PES1_ARATH
ID PES1_ARATH Reviewed; 704 AA.
AC Q9ZVN2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Phytyl ester synthase 1, chloroplastic {ECO:0000303|PubMed:22623494};
DE EC=2.3.1.- {ECO:0000269|PubMed:22623494};
DE Flags: Precursor;
GN Name=PES1 {ECO:0000303|PubMed:22623494};
GN OrderedLocusNames=At1g54570 {ECO:0000312|Araport:AT1G54570};
GN ORFNames=T22H22.2 {ECO:0000312|EMBL:AAC64874.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INDUCTION BY NITROGEN
RP DEPRIVATION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=22623494; DOI=10.1105/tpc.112.095588;
RA Lippold F., vom Dorp K., Abraham M., Hoelzl G., Wewer V., Yilmaz J.L.,
RA Lager I., Montandon C., Besagni C., Kessler F., Stymne S., Doermann P.;
RT "Fatty acid phytyl ester synthesis in chloroplasts of Arabidopsis.";
RL Plant Cell 24:2001-2014(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=22274653; DOI=10.1104/pp.111.193144;
RA Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA van Wijk K.J.;
RT "The functional network of the Arabidopsis plastoglobule proteome based on
RT quantitative proteomics and genome-wide coexpression analysis.";
RL Plant Physiol. 158:1172-1192(2012).
RN [9]
RP INTERACTION WITH PGM48.
RX PubMed=27895226; DOI=10.1105/tpc.16.00745;
RA Bhuiyan N.H., Friso G., Rowland E., Majsec K., van Wijk K.J.;
RT "The plastoglobule-localized metallopeptidase PGM48 is a positive regulator
RT of senescence in Arabidopsis thaliana.";
RL Plant Cell 28:3020-3037(2016).
RN [10]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=28534654; DOI=10.1080/15592324.2017.1331197;
RA Bhuiyan N.H., van Wijk K.J.;
RT "Functions and substrates of plastoglobule-localized metallopeptidase
RT PGM48.";
RL Plant Signal. Behav. 12:e1331197-e1331197(2017).
RN [11]
RP INDUCTION BY NAC072/RD26.
RC STRAIN=cv. Columbia;
RX PubMed=29659022; DOI=10.1111/nph.15127;
RA Kamranfar I., Xue G.-P., Tohge T., Sedaghatmehr M., Fernie A.R.,
RA Balazadeh S., Mueller-Roeber B.;
RT "Transcription factor RD26 is a key regulator of metabolic reprogramming
RT during dark-induced senescence.";
RL New Phytol. 218:1543-1557(2018).
CC -!- FUNCTION: Acyltransferase involved in fatty acid phytyl ester synthesis
CC in chloroplasts, a process required for the maintenance of the
CC photosynthetic membrane integrity during abiotic stress and senescence
CC (PubMed:22623494). Exhibits phytyl ester synthesis and diacylglycerol
CC acyltransferase activities with broad substrate specificities, and can
CC employ acyl-CoAs, acyl carrier proteins, and galactolipids as acyl
CC donors (PubMed:22623494). {ECO:0000269|PubMed:22623494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + a 1,2-
CC diacylglycerol = a triacylglycerol + an acyl-3-O-(beta-D-galactosyl)-
CC sn-glycerol; Xref=Rhea:RHEA:68116, ChEBI:CHEBI:17615,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:49172, ChEBI:CHEBI:141434;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68117;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacylglycerol + a fatty acyl-CoA = a triacylglycerol +
CC CoA; Xref=Rhea:RHEA:68120, ChEBI:CHEBI:17855, ChEBI:CHEBI:49172,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77636;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68121;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacylglycerol + a fatty acyl-[ACP] = a triacylglycerol
CC + holo-[ACP]; Xref=Rhea:RHEA:68124, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:14125, ChEBI:CHEBI:17855, ChEBI:CHEBI:49172, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138651; Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68125;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + phytol = a fatty acid phytyl ester + CoA;
CC Xref=Rhea:RHEA:68128, ChEBI:CHEBI:17327, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:77636, ChEBI:CHEBI:177021;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68129;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phytol + tetradecanoyl-CoA = CoA + tetradecanoate phytyl
CC ester; Xref=Rhea:RHEA:68132, ChEBI:CHEBI:17327, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:177026;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68133;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,3-diacylglycerol + a fatty acyl-CoA = a triacylglycerol +
CC CoA; Xref=Rhea:RHEA:68152, ChEBI:CHEBI:17855, ChEBI:CHEBI:47777,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77636;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68153;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexanoylglycerol + tetradecanoyl-CoA = 1,2-dihexanoyl-3-
CC tetradecanoylglycerol + CoA; Xref=Rhea:RHEA:68196, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:177077, ChEBI:CHEBI:177078;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68197;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexanoylglycerol + hexadecanoyl-CoA = 1,2-dihexanoyl-3-
CC hexadecanoylglycerol + CoA; Xref=Rhea:RHEA:68200, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:177077, ChEBI:CHEBI:177079;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68201;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexanoylglycerol + octadecanoyl-CoA = 1,2-dihexanoyl-3-
CC octadecanoylglycerol + CoA; Xref=Rhea:RHEA:68204, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:177077, ChEBI:CHEBI:177080;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68205;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z)-hexadecatrienoyl-CoA + 1,2-dihexanoylglycerol =
CC 1,2-dihexanoyl-3-(7Z,10Z,13Z-hexadecatrienoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:68208, ChEBI:CHEBI:57287, ChEBI:CHEBI:177077,
CC ChEBI:CHEBI:177083, ChEBI:CHEBI:177091;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68209;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,2-dihexanoylglycerol = 1,2-
CC dihexanoyl-3-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:68212,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:177077,
CC ChEBI:CHEBI:177087; Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68213;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 1,2-dihexanoylglycerol =
CC 1,2-dihexanoyl-3-(9Z,12Z,15Z-octadecatrienoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:68216, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:177077, ChEBI:CHEBI:177088;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68217;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + phytol = CoA + decanoate phytyl ester;
CC Xref=Rhea:RHEA:68192, ChEBI:CHEBI:17327, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61430, ChEBI:CHEBI:177028;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68193;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z)-hexadecatrienoyl-CoA + phytol = (7Z,10Z,13Z)-
CC hexadecatrienoate phytyl ester + CoA; Xref=Rhea:RHEA:68220,
CC ChEBI:CHEBI:17327, ChEBI:CHEBI:57287, ChEBI:CHEBI:177029,
CC ChEBI:CHEBI:177091; Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68221;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + phytol = CoA + dodecanoate phytyl ester;
CC Xref=Rhea:RHEA:68188, ChEBI:CHEBI:17327, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:177027;
CC Evidence={ECO:0000269|PubMed:22623494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68189;
CC Evidence={ECO:0000269|PubMed:22623494};
CC -!- SUBUNIT: Interacts with PGM48. {ECO:0000269|PubMed:27895226}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653,
CC ECO:0000269|PubMed:22623494}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers (e.g. sepals, petals
CC and stamen). {ECO:0000269|PubMed:28534654}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during senescence.
CC {ECO:0000269|PubMed:22623494, ECO:0000269|PubMed:28534654}.
CC -!- INDUCTION: Accumulates upon nitrogen deprivation (PubMed:22623494).
CC Triggered by NAC072/RD26 during senescence (PubMed:29659022).
CC {ECO:0000269|PubMed:22623494, ECO:0000269|PubMed:29659022}.
CC -!- DISRUPTION PHENOTYPE: Plants lacking both PES1 and PES2 grow normally
CC but show reduced phytyl ester and triacylglycerol accumulation.
CC {ECO:0000269|PubMed:22623494}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005388; AAC64874.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33119.1; -; Genomic_DNA.
DR EMBL; BT005958; AAO64893.1; -; mRNA.
DR EMBL; AK118486; BAC43090.1; -; mRNA.
DR EMBL; AY086491; AAM63493.1; -; mRNA.
DR PIR; G96587; G96587.
DR RefSeq; NP_564662.1; NM_104335.5.
DR AlphaFoldDB; Q9ZVN2; -.
DR BioGRID; 27124; 3.
DR STRING; 3702.AT1G54570.1; -.
DR ESTHER; arath-Y1457; AlphaBeta_hydrolase.
DR MetOSite; Q9ZVN2; -.
DR PaxDb; Q9ZVN2; -.
DR PRIDE; Q9ZVN2; -.
DR ProteomicsDB; 242418; -.
DR EnsemblPlants; AT1G54570.1; AT1G54570.1; AT1G54570.
DR GeneID; 841899; -.
DR Gramene; AT1G54570.1; AT1G54570.1; AT1G54570.
DR KEGG; ath:AT1G54570; -.
DR Araport; AT1G54570; -.
DR TAIR; locus:2199481; AT1G54570.
DR eggNOG; ENOG502QQUD; Eukaryota.
DR HOGENOM; CLU_015395_2_1_1; -.
DR InParanoid; Q9ZVN2; -.
DR OMA; WPSKPEF; -.
DR OrthoDB; 1152269at2759; -.
DR PhylomeDB; Q9ZVN2; -.
DR PRO; PR:Q9ZVN2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVN2; baseline and differential.
DR Genevisible; Q9ZVN2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; IDA:UniProtKB.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0033306; P:phytol metabolic process; IDA:TAIR.
DR GO; GO:0090693; P:plant organ senescence; IEP:UniProtKB.
DR GO; GO:1904963; P:regulation of phytol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IGI:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR Pfam; PF03982; DAGAT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Chloroplast; Plastid; Reference proteome; Stress response;
KW Transferase; Transit peptide.
FT TRANSIT 1..27
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 28..704
FT /note="Phytyl ester synthase 1, chloroplastic"
FT /id="PRO_0000286519"
SQ SEQUENCE 704 AA; 78204 MW; CE62CCEEC3698AD9 CRC64;
MATCSSSLLV LPNLRLSSNQ RRNFKVRAQI SGENKKATSL EPVNNNGSVS LSTTVQNQKG
ANEVNGKGKS KRKIVSDEIE LLWDDGYGSK SVKDYFAAAK EILKADGGPP RWFSPVDCGR
PVEDAPTLLF LPGMDGTGMG LVPHHKALGK AFHVSCLHIP VLDRTPFEGL LKVVEDVLRQ
EQATRPNKPI YLVGDSFGGC LALAVAARNR SLDLVLILVN PATSFDRSPL QPLLPILEMV
PEELHFTVPY ALSFIMGDPI KMATLGIDNQ LPTGVKIEKL RQRLTKTMLP LLSELGGIIP
RETLLWKLKL LRSGCAYANS RIHAVQAEVL VLASGKDMML PSQEEAKRLH GLLKNCSVRC
FKDNGHTLLL EDSISLLTVI KGTGKYRRSW RYDLVSDFLP PSKGELAYAL DEVLGFLRNA
VGSVFFSTME DGKIVKGLAG VPDKGPVLLV GYHMLMGLEL GPMSEAFIKE KNILFRGMAH
PVLYSDNDPA KAFDYGDWIK VFGAYPVTAT NLFKLLDSKS HVLLFPGGAR EALHNRGEQY
KLIWPEQQEF VRMAARFGAT IVPFGTVGED DIAELVLDYN DLMKIPILND YITEVTRDTK
QFKLREESEG EVANQPLYLP GLIPKVPGRF YYLFGKPIET KGRPELVKDK EEANQVYLEV
KAEVENSIAY LLKKREEDPY RSVLDRLNYS LTHTTATHVP SFEP
