471595,
CC ECO:0000269|PubMed:25647642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + H(+) = 4-hydroxystyrene + CO2;
CC Xref=Rhea:RHEA:33227, ChEBI:CHEBI:1883, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; EC=4.1.1.102;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:20471595, ECO:0000269|PubMed:25647642,
CC ECO:0000269|PubMed:25862228, ECO:0000269|PubMed:26083754};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + H(+) = CO2 + styrene; Xref=Rhea:RHEA:46920,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15669, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:27452; EC=4.1.1.102; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03196, ECO:0000269|PubMed:20471595,
CC ECO:0000269|PubMed:25647642, ECO:0000269|PubMed:25862228,
CC ECO:0000269|PubMed:26083754};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-ferulate + H(+) = 2-methoxy-4-vinylphenol + CO2;
CC Xref=Rhea:RHEA:33807, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29749, ChEBI:CHEBI:42438; EC=4.1.1.102;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:20471595, ECO:0000269|PubMed:25647642,
CC ECO:0000269|PubMed:25862228, ECO:0000269|PubMed:26083754};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:26083754};
CC -!- COFACTOR:
CC Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:26083754};
CC Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for ferulic acid {ECO:0000269|PubMed:25647642};
CC KM=0.79 mM for ferulic acid {ECO:0000269|PubMed:25862228};
CC KM=110 uM for p-coumaric acid {ECO:0000269|PubMed:25647642};
CC KM=0.92 mM for p-coumaric acid {ECO:0000269|PubMed:25862228};
CC KM=180 uM for cinnamic acid {ECO:0000269|PubMed:25647642};
CC Vmax=6.8 nmol/min/mg enzyme for ferulic acid
CC {ECO:0000269|PubMed:25862228};
CC Vmax=7.2 nmol/min/mg enzyme for p-coumaric acid
CC {ECO:0000269|PubMed:25862228};
CC Note=kcat is 3.8 sec(-1) with ferulic acid as substrate, 1.5 sec(-1)
CC with p-coumaric acid as substrate and 4.6 sec(-1) with cinnamic acid
CC as substrate. {ECO:0000269|PubMed:25647642};
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:25647642};
CC -!- SUBUNIT: Homodimer (PubMed:25862228). May form higher order oligomers
CC (PubMed:25647642). {ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:25647642, ECO:0000269|PubMed:25862228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03196,
CC ECO:0000269|PubMed:14562095}.
CC -!- MASS SPECTROMETRY: Mass=57898; Method=Electrospray; Note=The measured
CC mass includes the mass of an N-terminal hexahistidine tag, expressed in
CC E.coli.; Evidence={ECO:0000269|PubMed:25647642};
CC -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UbiD family. UbiD-like/FDC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000305}.
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DR EMBL; U43834; AAB64981.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12368.1; -; Genomic_DNA.
DR PIR; S62018; S62018.
DR RefSeq; NP_010828.1; NM_001180847.1.
DR PDB; 4S13; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-503.
DR PDB; 4ZAC; X-ray; 1.65 A; A/B/C/D=1-503.
DR PDB; 6EVE; X-ray; 2.05 A; A/B/C/D=1-503.
DR PDB; 6EVF; X-ray; 2.06 A; A/B/C/D=1-503.
DR PDBsum; 4S13; -.
DR PDBsum; 4ZAC; -.
DR PDBsum; 6EVE; -.
DR PDBsum; 6EVF; -.
DR AlphaFoldDB; Q03034; -.
DR SMR; Q03034; -.
DR BioGRID; 32586; 41.
DR DIP; DIP-7852N; -.
DR IntAct; Q03034; 7.
DR STRING; 4932.YDR539W; -.
DR MaxQB; Q03034; -.
DR PaxDb; Q03034; -.
DR PRIDE; Q03034; -.
DR EnsemblFungi; YDR539W_mRNA; YDR539W; YDR539W.
DR GeneID; 852152; -.
DR KEGG; sce:YDR539W; -.
DR SGD; S000002947; FDC1.
DR VEuPathDB; FungiDB:YDR539W; -.
DR eggNOG; ENOG502QR5I; Eukaryota.
DR GeneTree; ENSGT00940000176404; -.
DR HOGENOM; CLU_023348_0_0_1; -.
DR InParanoid; Q03034; -.
DR OMA; TEGGCCW; -.
DR BioCyc; MetaCyc:G3O-30047-MON; -.
DR BioCyc; YEAST:G3O-30047-MON; -.
DR BRENDA; 4.1.1.102; 984.
DR PRO; PR:Q03034; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03034; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046281; P:cinnamic acid catabolic process; IMP:SGD.
DR GO; GO:1901067; P:ferulate catabolic process; EXP:CACAO.
DR GO; GO:0033494; P:ferulate metabolic process; IDA:SGD.
DR HAMAP; MF_01983; UbiD_FDC; 1.
DR InterPro; IPR002830; UbiD.
DR InterPro; IPR032903; UbiD/Fdc1.
DR PANTHER; PTHR30108; PTHR30108; 1.
DR Pfam; PF01977; UbiD; 1.
DR TIGRFAMs; TIGR00148; TIGR00148; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Decarboxylase; Flavoprotein; FMN; Lyase;
KW Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..503
FT /note="Ferulic acid decarboxylase 1"
FT /id="PRO_0000157387"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A2QHE5, ECO:0000255|HAMAP-
FT Rule:MF_03196, ECO:0000305|PubMed:25862228"
FT BINDING 170..175
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 192..193
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 236
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT BINDING 394
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03196,
FT ECO:0000269|PubMed:26083754"
FT MUTAGEN 285
FT /note="E->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:25862228"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:4ZAC"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 265..280
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 296..308
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 330..345
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:4ZAC"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:4ZAC"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 459..465
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:4ZAC"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:6EVF"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:4ZAC"
FT HELIX 487..500
FT /evidence="ECO:0007829|PDB:4ZAC"
SQ SEQUENCE 503 AA; 56164 MW; 379B19319930B84F CRC64;
MRKLNPALEF RDFIQVLKDE DDLIEITEEI DPNLEVGAIM RKAYESHLPA PLFKNLKGAS
KDLFSILGCP AGLRSKEKGD HGRIAHHLGL DPKTTIKEII DYLLECKEKE PLPPITVPVS
SAPCKTHILS EEKIHLQSLP TPYLHVSDGG KYLQTYGMWI LQTPDKKWTN WSIARGMVVD
DKHITGLVIK PQHIRQIADS WAAIGKANEI PFALCFGVPP AAILVSSMPI PEGVSESDYV
GAILGESVPV VKCETNDLMV PATSEMVFEG TLSLTDTHLE GPFGEMHGYV FKSQGHPCPL
YTVKAMSYRD NAILPVSNPG LCTDETHTLI GSLVATEAKE LAIESGLPIL DAFMPYEAQA
LWLILKVDLK GLQALKTTPE EFCKKVGDIY FRTKVGFIVH EIILVADDID IFNFKEVIWA
YVTRHTPVAD QMAFDDVTSF PLAPFVSQSS RSKTMKGGKC VTNCIFRQQY ERSFDYITCN
FEKGYPKGLV DKVNENWKRY GYK
