BTS_ARATH
ID BTS_ARATH Reviewed; 1254 AA.
AC Q8LPQ5; Q0WL18; Q9LJQ1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Zinc finger protein BRUTUS {ECO:0000303|PubMed:20675571};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2454 {ECO:0000303|PubMed:20675571};
GN Name=BTS {ECO:0000303|PubMed:20675571};
GN Synonyms=EMB2454 {ECO:0000303|PubMed:20675571};
GN OrderedLocusNames=At3g18290 {ECO:0000312|Araport:AT3G18290};
GN ORFNames=MIE15.8 {ECO:0000312|EMBL:BAB01179.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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] OF 768-1254.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BHLH115; BHLH104 AND ILR3,
RP AND INDUCTION BY IRON DEFICIENCY.
RC STRAIN=cv. Columbia;
RX PubMed=20675571; DOI=10.1105/tpc.110.074096;
RA Long T.A., Tsukagoshi H., Busch W., Lahner B., Salt D.E., Benfey P.N.;
RT "The bHLH transcription factor POPEYE regulates response to iron deficiency
RT in Arabidopsis roots.";
RL Plant Cell 22:2219-2236(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZINC AND IRON IONS.
RX PubMed=24253678; DOI=10.1038/ncomms3792;
RA Kobayashi T., Nagasaka S., Senoura T., Itai R.N., Nakanishi H.,
RA Nishizawa N.K.;
RT "Iron-binding haemerythrin RING ubiquitin ligases regulate plant iron
RT responses and accumulation.";
RL Nat. Commun. 4:2792-2792(2013).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25794933; DOI=10.1105/tpc.114.132704;
RA Zhang J., Liu B., Li M., Feng D., Jin H., Wang P., Liu J., Xiong F.,
RA Wang J., Wang H.-B.;
RT "The bHLH transcription factor bHLH104 interacts with IAA-LEUCINE
RT RESISTANT3 and modulates iron homeostasis in Arabidopsis.";
RL Plant Cell 27:787-805(2015).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-108; GLU-369 AND
RP GLU-716, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP BHLH115; BHLH104 AND ILR3, INDUCTION BY IRON DEFICIENCY, AND INTERACTION
RP WITH ZINC AND IRON IONS.
RC STRAIN=cv. Columbia;
RX PubMed=25452667; DOI=10.1104/pp.114.250837;
RA Selote D., Samira R., Matthiadis A., Gillikin J.W., Long T.A.;
RT "Iron-binding E3 ligase mediates iron response in plants by targeting basic
RT helix-loop-helix transcription factors.";
RL Plant Physiol. 167:273-286(2015).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27359166; DOI=10.1080/15592324.2016.1204508;
RA Matthiadis A., Long T.A.;
RT "Further insight into BRUTUS domain composition and functionality.";
RL Plant Signal. Behav. 0:0-0(2016).
CC -!- FUNCTION: Essential protein (PubMed:20675571, PubMed:25452667).
CC Negatively regulates the response to iron deficiency and thus
CC contributes to iron homeostasis (PubMed:20675571, PubMed:25794933).
CC Exhibits E3 ubiquitin-protein ligase activity in vitro
CC (PubMed:24253678, PubMed:25452667). Plays a role in root growth,
CC rhizosphere acidification, and iron reductase activity in response to
CC iron deprivation (PubMed:25452667, PubMed:27359166). Facilitates 26S
CC proteasome-mediated degradation of PYEL proteins in the absence of iron
CC (PubMed:25452667). {ECO:0000269|PubMed:20675571,
CC ECO:0000269|PubMed:24253678, ECO:0000269|PubMed:25452667,
CC ECO:0000269|PubMed:25794933, ECO:0000269|PubMed:27359166,
CC ECO:0000303|PubMed:20675571}.
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with the PYEL proteins bHLH115, bHLH104 and ILR3 in
CC the nucleus (PubMed:20675571, PubMed:25452667). Binds zinc and iron
CC ions (PubMed:24253678, PubMed:25452667). {ECO:0000269|PubMed:20675571,
CC ECO:0000269|PubMed:24253678, ECO:0000269|PubMed:25452667}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:24253678,
CC ECO:0000269|PubMed:25452667}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons of seedlings, young leaves,
CC developing and mature embryos, and other reproductive tissues including
CC floral vasculature, funiculus, septum, and gynoecium valves.
CC {ECO:0000269|PubMed:25452667}.
CC -!- INDUCTION: By iron deficiency, specifically in the root vasculature
CC (e.g. pericycle) (PubMed:20675571, PubMed:25452667). Destabilized upon
CC iron-binding (PubMed:25452667). {ECO:0000269|PubMed:20675571,
CC ECO:0000269|PubMed:25452667}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:20675571,
CC PubMed:25452667). Increased tolerance to iron deprivation
CC (PubMed:20675571, PubMed:25794933, PubMed:27359166). Over-accumulation
CC of iron ions in phloems, rosette leaves, flowers and seeds. In normal
CC conditions, at the late reproductive stage, aborted siliques and
CC abnormal necrotic lesions in cauline leaves (PubMed:25794933).
CC Increased root elongation, rhizosphere acidification, and iron
CC reductase activity under iron deficiency (PubMed:25452667,
CC PubMed:27359166). {ECO:0000269|PubMed:20675571,
CC ECO:0000269|PubMed:25452667, ECO:0000269|PubMed:25794933,
CC ECO:0000269|PubMed:27359166, ECO:0000303|PubMed:20675571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01179.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000414; BAB01179.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76077.1; -; Genomic_DNA.
DR EMBL; AY094471; AAM19839.1; -; mRNA.
DR EMBL; BT005819; AAO64754.1; -; mRNA.
DR EMBL; AK230391; BAF02189.1; -; mRNA.
DR RefSeq; NP_188457.1; NM_112713.4.
DR AlphaFoldDB; Q8LPQ5; -.
DR SMR; Q8LPQ5; -.
DR STRING; 3702.AT3G18290.1; -.
DR PaxDb; Q8LPQ5; -.
DR PRIDE; Q8LPQ5; -.
DR ProteomicsDB; 240292; -.
DR EnsemblPlants; AT3G18290.1; AT3G18290.1; AT3G18290.
DR GeneID; 821357; -.
DR Gramene; AT3G18290.1; AT3G18290.1; AT3G18290.
DR KEGG; ath:AT3G18290; -.
DR Araport; AT3G18290; -.
DR TAIR; locus:2089678; AT3G18290.
DR eggNOG; KOG1940; Eukaryota.
DR HOGENOM; CLU_003967_0_0_1; -.
DR InParanoid; Q8LPQ5; -.
DR OMA; LIDCNET; -.
DR OrthoDB; 571648at2759; -.
DR PhylomeDB; Q8LPQ5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LPQ5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LPQ5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:UniProtKB.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR039512; RCHY1_zinc-ribbon.
DR InterPro; IPR008913; Znf_CHY.
DR InterPro; IPR037274; Znf_CHY_sf.
DR InterPro; IPR017921; Znf_CTCHY.
DR InterPro; IPR037275; Znf_CTCHY_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01814; Hemerythrin; 3.
DR Pfam; PF05495; zf-CHY; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14599; zinc_ribbon_6; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF161219; SSF161219; 1.
DR SUPFAM; SSF161245; SSF161245; 1.
DR PROSITE; PS51266; ZF_CHY; 1.
DR PROSITE; PS51270; ZF_CTCHY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Iron; Ligase; Membrane; Metal-binding; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1254
FT /note="Zinc finger protein BRUTUS"
FT /id="PRO_0000437680"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 999..1068
FT /note="CHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT ZN_FING 1071..1134
FT /note="CTCHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT ZN_FING 1135..1176
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1006
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1008
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1019
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1020
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1026
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1029
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1030
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1036
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1048
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1051
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1061
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1066
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1076
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1079
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1090
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1091
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1094
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1097
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT SITE 108
FT /note="Required for iron-dependent instability"
FT /evidence="ECO:0000269|PubMed:25452667"
FT SITE 369
FT /note="Required for iron-dependent instability"
FT /evidence="ECO:0000269|PubMed:25452667"
FT MUTAGEN 108
FT /note="E->A: Loss of sensitivity to iron."
FT /evidence="ECO:0000269|PubMed:25452667"
FT MUTAGEN 369
FT /note="E->A: Loss of sensitivity to iron."
FT /evidence="ECO:0000269|PubMed:25452667"
FT MUTAGEN 716
FT /note="E->A: Normal sensitivity to iron."
FT /evidence="ECO:0000269|PubMed:25452667"
SQ SEQUENCE 1254 AA; 141467 MW; BF7877F23948382C CRC64;
MATPLPDFET ARGGGAVASS STTVLPSSVS SSSSSSRPLP VANSFSDDAE EISPILIFLF
FHKAVCSELE ALHRLALEFA TGHHVDLRLL RERYRFLRSI YKHHCNAEDE VIFSALDIRV
KNVAQTYSLE HKGESNLFDH LFELLNSATE TDESYRRELA RSTGALQTSV SQHLAKEQKQ
VFPLLIEKFK YEEQAYIVWR FLCSIPVNML AVFLPWISSS ISVDESKEMQ TCLKKIVPGE
KLLQQVIFTW LGGKSNTVAS CRIEDSMFQC CLDSSSSMLP CKASREQCAC EGSKIGKRKY
PELTNFGSSD TLHPVDEIKL WHKSINKEMK EIADEARKIQ LSGDFSDLSA FDERLQYIAE
VCIFHSLAED KIIFPAVDGE FSFSEEHDEE ENQFNEFRCL IENIKSAGAS STSAAEFYTK
LCSHADQIME TIQRHFHNEE IQVLPLARKN FSFKRQQELL YQSLCIMPLR LIERVLPWLT
ASLTEDEAKN FLKNLQAGAP KSDVALVTLF SGWACKGRKA GECLSPNGNG LCPVKTLSNI
KEVNLQSCNA CASVPCTSRS TKSCCQHQDK RPAKRTAVLS CEKKTTPHST EVANGCKPSG
NGRSCCVPDL GVNNNCLELG SLPAAKAMRS SSLNSAAPAL NSSLFIWEMD SNSFGTGHAE
RPVATIFKFH KAISKDLEFL DVESGKLIDC DGTFIRQFIG RFHLLWGFYK AHSNAEDDIL
FPALESKETL HNVSHSYTLD HKQEEKLFGD IYSVLTELSI LHEKLQSDSM MEDIAQTDTV
RTDIDNGDCN KKYNELATKL QGMCKSIKIT LDQHIFLEEL ELWPLFDKHF SIQEQDKIVG
RIIGTTGAEV LQSMLPWVTS ALSEDEQNRM MDTWKQATKN TMFDEWLNEC WKGSPDSSST
ETSKPSPQKD NDHQEILDQS GELFKPGWKD IFRMNQNELE AEIRKVYQDS TLDPRRKDYL
VQNWRTSRWI AAQQKLPKEA ETAVNGDVEL GCSPSFRDPE KQIYGCEHYK RNCKLRAACC
DQLFTCRFCH DKVSDHSMDR KLVTEMLCMR CLKVQPVGPI CTTPSCDGFP MAKHYCSICK
LFDDERAVYH CPFCNLCRVG EGLGIDFFHC MTCNCCLGMK LVNHKCLEKS LETNCPICCE
FLFTSSEAVR ALPCGHYMHS ACFQAYTCSH YTCPICGKSL GDMAVYFGML DALLAAEELP
EEYKNRCQDI LCNDCERKGT TRFHWLYHKC GSCGSYNTRV IKSETIPPDC STSS
