ID   ELP3_ARATH              Reviewed;         565 AA.
AC   Q93ZR1; Q9FK40;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Elongator complex protein 3 {ECO:0000303|PubMed:20398216};
DE            Short=AtELP3 {ECO:0000303|PubMed:20398216};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9};
DE   AltName: Full=Elongator component 3 {ECO:0000303|PubMed:20398216};
DE   AltName: Full=Protein ELONGATA 3 {ECO:0000303|PubMed:15894610};
DE   AltName: Full=Protein ENHANCER-OF-ASYMMETRIC-LEAVES-TWO1 {ECO:0000303|PubMed:21700721};
DE   AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305};
GN   Name=HAG3 {ECO:0000303|PubMed:12466527};
GN   Synonyms=EAST1 {ECO:0000303|PubMed:21700721}, ELO3
GN   {ECO:0000303|PubMed:15894610}, ELP3 {ECO:0000303|PubMed:20398216};
GN   OrderedLocusNames=At5g50320 {ECO:0000312|Araport:AT5G50320};
GN   ORFNames=MXI22.3 {ECO:0000312|EMBL:BAB09451.1};
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], MUTAGENESIS OF ASP-331, DISRUPTION PHENOTYPE,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX   PubMed=15894610; DOI=10.1073/pnas.0502600102;
RA   Nelissen H., Fleury D., Bruno L., Robles P., de Veylder L., Traas J.,
RA   Micol J., Van Montagu M., Inze D., Van Lijsebettens M.;
RT   "The elongata mutants identify a functional Elongator complex in plants
RT   with a role in cell proliferation during organ growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:7754-7759(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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   NOMENCLATURE.
RX   PubMed=12466527; DOI=10.1093/nar/gkf660;
RA   Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA   Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT   "Analysis of histone acetyltransferase and histone deacetylase families of
RT   Arabidopsis thaliana suggests functional diversification of chromatin
RT   modification among multicellular eukaryotes.";
RL   Nucleic Acids Res. 30:5036-5055(2002).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20398216; DOI=10.1111/j.1365-2958.2010.07163.x;
RA   Mehlgarten C., Jablonowski D., Wrackmeyer U., Tschitschmann S.,
RA   Sondermann D., Jaeger G., Gong Z., Bystroem A.S., Schaffrath R.,
RA   Breunig K.D.;
RT   "Elongator function in tRNA wobble uridine modification is conserved
RT   between yeast and plants.";
RL   Mol. Microbiol. 76:1082-1094(2010).
RN   [7]
RP   FUNCTION, IDENTIFICATION IN THE ELONGATOR COMPLEX, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20080602; DOI=10.1073/pnas.0913559107;
RA   Nelissen H., De Groeve S., Fleury D., Neyt P., Bruno L., Bitonti M.B.,
RA   Vandenbussche F., Van der Straeten D., Yamaguchi T., Tsukaya H.,
RA   Witters E., De Jaeger G., Houben A., Van Lijsebettens M.;
RT   "Plant Elongator regulates auxin-related genes during RNA polymerase II
RT   transcription elongation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:1678-1683(2010).
RN   [8]
RP   INTERACTION WITH IYO.
RX   PubMed=21620701; DOI=10.1016/j.cub.2011.04.041;
RA   Sanmartin M., Sauer M., Munoz A., Zouhar J., Ordonez A., van de Ven W.T.,
RA   Caro E., de la Paz Sanchez M., Raikhel N.V., Gutierrez C.,
RA   Sanchez-Serrano J.J., Rojo E.;
RT   "A molecular switch for initiating cell differentiation in Arabidopsis.";
RL   Curr. Biol. 21:999-1008(2011).
RN   [9]
RP   FUNCTION, MUTAGENESIS OF ARG-200, AND DISRUPTION PHENOTYPE.
RX   PubMed=21700721; DOI=10.1093/pcp/pcr083;
RA   Kojima S., Iwasaki M., Takahashi H., Imai T., Matsumura Y., Fleury D.,
RA   Van Lijsebettens M., Machida Y., Machida C.;
RT   "Asymmetric leaves2 and Elongator, a histone acetyltransferase complex,
RT   mediate the establishment of polarity in leaves of Arabidopsis thaliana.";
RL   Plant Cell Physiol. 52:1259-1273(2011).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22404109; DOI=10.1111/j.1365-313x.2012.04984.x;
RA   Tran H.T., Nimick M., Uhrig R.G., Templeton G., Morrice N., Gourlay R.,
RA   DeLong A., Moorhead G.B.;
RT   "Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin
RT   deacetylase that associates with PP2A and enriches in the microtubule
RT   fraction with the putative histone acetyltransferase ELP3.";
RL   Plant J. 71:263-272(2012).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22026817; DOI=10.1111/j.1365-313x.2011.04831.x;
RA   Xu D., Huang W., Li Y., Wang H., Huang H., Cui X.;
RT   "Elongator complex is critical for cell cycle progression and leaf
RT   patterning in Arabidopsis.";
RL   Plant J. 69:792-808(2012).
RN   [12]
RP   FUNCTION, MUTAGENESIS OF GLU-423, AND TISSUE SPECIFICITY.
RX   PubMed=23969312; DOI=10.1016/j.ydbio.2013.08.008;
RA   Skylar A., Matsuwaka S., Wu X.;
RT   "ELONGATA3 is required for shoot meristem cell cycle progression in
RT   Arabidopsis thaliana seedlings.";
RL   Dev. Biol. 382:436-445(2013).
RN   [13]
RP   FUNCTION.
RX   PubMed=25907565; DOI=10.1093/pcp/pcv054;
RA   Fina J.P., Casati P.;
RT   "HAG3, a histone acetyltransferase, affects UV-B responses by negatively
RT   regulating the expression of DNA repair enzymes and sunscreen content in
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 56:1388-1400(2015).
CC   -!- FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator
CC       complex which is required for multiple tRNA modifications, including
CC       mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-
CC       methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl
CC       uridine) (PubMed:20398216). In the elongator complex, acts as a tRNA
CC       uridine(34) acetyltransferase by mediating formation of
CC       carboxymethyluridine in the wobble base at position 34 in tRNAs (By
CC       similarity). Promotes organ development by modulating cell division
CC       rate (PubMed:20080602). Required for auxin distribution or signaling
CC       (PubMed:20080602). Required for meristem cell cycle activation at the
CC       time of germination (PubMed:23969312). Mediates the establishment of
CC       leaf polarity independently of AS2 and the ta-siRNA-related pathway
CC       (PubMed:21700721). Indirectly involved in negatively regulating the
CC       expression of genes that participate in UV-B responses, such as DNA
CC       repair enzymes and enzymes that participate in sunscreen pigment
CC       biosynthesis (PubMed:25907565). {ECO:0000250|UniProtKB:D5VRB9,
CC       ECO:0000269|PubMed:20080602, ECO:0000269|PubMed:20398216,
CC       ECO:0000269|PubMed:21700721, ECO:0000269|PubMed:23969312,
CC       ECO:0000269|PubMed:25907565}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in
CC         tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA
CC         + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407,
CC         Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315,
CC         ChEBI:CHEBI:74882; Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021;
CC         Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q02908};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000250|UniProtKB:Q02908};
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000250|UniProtKB:Q9H9T3}.
CC   -!- SUBUNIT: Component of the elongator complex which consists of
CC       ELP1/ELO2, ELP2, ELP3/ELO3, ELP4/ELO1, ELP5, and ELP6
CC       (PubMed:20080602). Interacts with IYO (PubMed:21620701).
CC       {ECO:0000269|PubMed:20080602, ECO:0000269|PubMed:21620701}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20080602,
CC       ECO:0000269|PubMed:22026817, ECO:0000269|PubMed:22404109}. Cytoplasm
CC       {ECO:0000269|PubMed:22404109}. Note=Localized in euchromatin during
CC       interphase. {ECO:0000269|PubMed:20080602}.
CC   -!- TISSUE SPECIFICITY: Expressed in meristematic tissues of in roots,
CC       leaves, seedlings, cotyledons, floral buds and shoot apices
CC       (PubMed:15894610, PubMed:20080602, PubMed:23969312). Expressed in the
CC       shoot meristem and the emerging leaves immediately after germination
CC       (PubMed:23969312). In the root, expressed in the transition zone and
CC       the upper meristematic zone (PubMed:23969312).
CC       {ECO:0000269|PubMed:15894610, ECO:0000269|PubMed:20080602,
CC       ECO:0000269|PubMed:23969312}.
CC   -!- DISRUPTION PHENOTYPE: Slow growing rate associated with pale-green and
CC       downwardly curled narrow leaves and reduced root growth that results
CC       from a decreased cell division rate and a reduced apical dominance.
CC       Defect in tRNA wobble uridine modification. Filamentous leaves with
CC       abaxialized epidermis in AS2 defective plants.
CC       {ECO:0000269|PubMed:15894610, ECO:0000269|PubMed:20080602,
CC       ECO:0000269|PubMed:20398216, ECO:0000269|PubMed:21700721}.
CC   -!- SIMILARITY: Belongs to the ELP3 family. {ECO:0000305}.
CC   -!- CAUTION: The elongator complex was originally thought to play a role in
CC       transcription elongation. However, it is no longer thought to play a
CC       direct role in this process and its primary function is thought to be
CC       in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL06951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ964958; CAI79647.1; -; mRNA.
DR   EMBL; AB012248; BAB09451.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95925.1; -; Genomic_DNA.
DR   EMBL; AY054293; AAL06951.1; ALT_INIT; mRNA.
DR   EMBL; AY056323; AAL07172.1; -; mRNA.
DR   EMBL; AY133528; AAM91358.1; -; mRNA.
DR   RefSeq; NP_568725.1; NM_124412.3.
DR   AlphaFoldDB; Q93ZR1; -.
DR   SMR; Q93ZR1; -.
DR   BioGRID; 20344; 3.
DR   IntAct; Q93ZR1; 3.
DR   STRING; 3702.Q93ZR1; -.
DR   iPTMnet; Q93ZR1; -.
DR   PaxDb; 3702-AT5G50320-1; -.
DR   ProteomicsDB; 221890; -.
DR   EnsemblPlants; AT5G50320.1; AT5G50320.1; AT5G50320.
DR   GeneID; 835098; -.
DR   Gramene; AT5G50320.1; AT5G50320.1; AT5G50320.
DR   KEGG; ath:AT5G50320; -.
DR   Araport; AT5G50320; -.
DR   TAIR; AT5G50320; ELO3.
DR   eggNOG; KOG2535; Eukaryota.
DR   HOGENOM; CLU_025983_2_1_1; -.
DR   InParanoid; Q93ZR1; -.
DR   OMA; TFETRPD; -.
DR   OrthoDB; 46095at2759; -.
DR   PhylomeDB; Q93ZR1; -.
DR   BRENDA; 2.3.1.48; 399.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q93ZR1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q93ZR1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR   GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; IEA:RHEA.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IMP:TAIR.
DR   GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR   GO; GO:0035265; P:organ growth; IMP:TAIR.
DR   GO; GO:0010928; P:regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:2000025; P:regulation of leaf formation; IMP:UniProtKB.
DR   GO; GO:0090708; P:specification of plant organ axis polarity; IMP:UniProtKB.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IMP:UniProtKB.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR039661; ELP3.
DR   InterPro; IPR034687; ELP3-like.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR032432; Radical_SAM_C.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR01211; ELP3; 1.
DR   PANTHER; PTHR11135:SF0; ELONGATOR COMPLEX PROTEIN 3; 1.
DR   PANTHER; PTHR11135; HISTONE ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF16199; Radical_SAM_C; 1.
DR   PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1.
DR   SFLD; SFLDF00344; ELP3-like; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
DR   Genevisible; Q93ZR1; AT.
PE   1: Evidence at protein level;
KW   4Fe-4S; Acyltransferase; Auxin signaling pathway; Cytoplasm; Iron;
KW   Iron-sulfur; Metal-binding; Nucleus; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..565
FT                   /note="Elongator complex protein 3"
FT                   /id="PRO_0000232128"
FT   DOMAIN          100..390
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   DOMAIN          414..565
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         117
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q02908"
FT   BINDING         127
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q02908"
FT   BINDING         130
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q02908"
FT   BINDING         182
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         492..495
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         515..517
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         548
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   MUTAGEN         200
FT                   /note="R->W: In east1-1; slow growth associated with
FT                   pale-green and downwardly curled leaves."
FT                   /evidence="ECO:0000269|PubMed:21700721"
FT   MUTAGEN         331
FT                   /note="D->N: In elo3-1; reduced cell proliferation."
FT                   /evidence="ECO:0000269|PubMed:15894610"
FT   MUTAGEN         423
FT                   /note="E->K: In elo3-14; reduced tissue proliferation in
FT                   the meristem."
FT                   /evidence="ECO:0000269|PubMed:23969312"
SQ   SEQUENCE   565 AA;  63694 MW;  8F993E4D41CF4B05 CRC64;
     MATAVVMNGE LKKQPRPGKG GYQGRGLTEE EARVRAISEI VSTMIERSHR NENVDLNAIK
     TAACRKYGLA RAPKLVEMIA ALPDSERETL LPKLRAKPVR TASGIAVVAV MSKPHRCPHI
     ATTGNICVYC PGGPDSDFEY STQSYTGYEP TSMRAIRARY NPYVQARSRI DQLKRLGHSV
     DKVEFILMGG TFMSLPAEYR DFFIRNLHDA LSGHTSANVE EAVAYSEHSA TKCIGMTIET
     RPDYCLGPHL RQMLIYGCTR LEIGVQSTYE DVARDTNRGH TVAAVADCFC LAKDAGFKVV
     AHMMPDLPNV GVERDMESFK EFFESPSFRA DGLKIYPTLV IRGTGLYELW KTGRYRNYPP
     EQLVDIVARI LSMVPPWTRV YRVQRDIPMP LVTSGVEKGN LRELALARMD DLGLKCRDVR
     TREAGIQDIH HKIKPEQVEL VRRDYTANEG WETFLSYEDT RQDILVGLLR LRKCGKNVTC
     PELMGKCSVV RELHVYGTAV PVHGRDADKL QHQGYGTLLM EEAERIARRE HRSNKIGVIS
     GVGTRHYYRK LGYELEGPYM VKHLL
//