WRK52_ARATH
ID WRK52_ARATH Reviewed; 1288 AA.
AC P0DKH5; Q0WWA0; Q689Y9; Q8GZ83; Q9FH83; Q9FH84;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Disease resistance protein RRS1 {ECO:0000303|PubMed:11842188};
DE AltName: Full=Disease resistance protein RCH2 {ECO:0000303|PubMed:19519800};
DE AltName: Full=Disease resistance protein SLH1;
DE AltName: Full=Probable WRKY transcription factor 52;
DE AltName: Full=Protein RPS4-homolog {ECO:0000303|PubMed:10571887};
DE AltName: Full=Protein SENSITIVE TO LOW HUMIDITY 1;
DE AltName: Full=Resistance to Colletotrichum higginsianum 2 protein {ECO:0000303|PubMed:19519800};
DE AltName: Full=Resistance to Ralstonia solanacearum 1 protein {ECO:0000303|PubMed:11842188};
DE AltName: Full=WRKY DNA-binding protein 52;
GN Name=RRS1 {ECO:0000303|PubMed:11842188};
GN Synonyms=RCH2 {ECO:0000303|PubMed:19519800},
GN RRS1-S {ECO:0000303|PubMed:11842188}, RSH4 {ECO:0000303|PubMed:10571887},
GN SLH1, WRKY52; OrderedLocusNames=At5g45260/At5g45270;
GN ORFNames=K9E15.2/K9E15.3;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Col-5;
RX PubMed=11842188; DOI=10.1073/pnas.032485099;
RA Deslandes L., Olivier J., Theulieres F., Hirsch J., Feng D.X.,
RA Bittner-Eddy P., Beynon J., Marco Y.;
RT "Resistance to Ralstonia solanacearum in Arabidopsis thaliana is conferred
RT by the recessive RRS1-R gene, a member of a novel family of resistance
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2404-2409(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 2).
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] (ISOFORM 1).
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 [6]
RP FUNCTION.
RX PubMed=10571887; DOI=10.1046/j.1365-313x.1999.t01-1-00600.x;
RA Gassmann W., Hinsch M.E., Staskawicz B.J.;
RT "The Arabidopsis RPS4 bacterial-resistance gene is a member of the TIR-NBS-
RT LRR family of disease-resistance genes.";
RL Plant J. 20:265-277(1999).
RN [7]
RP INTERACTION WITH POPP2, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Col-5, and cv. Nd-1;
RX PubMed=12788974; DOI=10.1073/pnas.1230660100;
RA Deslandes L., Olivier J., Peeters N., Feng D.X., Khounlotham M.,
RA Boucher C., Somssich I., Genin S., Marco Y.;
RT "Physical interaction between RRS1-R, a protein conferring resistance to
RT bacterial wilt, and PopP2, a type III effector targeted to the plant
RT nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8024-8029(2003).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Columbia, cv. RLD, and cv. Wassilewskija;
RX PubMed=19519800; DOI=10.1111/j.1365-313x.2009.03949.x;
RA Narusaka M., Shirasu K., Noutoshi Y., Kubo Y., Shiraishi T., Iwabuchi M.,
RA Narusaka Y.;
RT "RRS1 and RPS4 provide a dual Resistance-gene system against fungal and
RT bacterial pathogens.";
RL Plant J. 60:218-226(2009).
RN [9]
RP FUNCTION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=24146667; DOI=10.3389/fpls.2013.00403;
RA Heidrich K., Tsuda K., Blanvillain-Baufume S., Wirthmueller L., Bautor J.,
RA Parker J.E.;
RT "Arabidopsis TNL-WRKY domain receptor RRS1 contributes to temperature-
RT conditioned RPS4 auto-immunity.";
RL Front. Plant Sci. 4:403-403(2013).
RN [10]
RP REVIEW.
RX PubMed=25506347; DOI=10.3389/fpls.2014.00606;
RA Cesari S., Bernoux M., Moncuquet P., Kroj T., Dodds P.N.;
RT "A novel conserved mechanism for plant NLR protein pairs: the 'integrated
RT decoy' hypothesis.";
RL Front. Plant Sci. 5:606-606(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 6-153 IN COMPLEX WITH RPS4,
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF SER-25; HIS-26 AND LYS-185.
RC STRAIN=cv. Columbia;
RX PubMed=24744375; DOI=10.1126/science.1247357;
RA Williams S.J., Sohn K.H., Wan L., Bernoux M., Sarris P.F., Segonzac C.,
RA Ve T., Ma Y., Saucet S.B., Ericsson D.J., Casey L.W., Lonhienne T.,
RA Winzor D.J., Zhang X., Coerdt A., Parker J.E., Dodds P.N., Kobe B.,
RA Jones J.D.;
RT "Structural basis for assembly and function of a heterodimeric plant immune
RT receptor.";
RL Science 344:299-303(2014).
CC -!- FUNCTION: Transcription factor. Interacts specifically with the W box
CC (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC acting element. Acts also as a disease resistance protein involved in
CC resistance to fungal and bacterial pathogens, including R.solanacearum,
CC P.syringae pv. tomato and C.higginsianum. Heterodimerization with RPS4
CC is required to form a functional complex to recognize AvrRps4 and PopP2
CC (PubMed:24744375). Contributes to temperature-conditioned RPS4 auto-
CC immunity (PubMed:24146667). {ECO:0000269|PubMed:10571887,
CC ECO:0000269|PubMed:11842188, ECO:0000269|PubMed:19519800,
CC ECO:0000269|PubMed:24146667, ECO:0000269|PubMed:24744375, ECO:0000305}.
CC -!- SUBUNIT: Interacts with PopP2, a R.solanacearum type III effector
CC (PubMed:12788974). Interacts with RPS4 (PubMed:24744375).
CC {ECO:0000269|PubMed:12788974, ECO:0000269|PubMed:24744375}.
CC -!- INTERACTION:
CC P0DKH5; Q9XGM3: RPS4; NbExp=18; IntAct=EBI-15211292, EBI-16102886;
CC P0DKH5; P0DKH5: RRS1; NbExp=5; IntAct=EBI-15211292, EBI-15211292;
CC P0DKH5; Q52432: avrRps4; Xeno; NbExp=4; IntAct=EBI-15211292, EBI-16103048;
CC P0DKH5; Q8Y125: popP2; Xeno; NbExp=4; IntAct=EBI-15211292, EBI-16103222;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12788974}. Cytoplasm
CC {ECO:0000305|PubMed:12788974}. Note=The nuclear localization is only
CC detected upon interaction with PopP2. {ECO:0000269|PubMed:12788974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DKH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DKH5-2; Sequence=VSP_015696;
CC -!- DOMAIN: The TIR does not cause cell death, but can suppress RPS4 TIR
CC domain-induced cell death (PubMed:24744375). The TIR domain is involved
CC in homo- and heterodimerization, but other domains also contribute to
CC the interaction (PubMed:24744375). {ECO:0000269|PubMed:24744375}.
CC -!- MISCELLANEOUS: Ecotypes susceptible to C.higginsianum or
CC R.solanacearum, such as cv. Columbia, contain a protein with a
CC premature stop codon, while the longer allele found in cv. Nd-1, cv.
CC Wassilewskija or cv. RLD confers resistance.
CC {ECO:0000269|PubMed:19519800}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the disease resistance TIR-NB-LRR family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10247.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g45260 and At5g45270.; Evidence={ECO:0000305};
CC Sequence=BAB10248.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g45260 and At5g45270.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIB-LRRS; Note=Functional and comparative genomics
CC of disease resistance gene homologs;
CC URL="http://niblrrs.ucdavis.edu";
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DR EMBL; AX103684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB020744; BAB10247.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB020744; BAB10248.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95222.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95223.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68859.1; -; Genomic_DNA.
DR EMBL; AK117156; BAC41834.1; -; mRNA.
DR EMBL; AK226456; BAE98598.1; -; mRNA.
DR RefSeq; NP_001078715.1; NM_001085246.2. [P0DKH5-2]
DR RefSeq; NP_001318742.1; NM_001344604.1. [P0DKH5-2]
DR RefSeq; NP_199339.2; NM_123894.4. [P0DKH5-1]
DR PDB; 4C6S; X-ray; 1.75 A; A=7-153.
DR PDB; 4C6T; X-ray; 2.65 A; A/C=6-153.
DR PDBsum; 4C6S; -.
DR PDBsum; 4C6T; -.
DR AlphaFoldDB; P0DKH5; -.
DR SMR; P0DKH5; -.
DR BioGRID; 19811; 2.
DR DIP; DIP-61676N; -.
DR IntAct; P0DKH5; 4.
DR STRING; 3702.AT5G45260.1; -.
DR PaxDb; P0DKH5; -.
DR PRIDE; P0DKH5; -.
DR EnsemblPlants; AT5G45260.1; AT5G45260.1; AT5G45260. [P0DKH5-1]
DR EnsemblPlants; AT5G45260.2; AT5G45260.2; AT5G45260. [P0DKH5-2]
DR EnsemblPlants; AT5G45260.3; AT5G45260.3; AT5G45260. [P0DKH5-2]
DR GeneID; 834562; -.
DR Gramene; AT5G45260.1; AT5G45260.1; AT5G45260. [P0DKH5-1]
DR Gramene; AT5G45260.2; AT5G45260.2; AT5G45260. [P0DKH5-2]
DR Gramene; AT5G45260.3; AT5G45260.3; AT5G45260. [P0DKH5-2]
DR KEGG; ath:AT5G45260; -.
DR Araport; AT5G45260; -.
DR OMA; KHIPREY; -.
DR OrthoDB; 73809at2759; -.
DR PhylomeDB; P0DKH5; -.
DR PRO; PR:P0DKH5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P0DKH5; baseline and differential.
DR Genevisible; P0DKH5; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 2.20.25.80; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003657; WRKY_dom.
DR InterPro; IPR036576; WRKY_dom_sf.
DR PANTHER; PTHR11017; PTHR11017; 2.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF03106; WRKY; 1.
DR SMART; SM00774; WRKY; 1.
DR SUPFAM; SSF118290; SSF118290; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
DR PROSITE; PS50811; WRKY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; DNA-binding;
KW Leucine-rich repeat; Nucleotide-binding; Nucleus; Plant defense;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1288
FT /note="Disease resistance protein RRS1"
FT /id="PRO_0000133693"
FT DOMAIN 5..146
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 170..421
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 498..522
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 535..553
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 554..575
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 577..598
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 621..646
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 665..688
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 697..720
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 740..764
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 766..791
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 792..807
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 808..829
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 830..852
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT DNA_BIND 1202..1270
FT /note="WRKY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 25..26
FT /note="Important for interaction with RPS4"
FT /evidence="ECO:0000269|PubMed:24744375"
FT REGION 1267..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 986..1003
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1188..1288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_015696"
FT MUTAGEN 25
FT /note="S->A: No effect on TIR domain homodimerization. Loss
FT of TIR domain heterodimerization; when associated with A-33
FT in RPS4."
FT /evidence="ECO:0000269|PubMed:24744375"
FT MUTAGEN 26
FT /note="H->A: No effect on TIR domain homodimerization. Loss
FT of TIR domain heterodimerization with RPS4."
FT /evidence="ECO:0000269|PubMed:24744375"
FT MUTAGEN 185
FT /note="K->A: No effect on pathogen effectors triggered cell
FT death."
FT /evidence="ECO:0000269|PubMed:24744375"
FT CONFLICT 395
FT /note="L -> S (in Ref. 4; BAC41834)"
FT /evidence="ECO:0000305"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:4C6S"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:4C6S"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:4C6S"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:4C6S"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4C6S"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:4C6S"
SQ SEQUENCE 1288 AA; 145879 MW; B364DE7CE4DB6706 CRC64;
MTNCEKDEEF VCISCVEEVR YSFVSHLSEA LRRKGINNVV VDVDIDDLLF KESQAKIEKA
GVSVMVLPGN CDPSEVWLDK FAKVLECQRN NKDQAVVSVL YGDSLLRDQW LSELDFRGLS
RIHQSRKECS DSILVEEIVR DVYETHFYVG RIGIYSKLLE IENMVNKQPI GIRCVGIWGM
PGIGKTTLAK AVFDQMSSAF DASCFIEDYD KSIHEKGLYC LLEEQLLPGN DATIMKLSSL
RDRLNSKRVL VVLDDVRNAL VGESFLEGFD WLGPGSLIII TSRDKQVFCL CGINQIYEVQ
GLNEKEARQL FLLSASIKED MGEQNLQELS VRVINYANGN PLAISVYGRE LKGKKKLSEM
ETAFLKLKRR PPFKIVDAFK STYDTLSDNE KNIFLDIACF FQGENVNYVI QLLEGCGFFP
HVEIDVLVDK CLVTISENRV WLHKLTQDIG REIINGETVQ IERRRRLWEP WSIKYLLEYN
EHKANGEPKT TFKRAQGSEE IEGLFLDTSN LRFDLQPSAF KNMLNLRLLK IYCSNPEVHP
VINFPTGSLH SLPNELRLLH WENYPLKSLP QNFDPRHLVE INMPYSQLQK LWGGTKNLEM
LRTIRLCHSH HLVDIDDLLK AENLEVIDLQ GCTRLQNFPA AGRLLRLRVV NLSGCIKIKS
VLEIPPNIEK LHLQGTGILA LPVSTVKPNH RELVNFLTEI PGLSEELERL TSLLESNSSC
QDLGKLICLE LKDCSCLQSL PNMANLDLNV LDLSGCSSLN SIQGFPRFLK QLYLGGTAIR
EVPQLPQSLE ILNAHGSCLR SLPNMANLEF LKVLDLSGCS ELETIQGFPR NLKELYFAGT
TLREVPQLPL SLEVLNAHGS DSEKLPMHYK FNNFFDLSQQ VVNDFLLKTL TYVKHIPRGY
TQELINKAPT FSFSAPSHTN QNATFDLQSG SSVMTRLNHS WRNTLVGFGM LVEVAFPEDY
CDATDVGISC VCRWSNKEGR SCRIERKFHC WAPWQVVPKV RKDHTFVFSD VNMRPSTGEG
NDPDIWAGLV VFEFFPINQQ TKCLNDRFTV RRCGVRVINV ATGNTSLENI ALVLSLDPVE
VSGYEVLRVS YDDLQEMDKV LFLYIASLFN DEDVDFVAPL IAGIDLDVSS GLKVLADVSL
ISVSSNGEIV MHSLQRQMGK EILHGQSMLL SDCESSMTEN LSDVPKKKKK HSESRVKKVV
SIPAIDEGDL WTWRKYGQKD ILGSRFPRGY YRCAYKFTHG CKATKQVQRS ETDSNMLAIT
YLSEHNHPRP TKRKALADST RSTSSSIC
