PSKR1_ARATH
ID PSKR1_ARATH Reviewed; 1008 AA.
AC Q9ZVR7; Q0WNS6; Q8S8L2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 4.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Phytosulfokine receptor 1 {ECO:0000303|PubMed:16829587};
DE Short=AtPSKR1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:21504901};
DE EC=4.6.1.2 {ECO:0000269|PubMed:21504901};
DE AltName: Full=Guanylate cyclase {ECO:0000303|PubMed:21504901};
DE AltName: Full=Phytosulfokine LRR receptor kinase 1;
DE AltName: Full=Protein serine-threonine kinase {ECO:0000303|PubMed:21504901};
DE Flags: Precursor;
GN Name=PSKR1 {ECO:0000303|PubMed:16829587}; Synonyms=PSKR;
GN OrderedLocusNames=At2g02220 {ECO:0000312|Araport:AT2G02220};
GN ORFNames=F5O4.1 {ECO:0000312|EMBL:AAM15093.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 439-1008.
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16829587; DOI=10.1104/pp.106.081109;
RA Matsubayashi Y., Ogawa M., Kihara H., Niwa M., Sakagami Y.;
RT "Disruption and overexpression of Arabidopsis phytosulfokine receptor gene
RT affects cellular longevity and potential for growth.";
RL Plant Physiol. 142:45-53(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17989228; DOI=10.1073/pnas.0706403104;
RA Amano Y., Tsubouchi H., Shinohara H., Ogawa M., Matsubayashi Y.;
RT "Tyrosine-sulfated glycopeptide involved in cellular proliferation and
RT expansion in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18333-18338(2007).
RN [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19076296; DOI=10.1111/j.1469-8137.2008.02710.x;
RA Kutschmar A., Rzewuski G., Stuehrwohldt N., Beemster G.T., Inze D.,
RA Sauter M.;
RT "PSK-alpha promotes root growth in Arabidopsis.";
RL New Phytol. 181:820-831(2009).
RN [7]
RP INDUCTION BY FUNGAL INFECTION AND WOUNDING.
RX PubMed=20403122; DOI=10.1111/j.1399-3054.2010.01371.x;
RA Loivamaki M., Stuhrwohldt N., Deeken R., Steffens B., Roitsch T.,
RA Hedrich R., Sauter M.;
RT "A role for PSK signaling in wounding and microbial interactions in
RT Arabidopsis.";
RL Physiol. Plantarum 139:348-357(2010).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF GLY-923.
RX PubMed=21504901; DOI=10.1074/jbc.m110.168823;
RA Kwezi L., Ruzvidzo O., Wheeler J.I., Govender K., Iacuone S.,
RA Thompson P.E., Gehring C., Irving H.R.;
RT "The phytosulfokine (PSK) receptor is capable of guanylate cyclase activity
RT and enabling cyclic GMP-dependent signaling in plants.";
RL J. Biol. Chem. 286:22580-22588(2011).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23062058; DOI=10.1111/tpj.12050;
RA Mosher S., Seybold H., Rodriguez P., Stahl M., Davies K.A., Dayaratne S.,
RA Morillo S.A., Wierzba M., Favery B., Keller H., Tax F.E., Kemmerling B.;
RT "The tyrosine-sulfated peptide receptors PSKR1 and PSY1R modify the
RT immunity of Arabidopsis to biotrophic and necrotrophic pathogens in an
RT antagonistic manner.";
RL Plant J. 73:469-482(2013).
RN [10]
RP SUBUNIT.
RX PubMed=25267325; DOI=10.1111/tpj.12680;
RA Fuglsang A.T., Kristensen A., Cuin T.A., Schulze W.X., Persson J.,
RA Thuesen K.H., Ytting C.K., Oehlenschlaeger C.B., Mahmood K.,
RA Sondergaard T.E., Shabala S., Palmgren M.G.;
RT "Receptor kinase-mediated control of primary active proton pumping at the
RT plasma membrane.";
RL Plant J. 80:951-964(2014).
RN [11]
RP FUNCTION, INTERACTION WITH AHA1; AHA2 AND BAK1, LACK OF INTERACTION WITH
RP CNGC17 AND BRI1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-923.
RX PubMed=26071421; DOI=10.1105/tpc.15.00306;
RA Ladwig F., Dahlke R.I., Stuehrwohldt N., Hartmann J., Harter K., Sauter M.;
RT "Phytosulfokine regulates growth in Arabidopsis through a response module
RT at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-
RT ATPase, and BAK1.";
RL Plant Cell 27:1718-1729(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 24-648 ALONE AND IN COMPLEX WITH
RP PSK AND CORECEPTOR, SUBUNIT, AND MUTAGENESIS OF PHE-596; SER-598; THR-619
RP AND SER-623.
RX PubMed=26308901; DOI=10.1038/nature14858;
RA Wang J., Li H., Han Z., Zhang H., Wang T., Lin G., Chang J., Yang W.,
RA Chai J.;
RT "Allosteric receptor activation by the plant peptide hormone
RT phytosulfokine.";
RL Nature 525:265-268(2015).
CC -!- FUNCTION: Phytosulfokine receptor with both a serine/threonine-protein
CC kinase activity and a guanylate cyclase activity (PubMed:21504901).
CC Regulates, in response to phytosulfokine binding, a signaling cascade
CC involved in plant cell differentiation, organogenesis, somatic
CC embryogenesis, cellular proliferation and plant growth. Involved in
CC plant immunity, with antagonistic effects on bacterial and fungal
CC resistances (PubMed:23062058). Not involved in PSY perception. CNGC17
CC and AHAs form a functional cation-translocating unit that is activated
CC by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421).
CC {ECO:0000269|PubMed:16829587, ECO:0000269|PubMed:17989228,
CC ECO:0000269|PubMed:21504901, ECO:0000269|PubMed:23062058}.
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:21504901};
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:21504901};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:21504901};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21504901};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21504901};
CC -!- ACTIVITY REGULATION: cGMP suppresses kinase activity.
CC {ECO:0000269|PubMed:21504901}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.5 uM for Ser/Thr peptide 1 for the protein serine-threonine
CC kinase activity {ECO:0000269|PubMed:21504901};
CC Vmax=1800 nmol/min/mg enzyme with Ser/Thr peptide 1 as substrate
CC {ECO:0000269|PubMed:21504901};
CC -!- SUBUNIT: Homo- and heterodimers with PSY1R (PubMed:25267325).
CC Heterodimers with the somatic embryogenesis receptor-like kinases
CC (SERKs) (PubMed:26308901). PSK is not directly involved in PSKR-SERK
CC interaction but stabilizes PSKR island domain for recruitment of a SERK
CC (PubMed:26308901). Part of a functional complex containing PSKR1, BAK1,
CC CNGC17, and AHA (PubMed:26071421). Interacts with AHA1, AHA2, and BAK1,
CC but not with CNGC17 or BRI1 (PubMed:26071421).
CC {ECO:0000269|PubMed:25267325, ECO:0000269|PubMed:26071421,
CC ECO:0000269|PubMed:26308901}.
CC -!- INTERACTION:
CC Q9ZVR7; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-16172949, EBI-20651385;
CC Q9ZVR7; Q9M9C5: At1g68400; NbExp=3; IntAct=EBI-16172949, EBI-1238661;
CC Q9ZVR7; A0A1I9LQ53: At3g50230; NbExp=3; IntAct=EBI-16172949, EBI-20654045;
CC Q9ZVR7; Q9FL63: At5g24100; NbExp=3; IntAct=EBI-16172949, EBI-20657062;
CC Q9ZVR7; A0A178UFM8: AXX17_At5g50380; NbExp=3; IntAct=EBI-16172949, EBI-20653342;
CC Q9ZVR7; Q94F62: BAK1; NbExp=5; IntAct=EBI-16172949, EBI-617138;
CC Q9ZVR7; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-16172949, EBI-16914444;
CC Q9ZVR7; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-16172949, EBI-1626936;
CC Q9ZVR7; Q94AG2: SERK1; NbExp=4; IntAct=EBI-16172949, EBI-1555537;
CC Q9ZVR7; Q9XIC7: SERK2; NbExp=5; IntAct=EBI-16172949, EBI-6299033;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26071421};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in roots, leaves, stems and
CC flowers (PubMed:16829587). Expressed in the primary and lateral roots,
CC including root primordia and root tips, but not in the hypocotyl
CC (PubMed:19076296). {ECO:0000269|PubMed:16829587,
CC ECO:0000269|PubMed:19076296}.
CC -!- INDUCTION: Up-regulated by fungal infection and wounding.
CC {ECO:0000269|PubMed:20403122}.
CC -!- DISRUPTION PHENOTYPE: Gradual loss of individual cells potential to
CC form callus as the tissues mature (PubMed:16829587). Premature
CC senescence of the leaves (PubMed:17989228). Limitted root growth
CC (PubMed:19076296). Enhanced resistance to bacterial biotrophic
CC pathogens, but increased susceptibility to necrotrophic fungal
CC infection (PubMed:23062058). {ECO:0000269|PubMed:16829587,
CC ECO:0000269|PubMed:17989228, ECO:0000269|PubMed:19076296,
CC ECO:0000269|PubMed:23062058}.
CC -!- MISCELLANEOUS: PSKR1 and PSYR1 mediate a signaling pathway by two
CC distinct ligands, which redundantly contribute to cellular
CC proliferation and plant growth. {ECO:0000269|PubMed:17989228}.
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; AC005312; AAC78507.3; -; Genomic_DNA.
DR EMBL; AC005936; AAM15093.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05558.1; -; Genomic_DNA.
DR EMBL; AK229360; BAF01223.1; -; mRNA.
DR PIR; D84434; D84434.
DR RefSeq; NP_178330.1; NM_126282.3.
DR PDB; 4Z63; X-ray; 2.51 A; A=24-648.
DR PDB; 4Z64; X-ray; 2.66 A; A=24-648.
DR PDBsum; 4Z63; -.
DR PDBsum; 4Z64; -.
DR AlphaFoldDB; Q9ZVR7; -.
DR SMR; Q9ZVR7; -.
DR BioGRID; 156; 37.
DR DIP; DIP-61780N; -.
DR IntAct; Q9ZVR7; 43.
DR STRING; 3702.AT2G02220.1; -.
DR TCDB; 1.A.87.2.9; the mechanosensitive calcium channel (mca) family.
DR iPTMnet; Q9ZVR7; -.
DR PaxDb; Q9ZVR7; -.
DR PRIDE; Q9ZVR7; -.
DR ProteomicsDB; 248894; -.
DR EnsemblPlants; AT2G02220.1; AT2G02220.1; AT2G02220.
DR GeneID; 814753; -.
DR Gramene; AT2G02220.1; AT2G02220.1; AT2G02220.
DR KEGG; ath:AT2G02220; -.
DR Araport; AT2G02220; -.
DR TAIR; locus:2051628; AT2G02220.
DR eggNOG; ENOG502QV5Y; Eukaryota.
DR HOGENOM; CLU_000288_22_9_1; -.
DR InParanoid; Q9ZVR7; -.
DR OMA; MSPYETH; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZVR7; -.
DR PRO; PR:Q9ZVR7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVR7; baseline and differential.
DR Genevisible; Q9ZVR7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031347; P:regulation of defense response; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 9.
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; Lyase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1008
FT /note="Phytosulfokine receptor 1"
FT /id="PRO_0000024371"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 75..98
FT /note="LRR 1"
FT REPEAT 99..123
FT /note="LRR 2"
FT REPEAT 124..148
FT /note="LRR 3"
FT REPEAT 150..170
FT /note="LRR 4"
FT REPEAT 172..194
FT /note="LRR 5"
FT REPEAT 195..219
FT /note="LRR 6"
FT REPEAT 221..243
FT /note="LRR 7"
FT REPEAT 244..266
FT /note="LRR 8"
FT REPEAT 291..315
FT /note="LRR 9"
FT REPEAT 316..339
FT /note="LRR 10"
FT REPEAT 341..362
FT /note="LRR 11"
FT REPEAT 363..387
FT /note="LRR 12"
FT REPEAT 392..414
FT /note="LRR 13"
FT REPEAT 415..438
FT /note="LRR 14"
FT REPEAT 439..464
FT /note="LRR 15"
FT REPEAT 466..486
FT /note="LRR 16"
FT REPEAT 521..545
FT /note="LRR 17"
FT REPEAT 546..570
FT /note="LRR 18"
FT REPEAT 571..594
FT /note="LRR 19"
FT REPEAT 596..619
FT /note="LRR 20"
FT DOMAIN 734..1005
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 860
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 300
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 346
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 370
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 372
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 398
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 424
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 445
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 508
FT /ligand="phytosulfokine"
FT /ligand_id="ChEBI:CHEBI:172962"
FT /evidence="ECO:0000269|PubMed:26308901"
FT BINDING 740..748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 731
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 807
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 847
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 902
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 596
FT /note="F->D: Decreased responsiveness to PSK for
FT interaction with BAK1 and decreased root length."
FT /evidence="ECO:0000269|PubMed:26308901"
FT MUTAGEN 598
FT /note="S->Y: Decreased responsiveness to PSK for
FT interaction with BAK1 and decreased root length."
FT /evidence="ECO:0000269|PubMed:26308901"
FT MUTAGEN 619
FT /note="T->Y: Decreased responsiveness to PSK for
FT interaction with BAK1 and decreased root length."
FT /evidence="ECO:0000269|PubMed:26308901"
FT MUTAGEN 623
FT /note="S->Y: No effect on responsiveness to PSK for
FT interaction with BAK1 and no effect on root length."
FT /evidence="ECO:0000269|PubMed:26308901"
FT MUTAGEN 923
FT /note="G->K: Decreased guanylate cyclase activity and
FT impaired PSK receptor function."
FT /evidence="ECO:0000269|PubMed:21504901,
FT ECO:0000269|PubMed:26071421"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4Z63"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4Z63"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4Z64"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4Z63"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4Z64"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4Z64"
FT HELIX 433..437
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:4Z64"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 565..569
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:4Z63"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 627..632
FT /evidence="ECO:0007829|PDB:4Z63"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:4Z64"
SQ SEQUENCE 1008 AA; 112354 MW; 858848FAE81F0A45 CRC64;
MRVHRFCVIV IFLTELLCFF YSSESQTTSR CHPHDLEALR DFIAHLEPKP DGWINSSSST
DCCNWTGITC NSNNTGRVIR LELGNKKLSG KLSESLGKLD EIRVLNLSRN FIKDSIPLSI
FNLKNLQTLD LSSNDLSGGI PTSINLPALQ SFDLSSNKFN GSLPSHICHN STQIRVVKLA
VNYFAGNFTS GFGKCVLLEH LCLGMNDLTG NIPEDLFHLK RLNLLGIQEN RLSGSLSREI
RNLSSLVRLD VSWNLFSGEI PDVFDELPQL KFFLGQTNGF IGGIPKSLAN SPSLNLLNLR
NNSLSGRLML NCTAMIALNS LDLGTNRFNG RLPENLPDCK RLKNVNLARN TFHGQVPESF
KNFESLSYFS LSNSSLANIS SALGILQHCK NLTTLVLTLN FHGEALPDDS SLHFEKLKVL
VVANCRLTGS MPRWLSSSNE LQLLDLSWNR LTGAIPSWIG DFKALFYLDL SNNSFTGEIP
KSLTKLESLT SRNISVNEPS PDFPFFMKRN ESARALQYNQ IFGFPPTIEL GHNNLSGPIW
EEFGNLKKLH VFDLKWNALS GSIPSSLSGM TSLEALDLSN NRLSGSIPVS LQQLSFLSKF
SVAYNNLSGV IPSGGQFQTF PNSSFESNHL CGEHRFPCSE GTESALIKRS RRSRGGDIGM
AIGIAFGSVF LLTLLSLIVL RARRRSGEVD PEIEESESMN RKELGEIGSK LVVLFQSNDK
ELSYDDLLDS TNSFDQANII GCGGFGMVYK ATLPDGKKVA IKKLSGDCGQ IEREFEAEVE
TLSRAQHPNL VLLRGFCFYK NDRLLIYSYM ENGSLDYWLH ERNDGPALLK WKTRLRIAQG
AAKGLLYLHE GCDPHILHRD IKSSNILLDE NFNSHLADFG LARLMSPYET HVSTDLVGTL
GYIPPEYGQA SVATYKGDVY SFGVVLLELL TDKRPVDMCK PKGCRDLISW VVKMKHESRA
SEVFDPLIYS KENDKEMFRV LEIACLCLSE NPKQRPTTQQ LVSWLDDV
