LRK19_ARATH
ID LRK19_ARATH Reviewed; 766 AA.
AC Q9LSR8; Q56XH0; Q93ZR5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=L-type lectin-domain containing receptor kinase I.9 {ECO:0000303|PubMed:19773388};
DE Short=LecRK-I.9 {ECO:0000303|PubMed:19773388};
DE Short=LecRK79 {ECO:0000303|PubMed:19773388};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein DOES NOT RESPOND TO NUCLEOTIDES 1 {ECO:0000303|PubMed:24436418};
DE AltName: Full=Purinoreceptor kinase 1 {ECO:0000303|PubMed:24436418};
DE Flags: Precursor;
GN Name=LECRK19 {ECO:0000303|PubMed:19773388};
GN Synonyms=DORN1 {ECO:0000303|PubMed:24436418},
GN P2K1 {ECO:0000303|PubMed:24436418};
GN OrderedLocusNames=At5g60300 {ECO:0000312|Araport:AT5G60300};
GN ORFNames=F15L12.17 {ECO:0000312|EMBL:BAA97509.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
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] (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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX DOI=10.1080/0735-260291044287;
RA Barre A., Herve C., Lescure B., Rouge P.;
RT "Lectin receptor kinases in plants.";
RL Crit. Rev. Plant Sci. 21:379-399(2002).
RN [6]
RP INTERACTION WITH RGD MOTIF, AND FUNCTION.
RX PubMed=16361528; DOI=10.1104/pp.105.066464;
RA Gouget A., Senchou V., Govers F., Sanson A., Barre A., Rouge P.,
RA Pont-Lezica R., Canut H.;
RT "Lectin receptor kinases participate in protein-protein interactions to
RT mediate plasma membrane-cell wall adhesions in Arabidopsis.";
RL Plant Physiol. 140:81-90(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19773388; DOI=10.1093/jxb/erp277;
RA Bouwmeester K., Govers F.;
RT "Arabidopsis L-type lectin receptor kinases: phylogeny, classification, and
RT expression profiles.";
RL J. Exp. Bot. 60:4383-4396(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21483488; DOI=10.1371/journal.ppat.1001327;
RA Bouwmeester K., de Sain M., Weide R., Gouget A., Klamer S., Canut H.,
RA Govers F.;
RT "The lectin receptor kinase LecRK-I.9 is a novel Phytophthora resistance
RT component and a potential host target for a RXLR effector.";
RL PLoS Pathog. 7:E1001327-E1001327(2011).
RN [9]
RP FUNCTION, MUTAGENESIS OF ASP-147; ALA-306; ARG-467; ASP-486; ASP-525 AND
RP ASP-572, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=25301072; DOI=10.1042/bj20140666;
RA Choi J., Tanaka K., Liang Y., Cao Y., Lee S.Y., Stacey G.;
RT "Extracellular ATP, a danger signal, is recognized by DORN1 in
RT Arabidopsis.";
RL Biochem. J. 463:429-437(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25083911; DOI=10.1094/mpmi-06-14-0191-r;
RA Wang Y., Bouwmeester K., Beseh P., Shan W., Govers F.;
RT "Phenotypic analyses of Arabidopsis T-DNA insertion lines and expression
RT profiling reveal that multiple L-type lectin receptor kinases are involved
RT in plant immunity.";
RL Mol. Plant Microbe Interact. 27:1390-1402(2014).
RN [11]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=23980842; DOI=10.1111/pbi.12111;
RA Bouwmeester K., Han M., Blanco-Portales R., Song W., Weide R., Guo L.-Y.,
RA van der Vossen E.A.G., Govers F.;
RT "The Arabidopsis lectin receptor kinase LecRK-I.9 enhances resistance to
RT Phytophthora infestans in Solanaceous plants.";
RL Plant Biotechnol. J. 12:10-16(2014).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-525 AND ASP-572.
RX PubMed=24436418; DOI=10.1126/science.343.6168.290;
RA Choi J., Tanaka K., Cao Y., Qi Y., Qiu J., Liang Y., Lee S.Y., Stacey G.;
RT "Identification of a plant receptor for extracellular ATP.";
RL Science 343:290-294(2014).
RN [13]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=26795144; DOI=10.1007/s00299-015-1926-2;
RA Wang Y., Nsibo D.L., Juhar H.M., Govers F., Bouwmeester K.;
RT "Ectopic expression of Arabidopsis L-type lectin receptor kinase genes
RT LecRK-I.9 and LecRK-IX.1 in Nicotiana benthamiana confers Phytophthora
RT resistance.";
RL Plant Cell Rep. 35:845-855(2016).
CC -!- FUNCTION: Essential receptor for extracellular ATP (PubMed:24436418,
CC PubMed:25301072). Binds ATP with high affinity through its
CC extracellular legume-lectin like region (PubMed:24436418). Is required
CC for ATP-induced intracellular calcium response, mitogen-activated
CC protein kinase 3 (MPK3) and MPK6 activation and ATP-induced gene
CC expression (PubMed:24436418, PubMed:25301072). May play a variety of
CC roles in stress resistance (PubMed:24436418). May be involved in
CC protein-protein interactions with RGD motif-containing proteins as
CC potential ligands (PubMed:21483488, PubMed:16361528). Plays probably a
CC structural and signaling role at the plant cell surfaces
CC (PubMed:24436418, PubMed:21483488). {ECO:0000269|PubMed:16361528,
CC ECO:0000269|PubMed:21483488, ECO:0000269|PubMed:24436418,
CC ECO:0000269|PubMed:25301072}.
CC -!- FUNCTION: Involved in resistance response to the pathogenic oomycetes
CC Phytophthora infestans and Phytophthora capsici.
CC {ECO:0000269|PubMed:23980842, ECO:0000269|PubMed:25083911,
CC ECO:0000269|PubMed:26795144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with RGD motif-containing proteins, suspected to
CC disrupt plasma membrane-cell wall adhesions, via its lectin region.
CC {ECO:0000269|PubMed:16361528}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21483488,
CC ECO:0000269|PubMed:25301072}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LSR8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSR8-2; Sequence=VSP_040342;
CC -!- TISSUE SPECIFICITY: Expressed in leaf petioles.
CC {ECO:0000269|PubMed:21483488}.
CC -!- INDUCTION: By infection with an avirulent isolate of Phytophthora
CC brassicae. {ECO:0000269|PubMed:21483488}.
CC -!- DOMAIN: The legume-lectin like region mediates RGD motif recognition.
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants (e.g. lecrk-I.9-1 and lecrk-I.9-2) are
CC defective in extracellular ATP-induced calcium response and susceptible
CC to an avirulent isolate of the oomycetes Phytophthora brassicae and
CC Phytophthora capsici. Impaired increase of cytoplasmic calcium
CC concentration in response to extracellular ATP (PubMed:25301072).
CC {ECO:0000269|PubMed:21483488, ECO:0000269|PubMed:24436418,
CC ECO:0000269|PubMed:25083911, ECO:0000269|PubMed:25301072}.
CC -!- BIOTECHNOLOGY: Confers enhanced resistance to late blight mediated by
CC the pathogenic oomycetes Phytophthora infestans and Phytophthora
CC capsici when transfected into Solanum tuberosum and Nicotiana
CC benthamiana. This resistance is associated with a high induction of
CC protease inhibitor genes. {ECO:0000269|PubMed:23980842,
CC ECO:0000269|PubMed:26795144}.
CC -!- MISCELLANEOUS: Plants over-expressing LECRK19 have more compact
CC rosettes with smaller and slightly wrinkled leaves, reduced height,
CC accumulate anthocyanin and lignin and show enhanced resistance to the
CC oomycete Phytophthora brassicae (PubMed:21483488). Ectopic expression
CC of LECRK19 increases plant response to physical wounding
CC (PubMed:24436418). {ECO:0000305|PubMed:21483488,
CC ECO:0000305|PubMed:24436418}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000305}.
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DR EMBL; AB026632; BAA97509.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97304.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97305.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97306.1; -; Genomic_DNA.
DR EMBL; AY056317; AAL07166.1; -; mRNA.
DR EMBL; AY120738; AAM53296.1; -; mRNA.
DR EMBL; AY139978; AAM98121.1; -; mRNA.
DR EMBL; BT000349; AAN15668.1; -; mRNA.
DR EMBL; AK221704; BAD95423.1; -; mRNA.
DR RefSeq; NP_001078773.1; NM_001085304.1. [Q9LSR8-1]
DR RefSeq; NP_200838.1; NM_125423.3. [Q9LSR8-2]
DR RefSeq; NP_851230.1; NM_180899.2. [Q9LSR8-2]
DR AlphaFoldDB; Q9LSR8; -.
DR SMR; Q9LSR8; -.
DR STRING; 3702.AT5G60300.3; -.
DR TCDB; 1.A.87.2.3; the mechanosensitive calcium channel (mca) family.
DR iPTMnet; Q9LSR8; -.
DR PaxDb; Q9LSR8; -.
DR PRIDE; Q9LSR8; -.
DR ProteomicsDB; 238562; -. [Q9LSR8-1]
DR EnsemblPlants; AT5G60300.1; AT5G60300.1; AT5G60300. [Q9LSR8-2]
DR EnsemblPlants; AT5G60300.2; AT5G60300.2; AT5G60300. [Q9LSR8-2]
DR EnsemblPlants; AT5G60300.3; AT5G60300.3; AT5G60300. [Q9LSR8-1]
DR GeneID; 836152; -.
DR Gramene; AT5G60300.1; AT5G60300.1; AT5G60300. [Q9LSR8-2]
DR Gramene; AT5G60300.2; AT5G60300.2; AT5G60300. [Q9LSR8-2]
DR Gramene; AT5G60300.3; AT5G60300.3; AT5G60300. [Q9LSR8-1]
DR KEGG; ath:AT5G60300; -.
DR Araport; AT5G60300; -.
DR TAIR; locus:2144045; AT5G60300.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR InParanoid; Q9LSR8; -.
DR OMA; VWIAPLK; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LSR8; -.
DR PRO; PR:Q9LSR8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSR8; baseline and differential.
DR Genevisible; Q9LSR8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0071318; P:cellular response to ATP; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IDA:UniProtKB.
DR GO; GO:0106167; P:extracellular ATP signaling; IMP:TAIR.
DR GO; GO:0048041; P:focal adhesion assembly; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:UniProtKB.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Lectin; Membrane; Nucleotide-binding; Plant defense; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal;
KW Stress response; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..766
FT /note="L-type lectin-domain containing receptor kinase I.9"
FT /id="PRO_0000403078"
FT TOPO_DOM 22..289
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 344..616
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..259
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 350..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 719..766
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040342"
FT MUTAGEN 147
FT /note="D->N: In dorn1-6; impaired increase of cytoplasmic
FT calcium concentration in response to extracellular ATP."
FT /evidence="ECO:0000269|PubMed:25301072"
FT MUTAGEN 306
FT /note="A->T: In dorn1-7; impaired increase of cytoplasmic
FT calcium concentration in response to extracellular ATP."
FT /evidence="ECO:0000269|PubMed:25301072"
FT MUTAGEN 467
FT /note="R->Q: In dorn1-9; impaired increase of cytoplasmic
FT calcium concentration in response to extracellular ATP."
FT /evidence="ECO:0000269|PubMed:25301072"
FT MUTAGEN 486
FT /note="D->N: In dorn1-5; impaired increase of cytoplasmic
FT calcium concentration in response to extracellular ATP."
FT /evidence="ECO:0000269|PubMed:25301072"
FT MUTAGEN 525
FT /note="D->N: In dorn1-2; loss of kinase activity. Impaired
FT increase of cytoplasmic calcium concentration in response
FT to extracellular ATP."
FT /evidence="ECO:0000269|PubMed:24436418,
FT ECO:0000269|PubMed:25301072"
FT MUTAGEN 572
FT /note="D->N: In dorn1-1; loss of kinase activity. Impaired
FT increase of cytoplasmic calcium concentration in response
FT to extracellular ATP."
FT /evidence="ECO:0000269|PubMed:24436418,
FT ECO:0000269|PubMed:25301072"
FT CONFLICT 475..477
FT /note="MLD -> VLE (in Ref. 4; BAD95423)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="E -> K (in Ref. 3; AAL07166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 85319 MW; F47912152E08F505 CRC64;
MARWLLQILI ISSLHLSSVS SQQETSFVYE SFLDRQNLYL DKSAIVLPSG LLQLTNASEH
QMGHAFHKKP IEFSSSGPLS FSTHFVCALV PKPGFEGGHG IVFVLSPSMD FTHAESTRYL
GIFNASTNGS SSYHVLAVEL DTIWNPDFKD IDHNHVGIDV NSPISVAIAS ASYYSDMKGS
NESINLLSGN PIQVWVDYEG TLLNVSVAPL EVQKPTRPLL SHPINLTELF PNRSSLFAGF
SAATGTAISD QYILWWSFSI DRGSLQRLDI SKLPEVPHPR APHKKVSTLI ILLPVCLAIL
VLAVLAGLYF RRRRKYSEVS ETWEKEFDAH RFSYRSLFKA TKGFSKDEFL GKGGFGEVYR
GNLPQGREIA VKRVSHNGDE GVKQFVAEVV SMRCLKHRNL VPLFGYCRRK RELLLVSEYM
PNGSLDEHLF DDQKPVLSWS QRLVVVKGIA SALWYLHTGA DQVVLHRDVK ASNIMLDAEF
HGRLGDFGMA RFHEHGGNAA TTAAVGTVGY MAPELITMGA STGTDVYAFG VFMLEVTCGR
RPVEPQLQVE KRHMIKWVCE CWKKDSLLDA TDPRLGGKFV AEEVEMVMKL GLLCSNIVPE
SRPTMEQVVL YLNKNLPLPD FSPYTLGIGT FAPVLVDASS LVVSSASWSL SGPSMSSSSP
NHSPYAWQST DQPWGQTIDT KNSLHIVAEP EKPSPAVKMV TLPAEDPQSN HSSISSQRVQ
PVKREKRRLH QILVAFPWIN KQYFKLGLPK HIVHVSLFFF LQLARL
