EDR1_ARATH
ID EDR1_ARATH Reviewed; 933 AA.
AC Q9FPR3; Q9FRR5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase EDR1;
DE EC=2.7.11.1;
DE AltName: Full=MAPKK kinase EDR1;
DE AltName: Full=Protein ENHANCED DISEASE RESISTANCE 1;
DE Short=AtEDR1;
DE AltName: Full=Serine/threonine/tyrosine-protein kinase 10;
GN Name=EDR1; Synonyms=STY10; OrderedLocusNames=At1g08720; ORFNames=F22O13.20;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11114160; DOI=10.1073/pnas.98.1.373;
RA Frye C.A., Tang D., Innes R.W.;
RT "Negative regulation of defense responses in plants by a conserved MAPKK
RT kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:373-378(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=19064707; DOI=10.1534/genetics.108.097279;
RA Caldwell K.S., Michelmore R.W.;
RT "Arabidopsis thaliana genes encoding defense signaling and recognition
RT proteins exhibit contrasting evolutionary dynamics.";
RL Genetics 181:671-684(2009).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9634583; DOI=10.2307/3870681;
RA Frye C.A., Innes R.W.;
RT "An Arabidopsis mutant with enhanced resistance to powdery mildew.";
RL Plant Cell 10:947-956(1998).
RN [6]
RP FUNCTION, MUTAGENESIS OF LYS-696, CATALYTIC ACTIVITY, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=12492839; DOI=10.1046/j.1365-313x.2002.01482.x;
RA Tang D., Innes R.W.;
RT "Overexpression of a kinase-deficient form of the EDR1 gene enhances
RT powdery mildew resistance and ethylene-induced senescence in Arabidopsis.";
RL Plant J. 32:975-983(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15894742; DOI=10.1104/pp.105.060400;
RA Tang D., Christiansen K.M., Innes R.W.;
RT "Regulation of plant disease resistance, stress responses, cell death, and
RT ethylene signaling in Arabidopsis by the EDR1 protein kinase.";
RL Plant Physiol. 138:1018-1026(2005).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16429265; DOI=10.1007/s11103-005-4109-7;
RA Rudrabhatla P., Reddy M.M., Rajasekharan R.;
RT "Genome-wide analysis and experimentation of plant
RT serine/threonine/tyrosine-specific protein kinases.";
RL Plant Mol. Biol. 60:293-319(2006).
RN [9]
RP FUNCTION IN DEFENSE PRIMING, AND DISRUPTION PHENOTYPE.
RX PubMed=16565218; DOI=10.1073/pnas.0510213103;
RA van Hulten M., Pelser M., van Loon L.C., Pieterse C.M., Ton J.;
RT "Costs and benefits of priming for defense in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5602-5607(2006).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18815384; DOI=10.1104/pp.108.127605;
RA Wawrzynska A., Christiansen K.M., Lan Y., Rodibaugh N.L., Innes R.W.;
RT "Powdery mildew resistance conferred by loss of the ENHANCED DISEASE
RT RESISTANCE1 protein kinase is suppressed by a missense mutation in KEEP ON
RT GOING, a regulator of abscisic acid signaling.";
RL Plant Physiol. 148:1510-1522(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19318610; DOI=10.1105/tpc.108.062158;
RA Beckers G.J.M., Jaskiewicz M., Liu Y., Underwood W.R., He S.Y., Zhang S.,
RA Conrath U.;
RT "Mitogen-activated protein kinases 3 and 6 are required for full priming of
RT stress responses in Arabidopsis thaliana.";
RL Plant Cell 21:944-953(2009).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21726375; DOI=10.1111/j.1364-3703.2011.00708.x;
RA Christiansen K.M., Gu Y., Rodibaugh N., Innes R.W.;
RT "Negative regulation of defence signalling pathways by the EDR1 protein
RT kinase.";
RL Mol. Plant Pathol. 12:746-758(2011).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21605210; DOI=10.1111/j.1365-313x.2011.04651.x;
RA Hiruma K., Nishiuchi T., Kato T., Bednarek P., Okuno T., Schulze-Lefert P.,
RA Takano Y.;
RT "Arabidopsis ENHANCED DISEASE RESISTANCE 1 is required for pathogen-induced
RT expression of plant defensins in nonhost resistance, and acts through
RT interference of MYC2-mediated repressor function.";
RL Plant J. 67:980-992(2011).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP KEG.
RX PubMed=21343429; DOI=10.1104/pp.110.171785;
RA Gu Y., Innes R.W.;
RT "The KEEP ON GOING protein of Arabidopsis recruits the ENHANCED DISEASE
RT RESISTANCE1 protein to trans-Golgi network/early endosome vesicles.";
RL Plant Physiol. 155:1827-1838(2011).
RN [15]
RP REVIEW.
RX PubMed=22057322; DOI=10.4161/psb.6.11.17494;
RA Hiruma K., Takano Y.;
RT "Roles of EDR1 in non-host resistance of Arabidopsis.";
RL Plant Signal. Behav. 6:1831-1833(2011).
RN [16]
RP INDUCTION BY POWDERY MILDEW, INTERACTION WITH EDR4, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25747881; DOI=10.1105/tpc.114.134668;
RA Wu G., Liu S., Zhao Y., Wang W., Kong Z., Tang D.;
RT "ENHANCED DISEASE RESISTANCE4 associates with CLATHRIN HEAVY CHAIN2 and
RT modulates plant immunity by regulating relocation of EDR1 in Arabidopsis.";
RL Plant Cell 27:857-873(2015).
CC -!- FUNCTION: MAPKKK serine/threonine-protein kinase involved in the
CC regulation of a MAP kinase cascade (probably including MPK3 and MPK6)
CC that negatively regulates salicylic acid- (SA-) dependent defense
CC responses, abscisic acid (ABA) signaling, and ethylene-induced
CC senescence. Modulates also stress response (e.g. drought) signaling and
CC cell death, in an ORE9-dependent manner. Functions at a point of cross
CC talk between ethylene, ABA and SA signaling that impinges on senescence
CC and cell death. On the other hand, it confers sensitivity to various
CC pathogens such as the fungus E.cichoracearum, the oomycete H.parasitica
CC and the bacteria P.syringae pv. tomato DC3000. Required for resistance
CC to some hemibiotrophic/necrotrophic fungal pathogens (e.g.
CC C.gloeosporioides, C.higginsianum and A.brassicicola) through the
CC induction of defensin expression, probably by repressing MYC2, an
CC inhibitor of defensin genes (PDFs). Together with KEG, may regulate
CC endocytic trafficking and/or the formation of signaling complexes on
CC trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress
CC responses. {ECO:0000269|PubMed:11114160, ECO:0000269|PubMed:12492839,
CC ECO:0000269|PubMed:15894742, ECO:0000269|PubMed:16565218,
CC ECO:0000269|PubMed:18815384, ECO:0000269|PubMed:19318610,
CC ECO:0000269|PubMed:21343429, ECO:0000269|PubMed:21605210,
CC ECO:0000269|PubMed:21726375, ECO:0000269|PubMed:9634583}.
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:0000269|PubMed:12492839};
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:0000269|PubMed:12492839};
CC -!- SUBUNIT: Interacts with KEG (PubMed:21343429). Binds and recruited by
CC EDR4 at the powdery mildew (e.g. G.cichoracearum) penetration site on
CC the plasma membrane (PubMed:25747881). {ECO:0000269|PubMed:21343429,
CC ECO:0000269|PubMed:25747881}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25747881}.
CC Endosome {ECO:0000269|PubMed:25747881}. Nucleus. Endoplasmic reticulum.
CC Golgi apparatus, trans-Golgi network. Early endosome. Note=Displays
CC dynamic movement in cells with accumulation at the plasma membrane
CC around pathogenic fungus penetration site (PubMed:25747881). Excluded
CC from the nucleolus. Targeted to trans-Golgi network and early endosome
CC vesicles via interaction with KEG. {ECO:0000269|PubMed:25747881}.
CC -!- INDUCTION: Accumulates at the penetration site of powdery mildew (e.g.
CC G.cichoracearum) infection. {ECO:0000269|PubMed:25747881}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to abscisic acid (ABA). Confers
CC defense priming against pathogens and stresses such as E.cichoracearum,
CC H.parasitica and P.syringae pv. tomato DC3000. This enhanced resistance
CC is associated with a faster induction of several defense responses,
CC including callose deposition and host cell death, in a salicylic
CC acid- (SA-) dependent manner, as well as a strong elicitation of
CC stress-induced MPK3 and MPK6 activity. Enhanced stress responses and
CC spontaneous necrotic lesions under drought conditions. In contrast,
CC reduced resistance to the non-adapted hemibiotrophic C.gloeosporioides
CC and higher susceptibility to the host-adapted pathogens C.higginsianum
CC and necrotrophic A.brassicicola. These phenotypes are rescued by
CC disruption of KEG. {ECO:0000269|PubMed:11114160,
CC ECO:0000269|PubMed:15894742, ECO:0000269|PubMed:16565218,
CC ECO:0000269|PubMed:18815384, ECO:0000269|PubMed:19318610,
CC ECO:0000269|PubMed:21343429, ECO:0000269|PubMed:21605210,
CC ECO:0000269|PubMed:21726375, ECO:0000269|PubMed:9634583}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99762.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g08720 and At1g08730.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF305913; AAG31143.1; -; mRNA.
DR EMBL; EF470626; ABR45962.1; -; Genomic_DNA.
DR EMBL; EF470630; ABR45966.1; -; Genomic_DNA.
DR EMBL; EF470631; ABR45967.1; -; Genomic_DNA.
DR EMBL; EF470634; ABR45970.1; -; Genomic_DNA.
DR EMBL; EF470643; ABR45979.1; -; Genomic_DNA.
DR EMBL; EF470645; ABR45981.1; -; Genomic_DNA.
DR EMBL; AC003981; AAF99762.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28339.1; -; Genomic_DNA.
DR PIR; T00726; T00726.
DR RefSeq; NP_563824.1; NM_100745.2.
DR AlphaFoldDB; Q9FPR3; -.
DR SMR; Q9FPR3; -.
DR BioGRID; 22634; 3.
DR STRING; 3702.AT1G08720.1; -.
DR iPTMnet; Q9FPR3; -.
DR PaxDb; Q9FPR3; -.
DR PRIDE; Q9FPR3; -.
DR ProteomicsDB; 247072; -.
DR EnsemblPlants; AT1G08720.1; AT1G08720.1; AT1G08720.
DR GeneID; 837393; -.
DR Gramene; AT1G08720.1; AT1G08720.1; AT1G08720.
DR KEGG; ath:AT1G08720; -.
DR Araport; AT1G08720; -.
DR TAIR; locus:2025515; AT1G08720.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_006806_0_0_1; -.
DR InParanoid; Q9FPR3; -.
DR OMA; IKMPCRL; -.
DR OrthoDB; 173077at2759; -.
DR PhylomeDB; Q9FPR3; -.
DR PRO; PR:Q9FPR3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FPR3; baseline and differential.
DR Genevisible; Q9FPR3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IMP:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; ISS:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Abscisic acid signaling pathway; ATP-binding; Cell membrane;
KW Endoplasmic reticulum; Endosome; Ethylene signaling pathway;
KW Golgi apparatus; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..933
FT /note="Serine/threonine-protein kinase EDR1"
FT /id="PRO_0000421116"
FT DOMAIN 669..925
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 792
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 675..683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 696
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12492839"
SQ SEQUENCE 933 AA; 103589 MW; 650E2FF0841205D7 CRC64;
MKHIFKKLHR GGNQEQQNRT NDAAPPSDQN RIHVSANPPQ ATPSSVTETL PVAGATSSMA
SPAPTAASNR ADYMSSEEEY QVQLALAISA SNSQSSEDPE KHQIRAATLL SLGSHQRMDS
RRDSSEVVAQ RLSRQYWEYG VLDYEEKVVD SFYDVYSLST DSAKQGEMPS LEDLESNHGT
PGFEAVVVNR PIDSSLHELL EIAECIALGC STTSVSVLVQ RLAELVTEHM GGSAEDSSIV
LARWTEKSSE FKAALNTCVF PIGFVKIGIS RHRALLFKVL ADSVRLPCRL VKGSHYTGNE
DDAVNTIRLE DEREYLVDLM TDPGTLIPAD FASASNNTVE PCNSNGNKFP TAQFSNDVPK
LSEGEGSSHS SMANYSSSLD RRTEAERTDS SYPKVGPLRN IDYSSPSSVT SSTQLENNSS
TAIGKGSRGA IIECSRTNMN IVPYNQNSEE DPKNLFADLN PFQNKGADKL YMPTKSGLNN
VDDFHQQKNN PLVGRSPAPM MWKNYSCNEA PKRKENSYIE NLLPKLHRDP RYGNTQSSYA
TSSSNGAISS NVHGRDNVTF VSPVAVPSSF TSTENQFRPS IVEDMNRNTN NELDLQPHTA
AVVHGQQNDE SHIHDHRKYT SDDISTGCDP RLKDHESTSS SLDSTSYRND PQVLDDADVG
ECEIPWNDLV IAERIGLGSY GEVYHADWHG TEVAVKKFLD QDFSGAALAE FRSEVRIMRR
LRHPNVVFFL GAVTRPPNLS IVTEFLPRGS LYRILHRPKS HIDERRRIKM ALDVAMGMNC
LHTSTPTIVH RDLKTPNLLV DNNWNVKVGD FGLSRLKHNT FLSSKSTAGT PEWMAPEVLR
NEPSNEKCDV YSFGVILWEL ATLRLPWRGM NPMQVVGAVG FQNRRLEIPK ELDPVVGRII
LECWQTDPNL RPSFAQLTEV LKPLNRLVLP TPQ
