ARO10_YEAST
ID ARO10_YEAST Reviewed; 635 AA.
AC Q06408; D6VT13;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Transaminated amino acid decarboxylase;
DE EC=4.1.1.- {ECO:0000269|PubMed:15933030};
DE EC=4.1.1.43 {ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:21501384};
DE EC=4.1.1.72 {ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:12499363};
DE EC=4.1.1.74 {ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:21501384};
DE EC=4.1.1.80 {ECO:0000269|PubMed:21501384};
DE AltName: Full=Thiamine diphosphate-dependent phenylpyruvate decarboxylase {ECO:0000303|PubMed:21501384};
DE Short=PPDC {ECO:0000303|PubMed:21501384};
DE AltName: Full=Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase;
DE Short=2ODC;
DE AltName: Full=Transaminated branched-chain amino acid decarboxylase;
GN Name=ARO10; OrderedLocusNames=YDR380W; ORFNames=D9481.3;
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 PROTEIN SEQUENCE OF 3-10, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21501384; DOI=10.1111/j.1742-4658.2011.08103.x;
RA Kneen M.M., Stan R., Yep A., Tyler R.P., Saehuan C., McLeish M.J.;
RT "Characterization of a thiamin diphosphate-dependent phenylpyruvate
RT decarboxylase from Saccharomyces cerevisiae.";
RL FEBS J. 278:1842-1853(2011).
RN [4]
RP FUNCTION, AND REGULATION OF EXPRESSION.
RX PubMed=10207060; DOI=10.1128/mcb.19.5.3360;
RA Iraqui I., Vissers S., Andre B., Urrestarazu A.;
RT "Transcriptional induction by aromatic amino acids in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 19:3360-3371(1999).
RN [5]
RP ROLE IN ISOLEUCINE CATABOLISM.
RX PubMed=10753893; DOI=10.1074/jbc.275.15.10937;
RA Dickinson J.R., Harrison S.J., Dickinson J.A., Hewlins M.J.;
RT "An investigation of the metabolism of isoleucine to active Amyl alcohol in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:10937-10942(2000).
RN [6]
RP CHARACTERIZATION.
RX PubMed=12902239; DOI=10.1128/aem.69.8.4534-4541.2003;
RA Vuralhan Z., Morais M.A., Tai S.L., Piper M.D., Pronk J.T.;
RT "Identification and characterization of phenylpyruvate decarboxylase genes
RT in Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 69:4534-4541(2003).
RN [7]
RP ROLE IN PHENYLALANINE; TRYPTOPHAN AND LEUCINE CATABOLISM.
RX PubMed=12499363; DOI=10.1074/jbc.m211914200;
RA Dickinson J.R., Salgado L.E., Hewlins M.J.;
RT "The catabolism of amino acids to long chain and complex alcohols in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:8028-8034(2003).
RN [8]
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 [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-588, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CEN.PK113-7D;
RX PubMed=15933030; DOI=10.1128/aem.71.6.3276-3284.2005;
RA Vuralhan Z., Luttik M.A., Tai S.L., Boer V.M., Morais M.A., Schipper D.,
RA Almering M.J., Koetter P., Dickinson J.R., Daran J.M., Pronk J.T.;
RT "Physiological characterization of the ARO10-dependent, broad-substrate-
RT specificity 2-oxo acid decarboxylase activity of Saccharomyces
RT cerevisiae.";
RL Appl. Environ. Microbiol. 71:3276-3284(2005).
RN [12]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22904058; DOI=10.1128/aem.01675-12;
RA Romagnoli G., Luttik M.A., Koetter P., Pronk J.T., Daran J.M.;
RT "Substrate specificity of thiamine pyrophosphate-dependent 2-oxo-acid
RT decarboxylases in Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 78:7538-7548(2012).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6,
CC ARO10, and THI3) involved in amino acid catabolism. The enzyme
CC catalyzes the decarboxylation of amino acids, which, in a first step,
CC have been transaminated to the corresponding 2-oxo acids (alpha-keto-
CC acids). In a third step, the resulting aldehydes are reduced to
CC alcohols, collectively referred to as fusel oils or alcohols. Its
CC preferred substrates are the transaminated amino acids derived from
CC phenylalanine (phenylpyruvate), tryptophan (3-(indol-3-yl)pyruvate),
CC and probably tyrosine (4-hydroxyphenylpyruvate), but also isoleucine
CC ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate)
CC and methionine (4-methylthio-2-oxobutanoate), whereas transaminated
CC leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) is a
CC low efficiency substrate and transaminated valine and pyruvate are no
CC substrates. In analogy to the pyruvate decarboxylases the enzyme may in
CC a side-reaction catalyze condensation (or carboligation) reactions
CC leading to the formation of 2-hydroxy ketone, collectively called
CC acyloins. {ECO:0000269|PubMed:10207060, ECO:0000269|PubMed:10753893,
CC ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:15933030,
CC ECO:0000269|PubMed:21501384}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methyl-2-oxopentanoate + H(+) = 3-methylbutanal + CO2;
CC Xref=Rhea:RHEA:54360, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16638, ChEBI:CHEBI:17865; EC=4.1.1.72;
CC Evidence={ECO:0000269|PubMed:12499363};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2;
CC Xref=Rhea:RHEA:21108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16182,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:35146; EC=4.1.1.72;
CC Evidence={ECO:0000269|PubMed:10753893};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde;
CC Xref=Rhea:RHEA:18017, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:18086; EC=4.1.1.74;
CC Evidence={ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:21501384};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2;
CC Xref=Rhea:RHEA:14185, ChEBI:CHEBI:15378, ChEBI:CHEBI:16424,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005; EC=4.1.1.43;
CC Evidence={ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:21501384};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylsulfanyl-2-oxobutanoate + H(+) = 3-
CC methylsulfanylpropanal + CO2; Xref=Rhea:RHEA:55076,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16723,
CC ChEBI:CHEBI:49017; Evidence={ECO:0000269|PubMed:15933030,
CC ECO:0000269|PubMed:21501384};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(4-hydroxyphenyl)pyruvate + H(+) = (4-
CC hydroxyphenyl)acetaldehyde + CO2; Xref=Rhea:RHEA:18697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15621, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:36242; EC=4.1.1.80;
CC Evidence={ECO:0000269|PubMed:21501384};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for phenylpyruvate {ECO:0000269|PubMed:22904058};
CC KM=12 mM for 3-methyl-2-oxobutanoate {ECO:0000269|PubMed:22904058};
CC KM=2.1 mM for 4-methyl-2-oxopentanoate {ECO:0000269|PubMed:22904058};
CC KM=4.7 mM for 3-methyl-2-oxopentanoate {ECO:0000269|PubMed:22904058};
CC KM=5.36 mM for 4-methylthio-2-oxobutanoate
CC {ECO:0000269|PubMed:22904058};
CC KM=0.03 mM for 3-(indol-3-yl)pyruvate {ECO:0000269|PubMed:21501384};
CC KM=0.09 mM for 4-hydroxyphenylpyruvate {ECO:0000269|PubMed:21501384};
CC Vmax=201 umol/min/mg enzyme for phenylpyruvate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=103 umol/min/mg enzyme for 3-methyl-2-oxobutanoate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=103 umol/min/mg enzyme for 4-methyl-2-oxopentanoate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=103 umol/min/mg enzyme for 3-methyl-2-oxopentanoate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=85 umol/min/mg enzyme for 4-methylthio-2-oxobutanoate
CC {ECO:0000269|PubMed:22904058};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:21501384};
CC -!- PATHWAY: Amino-acid degradation; Ehrlich pathway.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is induced by the presence of aromatic amino
CC acids and the lack of preferred nitrogen sources (e.g. ammonia,
CC glutamine) and requires the transcription activator ARO80.
CC -!- BIOTECHNOLOGY: Fusel oils are important flavor and aroma compounds in
CC yeast-fermented products contributing to the quality of beverages and
CC food. In low concentration they are generally desirable, whereas high
CC concentrations may spoil the product. By adjusting growth conditions
CC and substrate their production is sought to be influenced.
CC Phenylethanol, having a rose-like aroma, is an important fragrance in
CC the cosmetic industry and can be produced by fermentation.
CC -!- MISCELLANEOUS: Present with 6560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; U28373; AAB64816.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12223.1; -; Genomic_DNA.
DR PIR; S61175; S61175.
DR RefSeq; NP_010668.3; NM_001180688.3.
DR AlphaFoldDB; Q06408; -.
DR SMR; Q06408; -.
DR BioGRID; 32440; 47.
DR DIP; DIP-5252N; -.
DR IntAct; Q06408; 4.
DR MINT; Q06408; -.
DR STRING; 4932.YDR380W; -.
DR iPTMnet; Q06408; -.
DR MaxQB; Q06408; -.
DR PaxDb; Q06408; -.
DR PRIDE; Q06408; -.
DR EnsemblFungi; YDR380W_mRNA; YDR380W; YDR380W.
DR GeneID; 851987; -.
DR KEGG; sce:YDR380W; -.
DR SGD; S000002788; ARO10.
DR VEuPathDB; FungiDB:YDR380W; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q06408; -.
DR OMA; AQEISVM; -.
DR BioCyc; MetaCyc:MON3O-398; -.
DR BioCyc; YEAST:MON3O-398; -.
DR BRENDA; 4.1.1.43; 984.
DR UniPathway; UPA00866; -.
DR PRO; PR:Q06408; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06408; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0050546; F:4-hydroxyphenylpyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0047433; F:branched-chain-2-oxoacid decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016831; F:carboxy-lyase activity; IMP:SGD.
DR GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050177; F:phenylpyruvate decarboxylase activity; IDA:SGD.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
DR GO; GO:0000950; P:branched-chain amino acid catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IDA:SGD.
DR GO; GO:0006552; P:leucine catabolic process; IMP:SGD.
DR GO; GO:0000951; P:methionine catabolic process to 3-methylthiopropanol; IMP:SGD.
DR GO; GO:0006569; P:tryptophan catabolic process; IGI:SGD.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR012110; TPP_enzyme.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR43452; PTHR43452; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
PE 1: Evidence at protein level;
KW Branched-chain amino acid catabolism; Cytoplasm; Decarboxylase;
KW Direct protein sequencing; Isopeptide bond; Lyase; Magnesium;
KW Metal-binding; Phenylalanine catabolism; Reference proteome;
KW Thiamine pyrophosphate; Tryptophan catabolism; Tyrosine catabolism;
KW Ubl conjugation.
FT CHAIN 1..635
FT /note="Transaminated amino acid decarboxylase"
FT /id="PRO_0000090835"
FT CROSSLNK 588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
SQ SEQUENCE 635 AA; 71384 MW; 616DF7E06DA82415 CRC64;
MAPVTIEKFV NQEERHLVSN RSATIPFGEY IFKRLLSIDT KSVFGVPGDF NLSLLEYLYS
PSVESAGLRW VGTCNELNAA YAADGYSRYS NKIGCLITTY GVGELSALNG IAGSFAENVK
VLHIVGVAKS IDSRSSNFSD RNLHHLVPQL HDSNFKGPNH KVYHDMVKDR VACSVAYLED
IETACDQVDN VIRDIYKYSK PGYIFVPADF ADMSVTCDNL VNVPRISQQD CIVYPSENQL
SDIINKITSW IYSSKTPAIL GDVLTDRYGV SNFLNKLICK TGIWNFSTVM GKSVIDESNP
TYMGQYNGKE GLKQVYEHFE LCDLVLHFGV DINEINNGHY TFTYKPNAKI IQFHPNYIRL
VDTRQGNEQM FKGINFAPIL KELYKRIDVS KLSLQYDSNV TQYTNETMRL EDPTNGQSSI
ITQVHLQKTM PKFLNPGDVV VCETGSFQFS VRDFAFPSQL KYISQGFFLS IGMALPAALG
VGIAMQDHSN AHINGGNVKE DYKPRLILFE GDGAAQMTIQ ELSTILKCNI PLEVIIWNNN
GYTIERAIMG PTRSYNDVMS WKWTKLFEAF GDFDGKYTNS TLIQCPSKLA LKLEELKNSN
KRSGIELLEV KLGELDFPEQ LKCMVEAAAL KRNKK
