GES_ARATH
ID GES_ARATH Reviewed; 877 AA.
AC Q93YV0; O22733; Q84UU3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=(E,E)-geranyllinalool synthase {ECO:0000303|PubMed:12572612, ECO:0000303|PubMed:18398052};
DE Short=AtGES {ECO:0000303|PubMed:21334702};
DE EC=4.2.3.144 {ECO:0000269|PubMed:18398052, ECO:0000269|PubMed:18842097};
DE AltName: Full=Terpenoid synthase 4 {ECO:0000303|PubMed:12207221, ECO:0000303|PubMed:18400103, ECO:0000303|PubMed:18842097};
DE Short=AtTPS04 {ECO:0000303|PubMed:12207221, ECO:0000303|PubMed:18400103};
GN Name=GES {ECO:0000303|PubMed:18398052};
GN Synonyms=LIS {ECO:0000303|PubMed:12572612},
GN TPS04 {ECO:0000303|PubMed:12207221, ECO:0000303|PubMed:18400103},
GN TPS4 {ECO:0000303|PubMed:18842097};
GN OrderedLocusNames=At1g61120 {ECO:0000312|Araport:AT1G61120};
GN ORFNames=F11P17.15 {ECO:0000312|EMBL:AAB71482.1};
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12566586; DOI=10.1105/tpc.007989;
RA Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E., Gershenzon J.;
RT "Biosynthesis and emission of terpenoid volatiles from Arabidopsis
RT flowers.";
RL Plant Cell 15:481-494(2003).
RN [2]
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION.
RX PubMed=12572612; DOI=10.1093/oxfordjournals.molbev.a025876;
RA Cseke L., Dudareva N., Pichersky E.;
RT "Structure and evolution of linalool synthase.";
RL Mol. Biol. Evol. 15:1491-1498(1998).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
RA Aubourg S., Lecharny A., Bohlmann J.;
RT "Genomic analysis of the terpenoid synthase (AtTPS) gene family of
RT Arabidopsis thaliana.";
RL Mol. Genet. Genomics 267:730-745(2002).
RN [7]
RP GENE FAMILY.
RX PubMed=12777052; DOI=10.1023/a:1023005504702;
RA Lange B.M., Ghassemian M.;
RT "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT in isoprenoid and chlorophyll metabolism.";
RL Plant Mol. Biol. 51:925-948(2003).
RN [8]
RP INDUCTION BY METHYL JASMONATE.
RX PubMed=16021335; DOI=10.1007/s11103-005-7306-5;
RA Devoto A., Ellis C., Magusin A., Chang H.-S., Chilcott C., Zhu T.,
RA Turner J.G.;
RT "Expression profiling reveals COI1 to be a key regulator of genes involved
RT in wound- and methyl jasmonate-induced secondary metabolism, defence, and
RT hormone interactions.";
RL Plant Mol. Biol. 58:497-513(2005).
RN [9]
RP INDUCTION BY HERBIVORY.
RX PubMed=18400103; DOI=10.1186/1471-2164-9-154;
RA Ehlting J., Chowrira S.G., Mattheus N., Aeschliman D.S., Arimura G.,
RA Bohlmann J.;
RT "Comparative transcriptome analysis of Arabidopsis thaliana infested by
RT diamond back moth (Plutella xylostella) larvae reveals signatures of stress
RT response, secondary metabolism, and signalling.";
RL BMC Genomics 9:154-154(2008).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX PubMed=18842097; DOI=10.1094/mpmi-21-11-1482;
RA Attaran E., Rostas M., Zeier J.;
RT "Pseudomonas syringae elicits emission of the terpenoid (E,E)-4,8,12-
RT trimethyl-1,3,7,11-tridecatetraene in Arabidopsis leaves via jasmonate
RT signaling and expression of the terpene synthase TPS4.";
RL Mol. Plant Microbe Interact. 21:1482-1497(2008).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND PATHWAY.
RX PubMed=18398052; DOI=10.1105/tpc.106.049478;
RA Herde M., Gaertner K., Koellner T.G., Fode B., Boland W., Gershenzon J.,
RA Gatz C., Tholl D.;
RT "Identification and regulation of TPS04/GES, an Arabidopsis geranyllinalool
RT synthase catalyzing the first step in the formation of the insect-induced
RT volatile C16-homoterpene TMTT.";
RL Plant Cell 20:1152-1168(2008).
RN [12]
RP INDUCTION BY ALAMETHICIN.
RX PubMed=21088219; DOI=10.1073/pnas.1009975107;
RA Lee S., Badieyan S., Bevan D.R., Herde M., Gatz C., Tholl D.;
RT "Herbivore-induced and floral homoterpene volatiles are biosynthesized by a
RT single P450 enzyme (CYP82G1) in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21205-21210(2010).
RN [13]
RP REVIEW.
RX PubMed=21334702; DOI=10.1016/j.phytochem.2011.01.019;
RA Tholl D., Sohrabi R., Huh J.-H., Lee S.;
RT "The biochemistry of homoterpenes--common constituents of floral and
RT herbivore-induced plant volatile bouquets.";
RL Phytochemistry 72:1635-1646(2011).
CC -!- FUNCTION: Involved in the biosynthesis of homoterpenes, attractants of
CC herbivores parasitoids and predators (e.g. predatory mites and
CC parasitoid wasps) (PubMed:21334702). Involved in diterpene (C20)
CC biosynthesis (PubMed:18398052, PubMed:18842097). Catalyzes the
CC conversion of geranylgeranyl diphosphate to (E,E)-geranyllinalool, the
CC precursor of the insect-induced volatile C16-homoterpene TMTT
CC (PubMed:18398052, PubMed:18842097). {ECO:0000269|PubMed:18398052,
CC ECO:0000269|PubMed:18842097, ECO:0000303|PubMed:21334702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (6E,10E)-
CC geranyllinalool + diphosphate; Xref=Rhea:RHEA:38155,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:74299; EC=4.2.3.144;
CC Evidence={ECO:0000269|PubMed:18398052, ECO:0000269|PubMed:18842097};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:18398052, ECO:0000269|PubMed:18842097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18398052}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC {ECO:0000269|PubMed:12566586, ECO:0000269|PubMed:18398052}.
CC -!- INDUCTION: By methyl jasmonate, coronalon, alamethicin and in response
CC to the caterpillar P.xylostella feeding. Induced by infection of
CC avirulent and virulent bacterial pathogen P.syringae.
CC {ECO:0000269|PubMed:16021335, ECO:0000269|PubMed:18398052,
CC ECO:0000269|PubMed:18400103, ECO:0000269|PubMed:18842097,
CC ECO:0000269|PubMed:21088219}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No formation of (E,E)-geranyllinalool and TMMTT
CC detected. {ECO:0000269|PubMed:18398052, ECO:0000269|PubMed:18842097}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsf subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF497492; AAO85540.1; -; mRNA.
DR EMBL; AC002294; AAB71482.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33784.1; -; Genomic_DNA.
DR EMBL; AY059757; AAL24105.1; -; mRNA.
DR EMBL; BT001960; AAN71959.1; -; mRNA.
DR PIR; A96637; A96637.
DR RefSeq; NP_564772.1; NM_104793.3.
DR AlphaFoldDB; Q93YV0; -.
DR SMR; Q93YV0; -.
DR STRING; 3702.AT1G61120.1; -.
DR PaxDb; Q93YV0; -.
DR PRIDE; Q93YV0; -.
DR ProteomicsDB; 220733; -.
DR EnsemblPlants; AT1G61120.1; AT1G61120.1; AT1G61120.
DR GeneID; 842405; -.
DR Gramene; AT1G61120.1; AT1G61120.1; AT1G61120.
DR KEGG; ath:AT1G61120; -.
DR Araport; AT1G61120; -.
DR TAIR; locus:2008485; AT1G61120.
DR eggNOG; ENOG502REU3; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; Q93YV0; -.
DR OMA; MRAIYIP; -.
DR OrthoDB; 160028at2759; -.
DR PhylomeDB; Q93YV0; -.
DR BioCyc; ARA:AT1G61120-MON; -.
DR BioCyc; MetaCyc:AT1G61120-MON; -.
DR BRENDA; 4.2.3.144; 399.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q93YV0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93YV0; baseline and differential.
DR Genevisible; Q93YV0; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0080013; F:(E,E)-geranyllinalool synthase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0010333; F:terpene synthase activity; IBA:GO_Central.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IDA:TAIR.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IGI:TAIR.
DR GO; GO:0000304; P:response to singlet oxygen; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..877
FT /note="(E,E)-geranyllinalool synthase"
FT /id="PRO_0000403700"
FT MOTIF 540..544
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 544
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 544
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 544
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 677
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 680
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 680
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 688
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 14
FT /note="A -> T (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="G -> R (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="E -> Q (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Y -> YT (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="R -> G (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..107
FT /note="KDMCILT -> EDMYILI (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="I -> A (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> V (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="Q -> E (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="H -> D (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> I (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="D -> N (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="F -> L (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="S -> R (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="E -> K (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="S -> C (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="L -> P (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..401
FT /note="QEARE -> EEARK (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="K -> N (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="M -> I (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="T -> C (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="G -> A (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="N -> K (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="M -> I (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="M -> T (in Ref. 1; AAO85540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 877 AA; 101895 MW; E48C8C4F20FEC610 CRC64;
MKSSYGSSSN DLHAFVNEIK GEIQLSNINL DPYSFVSPSA YDTAWLSMIE EDINVDDNEL
KPMFQGCLDW IMCNQNAREG FWMNSTSYTT VADGRDEDGE KDMCILTSTL ACVVALQKWN
IGCFHLHKGT RYIERNTEMI IGKYINEEGS YPRWFAIKFT GILELAQKLG LHFVFSSRCI
EMIKGMFYQR QEIIQREKLV HDCNYKPLLA YLEVLPSKLY VTNQEDIIVK SLDSMDGSLF
QSPSATASAF MLTRNTKCLA YLQNLVQKCP NGVPQKYPLN EDLIKLSMVN LIESTGLGEF
FGIEIEHVLE QVYSRYEEKD FERMPMSYLA DQLHKDSLAF RMLRMHGRDV SPRSFCWFLN
DQETRNHLER NIDSFLLVIL SVYRATDLMF PGEHDLQEAR EYTRNLLEKR RSIKEKMIMH
ELSTPWIARL KHLDHRMWIE DKNSNVLSME KASFLRLHSS YSDKLTHLAA RNFEFQQAKY
CRELEELTMW VKKWGLSDIG FGREKTTYCY FATVTSLPYE YAIKFGKLAA KTAILITIAD
DFFDEKGSFN DLEGLTKAVL RWEGEELKSY GNIIFRALDD IVRETANTCR THHKTDIIVH
LRNIWGETFE SWLREAEWSK KGHTSSMDEY IRNGMISIAA HTIALSISCL MEPCFPHNKL
KPGNYDSITT LLMIIPRLLN DLQSYQKEQE QGKMNSVLLH MKNHPGLEIE DSIAHIEKII
DSKRKEFLEH VLVDGLSDLP KPCKEIHMSC CKVFEMFFNK KNRYDSNTEM LHDIKKALYD
PINVYELSEM EPMPLMAHGD EYMILPLLLN SLPNILEFKR KDGYGAMKTS MCFGRSYRVN
KRVMASQLDD QHKPLKIVAS QRKPVPMMQS IFAPCFY
