PEPR1_ARATH
ID PEPR1_ARATH Reviewed; 1123 AA.
AC Q9SSL9; Q8GZ71; Q8L740;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Leucine-rich repeat receptor-like protein kinase PEPR1;
DE EC=2.7.11.1;
DE AltName: Full=Elicitor peptide 1 receptor 1;
DE Short=PEP1 receptor 1;
DE Flags: Precursor;
GN Name=PEPR1; OrderedLocusNames=At1g73080; ORFNames=F3N23.28;
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=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 [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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION, AND
RP INTERACTION WITH PEP1.
RX PubMed=16785433; DOI=10.1073/pnas.0603729103;
RA Yamaguchi Y., Pearce G., Ryan C.A.;
RT "The cell surface leucine-rich repeat receptor for AtPep1, an endogenous
RT peptide elicitor in Arabidopsis, is functional in transgenic tobacco
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10104-10109(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [8]
RP INTERACTION WITH PEP1.
RX PubMed=18824048; DOI=10.1016/j.peptides.2008.08.019;
RA Pearce G., Yamaguchi Y., Munske G., Ryan C.A.;
RT "Structure-activity studies of AtPep1, a plant peptide signal involved in
RT the innate immune response.";
RL Peptides 29:2083-2089(2008).
RN [9]
RP INTERACTION WITH BAK1.
RX PubMed=20018402; DOI=10.1016/j.ejcb.2009.11.001;
RA Postel S., Kuefner I., Beuter C., Mazzotta S., Schwedt A., Borlotti A.,
RA Halter T., Kemmerling B., Nuernberger T.;
RT "The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated
RT in Arabidopsis development and immunity.";
RL Eur. J. Cell Biol. 89:169-174(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH BIK1 AND PBL1.
RX PubMed=23431184; DOI=10.1073/pnas.1215543110;
RA Liu Z., Wu Y., Yang F., Zhang Y., Chen S., Xie Q., Tian X., Zhou J.M.;
RT "BIK1 interacts with PEPRs to mediate ethylene-induced immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6205-6210(2013).
CC -!- FUNCTION: Acts as a receptor for PEP defense peptides. Unlike typical
CC immune receptors, senses an endogenous elicitor that potentiates
CC pathogen-associated molecular pattern (PAMP)-inducible plant responses.
CC Involved in PAMP-triggered immunity (PTI) signaling. Interacts with and
CC phosphorylates the kinase BIK1, a central rate-limiting kinase in PTI
CC signaling (PubMed:23431184). {ECO:0000269|PubMed:16785433,
CC ECO:0000269|PubMed:23431184}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with PEP1 and BAK1 (PubMed:16785433,
CC PubMed:18824048, PubMed:20018402). Interacts with BIK1 and PBL1
CC (PubMed:23431184). {ECO:0000269|PubMed:16785433,
CC ECO:0000269|PubMed:18824048, ECO:0000269|PubMed:20018402,
CC ECO:0000269|PubMed:23431184}.
CC -!- INTERACTION:
CC Q9SSL9; Q8W4S5: At5g63710; NbExp=5; IntAct=EBI-15588112, EBI-16934827;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16785433}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC008017; AAD55655.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35411.1; -; Genomic_DNA.
DR EMBL; AK117178; BAC41855.1; -; mRNA.
DR EMBL; AY139779; AAM98097.1; -; mRNA.
DR EMBL; FJ708680; ACN59275.1; -; mRNA.
DR PIR; D96756; D96756.
DR RefSeq; NP_177451.1; NM_105966.2.
DR PDB; 5GR8; X-ray; 2.59 A; A/D=29-738.
DR PDBsum; 5GR8; -.
DR AlphaFoldDB; Q9SSL9; -.
DR SMR; Q9SSL9; -.
DR BioGRID; 28858; 23.
DR DIP; DIP-61207N; -.
DR IntAct; Q9SSL9; 22.
DR STRING; 3702.AT1G73080.1; -.
DR iPTMnet; Q9SSL9; -.
DR PaxDb; Q9SSL9; -.
DR PRIDE; Q9SSL9; -.
DR ProteomicsDB; 236809; -.
DR EnsemblPlants; AT1G73080.1; AT1G73080.1; AT1G73080.
DR GeneID; 843639; -.
DR Gramene; AT1G73080.1; AT1G73080.1; AT1G73080.
DR KEGG; ath:AT1G73080; -.
DR Araport; AT1G73080; -.
DR TAIR; locus:2032697; AT1G73080.
DR eggNOG; ENOG502QUAH; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9SSL9; -.
DR OMA; TPCSSWV; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9SSL9; -.
DR PRO; PR:Q9SSL9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSL9; baseline and differential.
DR Genevisible; Q9SSL9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:TAIR.
DR GO; GO:0001653; F:peptide receptor activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; TAS:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 14.
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 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1123
FT /note="Leucine-rich repeat receptor-like protein kinase
FT PEPR1"
FT /id="PRO_0000389459"
FT TOPO_DOM 29..769
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 791..1123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..53
FT /note="LRR 1"
FT REPEAT 74..98
FT /note="LRR 2"
FT REPEAT 99..122
FT /note="LRR 3"
FT REPEAT 124..145
FT /note="LRR 4"
FT REPEAT 146..170
FT /note="LRR 5"
FT REPEAT 171..194
FT /note="LRR 6"
FT REPEAT 196..218
FT /note="LRR 7"
FT REPEAT 219..243
FT /note="LRR 8"
FT REPEAT 245..266
FT /note="LRR 9"
FT REPEAT 267..290
FT /note="LRR 10"
FT REPEAT 292..314
FT /note="LRR 11"
FT REPEAT 315..338
FT /note="LRR 12"
FT REPEAT 340..362
FT /note="LRR 13"
FT REPEAT 363..386
FT /note="LRR 14"
FT REPEAT 388..410
FT /note="LRR 15"
FT REPEAT 412..434
FT /note="LRR 16"
FT REPEAT 435..458
FT /note="LRR 17"
FT REPEAT 459..482
FT /note="LRR 18"
FT REPEAT 484..505
FT /note="LRR 19"
FT REPEAT 506..529
FT /note="LRR 20"
FT REPEAT 530..553
FT /note="LRR 21"
FT REPEAT 554..577
FT /note="LRR 22"
FT REPEAT 579..600
FT /note="LRR 23"
FT REPEAT 601..625
FT /note="LRR 24"
FT REPEAT 626..650
FT /note="LRR 25"
FT REPEAT 652..674
FT /note="LRR 26"
FT REPEAT 675..696
FT /note="LRR 27"
FT REPEAT 697..721
FT /note="LRR 28"
FT DOMAIN 827..1115
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 954
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 833..841
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 824
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 901
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 941
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 995
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 288
FT /note="G -> E (in Ref. 4; AAM98097)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="N -> D (in Ref. 3; BAC41855)"
FT /evidence="ECO:0000305"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:5GR8"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:5GR8"
FT TURN 453..458
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 524..528
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 548..552
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 572..576
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 581..584
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 596..600
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 644..647
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 669..673
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 692..696
FT /evidence="ECO:0007829|PDB:5GR8"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 720..724
FT /evidence="ECO:0007829|PDB:5GR8"
FT HELIX 726..729
FT /evidence="ECO:0007829|PDB:5GR8"
SQ SEQUENCE 1123 AA; 122897 MW; 280C3F0B49C9C566 CRC64;
MKNLGGLFKI LLLFFCLFLS THIISVSCLN SDGLTLLSLL KHLDRVPPQV TSTWKINASE
ATPCNWFGIT CDDSKNVASL NFTRSRVSGQ LGPEIGELKS LQILDLSTNN FSGTIPSTLG
NCTKLATLDL SENGFSDKIP DTLDSLKRLE VLYLYINFLT GELPESLFRI PKLQVLYLDY
NNLTGPIPQS IGDAKELVEL SMYANQFSGN IPESIGNSSS LQILYLHRNK LVGSLPESLN
LLGNLTTLFV GNNSLQGPVR FGSPNCKNLL TLDLSYNEFE GGVPPALGNC SSLDALVIVS
GNLSGTIPSS LGMLKNLTIL NLSENRLSGS IPAELGNCSS LNLLKLNDNQ LVGGIPSALG
KLRKLESLEL FENRFSGEIP IEIWKSQSLT QLLVYQNNLT GELPVEMTEM KKLKIATLFN
NSFYGAIPPG LGVNSSLEEV DFIGNKLTGE IPPNLCHGRK LRILNLGSNL LHGTIPASIG
HCKTIRRFIL RENNLSGLLP EFSQDHSLSF LDFNSNNFEG PIPGSLGSCK NLSSINLSRN
RFTGQIPPQL GNLQNLGYMN LSRNLLEGSL PAQLSNCVSL ERFDVGFNSL NGSVPSNFSN
WKGLTTLVLS ENRFSGGIPQ FLPELKKLST LQIARNAFGG EIPSSIGLIE DLIYDLDLSG
NGLTGEIPAK LGDLIKLTRL NISNNNLTGS LSVLKGLTSL LHVDVSNNQF TGPIPDNLEG
QLLSEPSSFS GNPNLCIPHS FSASNNSRSA LKYCKDQSKS RKSGLSTWQI VLIAVLSSLL
VLVVVLALVF ICLRRRKGRP EKDAYVFTQE EGPSLLLNKV LAATDNLNEK YTIGRGAHGI
VYRASLGSGK VYAVKRLVFA SHIRANQSMM REIDTIGKVR HRNLIKLEGF WLRKDDGLML
YRYMPKGSLY DVLHGVSPKE NVLDWSARYN VALGVAHGLA YLHYDCHPPI VHRDIKPENI
LMDSDLEPHI GDFGLARLLD DSTVSTATVT GTTGYIAPEN AFKTVRGRES DVYSYGVVLL
ELVTRKRAVD KSFPESTDIV SWVRSALSSS NNNVEDMVTT IVDPILVDEL LDSSLREQVM
QVTELALSCT QQDPAMRPTM RDAVKLLEDV KHLARSCSSD SVR
