CHO2_YEAST
ID CHO2_YEAST Reviewed; 869 AA.
AC P05374; D6VUT7;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000303|PubMed:2445736};
DE Short=PE methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000303|PubMed:2445736};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000303|PubMed:1954254};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639, ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
DE AltName: Full=Choline-requiring protein 2 {ECO:0000305|PubMed:3066687};
GN Name=CHO2 {ECO:0000303|PubMed:3066687};
GN Synonyms=PEM1 {ECO:0000303|PubMed:2445736};
GN OrderedLocusNames=YGR157W {ECO:0000312|SGD:S000003389}; ORFNames=G6673;
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, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=2445736; DOI=10.1016/s0021-9258(18)47744-7;
RA Kodaki T., Yamashita S.;
RT "Yeast phosphatidylethanolamine methylation pathway. Cloning and
RT characterization of two distinct methyltransferase genes.";
RL J. Biol. Chem. 262:15428-15435(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=6988218; DOI=10.1111/j.1432-1033.1980.tb04465.x;
RA Yamashita S., Oshima A.;
RT "Regulation of phosphatidylethanolamine methyltransferase level by myo-
RT inositol in Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 104:611-616(1980).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=6759124; DOI=10.1111/j.1432-1033.1982.tb07005.x;
RA Yamashita S., Oshima A., Nikawa J., Hosaka K.;
RT "Regulation of the phosphatidylethanolamine methylation pathway in
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 128:589-595(1982).
RN [7]
RP FUNCTION, AND PATHWAY.
RX PubMed=3066687; DOI=10.1093/genetics/120.4.909;
RA Summers E.F., Letts V.A., McGraw P., Henry S.A.;
RT "Saccharomyces cerevisiae cho2 mutants are deficient in phospholipid
RT methylation and cross-pathway regulation of inositol synthesis.";
RL Genetics 120:909-922(1988).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2684666; DOI=10.1111/j.1432-1033.1989.tb15109.x;
RA Kodaki T., Yamashita S.;
RT "Characterization of the methyltransferases in the yeast
RT phosphatidylethanolamine methylation pathway by selective gene
RT disruption.";
RL Eur. J. Biochem. 185:243-251(1989).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=2198947; DOI=10.1016/0005-2760(90)90145-n;
RA Gaynor P.M., Carman G.M.;
RT "Phosphatidylethanolamine methyltransferase and phospholipid
RT methyltransferase activities from Saccharomyces cerevisiae. Enzymological
RT and kinetic properties.";
RL Biochim. Biophys. Acta 1045:156-163(1990).
RN [10]
RP INDUCTION.
RX PubMed=1954254; DOI=10.1016/0167-4781(91)90197-t;
RA Gaynor P.M., Gill T., Toutenhoofd S., Summers E.F., McGraw P., Homann M.J.,
RA Henry S.A., Carman G.M.;
RT "Regulation of phosphatidylethanolamine methyltransferase and phospholipid
RT methyltransferase by phospholipid precursors in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1090:326-332(1991).
RN [11]
RP INDUCTION.
RX PubMed=1650774;
RA Kodaki T., Hosaka K., Nikawa J., Yamashita S.;
RT "Identification of the upstream activation sequences responsible for the
RT expression and regulation of the PEM1 and PEM2 genes encoding the enzymes
RT of the phosphatidylethanolamine methylation pathway in Saccharomyces
RT cerevisiae.";
RL J. Biochem. 109:276-287(1991).
RN [12]
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 [13]
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 [14]
RP FUNCTION.
RX PubMed=15258140; DOI=10.1074/jbc.m406517200;
RA Boumann H.A., Chin P.T., Heck A.J., De Kruijff B., De Kroon A.I.;
RT "The yeast phospholipid N-methyltransferases catalyzing the synthesis of
RT phosphatidylcholine preferentially convert di-C16:1 substrates both in vivo
RT and in vitro.";
RL J. Biol. Chem. 279:40314-40319(2004).
RN [15]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [16]
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 [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22001639; DOI=10.1016/j.bbalip.2011.09.018;
RA Bilgin M., Markgraf D.F., Duchoslav E., Knudsen J., Jensen O.N.,
RA de Kroon A.I., Ejsing C.S.;
RT "Quantitative profiling of PE, MMPE, DMPE, and PC lipid species by multiple
RT precursor ion scanning: a tool for monitoring PE metabolism.";
RL Biochim. Biophys. Acta 1811:1081-1089(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Catalyzes the first step of the methylation pathway of
CC phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine
CC (PMME). Preferentially converts di-C16:1 substrates.
CC {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:15258140,
CC ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639,
CC ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666,
CC ECO:0000269|PubMed:3066687, ECO:0000269|PubMed:6759124,
CC ECO:0000269|PubMed:6988218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03217,
CC ECO:0000269|PubMed:2198947, ECO:0000269|PubMed:22001639,
CC ECO:0000269|PubMed:2445736, ECO:0000269|PubMed:2684666};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:2684666};
CC KM=110 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:2198947};
CC KM=57 uM for phosphatidylethanolamine (PE)
CC {ECO:0000269|PubMed:2198947};
CC pH dependence:
CC Optimum pH is 9.9. {ECO:0000269|PubMed:2684666};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000305|PubMed:2445736,
CC ECO:0000305|PubMed:3066687}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:14562095}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03217}.
CC -!- INDUCTION: Repressed by myo-inositol and choline.
CC {ECO:0000269|PubMed:1650774, ECO:0000269|PubMed:1954254,
CC ECO:0000269|PubMed:6759124, ECO:0000269|PubMed:6988218}.
CC -!- MISCELLANEOUS: Present with 1810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000255|HAMAP-Rule:MF_03217}.
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DR EMBL; M16987; AAA34850.1; -; Genomic_DNA.
DR EMBL; X85807; CAA59814.1; -; Genomic_DNA.
DR EMBL; Z72942; CAA97171.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08248.1; -; Genomic_DNA.
DR PIR; A28443; A28443.
DR RefSeq; NP_011673.1; NM_001181286.1.
DR AlphaFoldDB; P05374; -.
DR BioGRID; 33405; 715.
DR DIP; DIP-8037N; -.
DR IntAct; P05374; 2.
DR MINT; P05374; -.
DR STRING; 4932.YGR157W; -.
DR SwissLipids; SLP:000000085; -.
DR iPTMnet; P05374; -.
DR MaxQB; P05374; -.
DR PaxDb; P05374; -.
DR PRIDE; P05374; -.
DR EnsemblFungi; YGR157W_mRNA; YGR157W; YGR157W.
DR GeneID; 853061; -.
DR KEGG; sce:YGR157W; -.
DR SGD; S000003389; CHO2.
DR VEuPathDB; FungiDB:YGR157W; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR InParanoid; P05374; -.
DR OMA; LAWEQTE; -.
DR BioCyc; MetaCyc:YGR157W-MON; -.
DR BioCyc; YEAST:YGR157W-MON; -.
DR UniPathway; UPA00753; -.
DR PRO; PR:P05374; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P05374; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
DR HAMAP; MF_03217; PEMT; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 1.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Methyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..869
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000058304"
FT TOPO_DOM 2..55
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 77..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 108..187
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 209..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 234..258
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 280..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 292..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 311..362
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 384..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 411..439
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 461..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 485..534
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 556..869
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217,
FT ECO:0000269|PubMed:16847258"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 869 AA; 101204 MW; A273F179B4E46A20 CRC64;
MSSCKTTLSE MVGSVTKDRG TINVEARTRS SNVTFKPPVT HDMVRSLFDP TLKKSLLEKC
IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN LGIGLVLHYQ SHYETLTNCA
KTHAIFSKIP QNKDANSNFS TNSNSFSEKF WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN
VWLIFRQFVD LILMQDFVTY IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV
VKDYAWYWGD FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH
YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN MGLSFNNFNK
LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL VSWLFISTIL YKQSQSKWFT
RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT LMIIHTGLQI WSNFSNINNS QLIFGLILVA
LQTWCDKETR LAISDFGWFY GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL
MTNFAVTNII LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI
VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR LSPYCELKIE
NEQVETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR ADREKTRVGS GGHWSATSKD
SYMNHGLRHK ESVTEIKATE KYVQGKVTFD TSLLYFENGI YEFRYHSGNS HKVLLISTPF
EISLPVLNTT TPELFEKDLT EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS
SEYMRRVNGD AHVISHRAWD IKQTLDSLA
