FERON_ARATH
ID FERON_ARATH Reviewed; 895 AA.
AC Q9SCZ4; A7U523; Q0WM33; Q94C93; Q9M4G2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Receptor-like protein kinase FERONIA;
DE EC=2.7.11.1;
DE AltName: Full=Protein SIRENE;
DE Flags: Precursor;
GN Name=FER; Synonyms=AAK1, SIR, SRN; OrderedLocusNames=At3g51550;
GN ORFNames=F26O13.190;
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], FUNCTION, MUTAGENESIS OF LYS-565,
RP AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17673660; DOI=10.1126/science.1143562;
RA Escobar-Restrepo J.-M., Huck N., Kessler S., Gagliardini V.,
RA Gheyselinck J., Yang W.-C., Grossniklaus U.;
RT "The FERONIA receptor-like kinase mediates male-female interactions during
RT pollen tube reception.";
RL Science 317:656-660(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 [MRNA] OF 427-895.
RA Desbrosses-Fonrouge A.G.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-895.
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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=12620194; DOI=10.1016/s0960-9822(03)00093-9;
RA Rotman N., Rozier F., Boavida L., Dumas C., Berger F., Faure J.-E.;
RT "Female control of male gamete delivery during fertilization in Arabidopsis
RT thaliana.";
RL Curr. Biol. 13:432-436(2003).
RN [8]
RP IDENTIFICATION.
RX PubMed=12668629; DOI=10.1242/dev.00458;
RA Huck N., Moore J.M., Federer M., Grossniklaus U.;
RT "The Arabidopsis mutant feronia disrupts the female gametophytic control of
RT pollen tube reception.";
RL Development 130:2149-2159(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [11]
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 [12]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY BRASSINOSTEROIDS.
RX PubMed=19383785; DOI=10.1073/pnas.0812346106;
RA Guo H., Li L., Ye H., Yu X., Algreen A., Yin Y.;
RT "Three related receptor-like kinases are required for optimal cell
RT elongation in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7648-7653(2009).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20400488; DOI=10.1093/mp/ssq015;
RA Deslauriers S.D., Larsen P.B.;
RT "FERONIA is a key modulator of brassinosteroid and ethylene responsiveness
RT in Arabidopsis hypocotyls.";
RL Mol. Plant 3:626-640(2010).
RN [15]
RP FUNCTION, AND INTERACTION WITH ROPGEF1.
RX PubMed=20876100; DOI=10.1073/pnas.1005366107;
RA Duan Q., Kita D., Li C., Cheung A.Y., Wu H.M.;
RT "FERONIA receptor-like kinase regulates RHO GTPase signaling of root hair
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17821-17826(2010).
RN [16]
RP FUNCTION IN POWDERY MILDEW INFECTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=21071669; DOI=10.1126/science.1195211;
RA Kessler S.A., Shimosato-Asano H., Keinath N.F., Wuest S.E., Ingram G.,
RA Panstruga R., Grossniklaus U.;
RT "Conserved molecular components for pollen tube reception and fungal
RT invasion.";
RL Science 330:968-971(2010).
RN [17]
RP REVIEW.
RX PubMed=21963060; DOI=10.1016/j.pbi.2011.09.001;
RA Cheung A.Y., Wu H.M.;
RT "THESEUS 1, FERONIA and relatives: a family of cell wall-sensing receptor
RT kinases?";
RL Curr. Opin. Plant Biol. 14:632-641(2011).
RN [18]
RP AUTOPHOSPHORYLATION [LARGE SCALE ANALYSIS].
RX PubMed=21477822; DOI=10.1016/j.phytochem.2011.02.029;
RA Nemoto K., Seto T., Takahashi H., Nozawa A., Seki M., Shinozaki K.,
RA Endo Y., Sawasaki T.;
RT "Autophosphorylation profiling of Arabidopsis protein kinases using the
RT cell-free system.";
RL Phytochemistry 72:1136-1144(2011).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22908257; DOI=10.1073/pnas.1212547109;
RA Yu F., Qian L., Nibau C., Duan Q., Kita D., Levasseur K., Li X., Lu C.,
RA Li H., Hou C., Li L., Buchanan B.B., Chen L., Cheung A.Y., Li D., Luan S.;
RT "FERONIA receptor kinase pathway suppresses abscisic acid signaling in
RT Arabidopsis by activating ABI2 phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14693-14698(2012).
RN [20]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RALF1, IDENTIFICATION BY
RP MASS SPECTROMETRY, PHOSPHORYLATION AT SER-858; SER-871 AND SER-874, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24458638; DOI=10.1126/science.1244454;
RA Haruta M., Sabat G., Stecker K., Minkoff B.B., Sussman M.R.;
RT "A peptide hormone and its receptor protein kinase regulate plant cell
RT expansion.";
RL Science 343:408-411(2014).
RN [21]
RP INTERACTION WITH LRE AND LLG1.
RX PubMed=26052747; DOI=10.7554/elife.06587;
RA Li C., Yeh F.L., Cheung A.Y., Duan Q., Kita D., Liu M.C., Maman J.,
RA Luu E.J., Wu B.W., Gates L., Jalal M., Kwong A., Carpenter H., Wu H.M.;
RT "Glycosylphosphatidylinositol-anchored proteins as chaperones and co-
RT receptors for FERONIA receptor kinase signaling in Arabidopsis.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Receptor-like protein kinase that mediates the female control
CC of male gamete delivery during fertilization, including growth
CC cessation of compatible pollen tubes ensuring a reproductive isolation
CC barriers, by regulating MLO7 subcellular polarization upon pollen tube
CC perception in the female gametophyte synergids. Required for cell
CC elongation during vegetative growth, mostly in a
CC brassinosteroids- (BR-) independent manner. Acts as an upstream
CC regulator for the Rac/Rop-signaling pathway that controls ROS-mediated
CC root hair development. Seems to regulate a cross-talk between
CC brassinosteroids and ethylene signaling pathways during hypocotyl
CC elongation. Negative regulator of brassinosteroid response in light-
CC grown hypocotyls, but required for brassinosteroid response in
CC etiolated seedlings. Mediates sensitivity to powdery mildew (e.g.
CC Golovinomyces orontii). Positive regulator of auxin-promoted growth
CC that represses the abscisic acid (ABA) signaling via the activation of
CC ABI2 phosphatase. Required for RALF1-mediated extracellular
CC alkalinization in a signaling pathway preventing cell expansion.
CC {ECO:0000269|PubMed:17673660, ECO:0000269|PubMed:19383785,
CC ECO:0000269|PubMed:20400488, ECO:0000269|PubMed:20876100,
CC ECO:0000269|PubMed:21071669, ECO:0000269|PubMed:22908257,
CC ECO:0000269|PubMed:24458638}.
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 ROPGEF1 (PubMed:20876100). Interacts with
CC RALF1; triggering phosphorylation status and subsequent activation
CC (PubMed:24458638). Interacts with LRE and LLG1 (PubMed:26052747).
CC {ECO:0000269|PubMed:20876100, ECO:0000269|PubMed:24458638,
CC ECO:0000269|PubMed:26052747}.
CC -!- INTERACTION:
CC Q9SCZ4; Q38919: ARAC4; NbExp=2; IntAct=EBI-15880405, EBI-1548187;
CC Q9SCZ4; Q9FN92: At5g59700; NbExp=3; IntAct=EBI-15880405, EBI-17071988;
CC Q9SCZ4; Q9LX66: HERK1; NbExp=5; IntAct=EBI-15880405, EBI-22028097;
CC Q9SCZ4; Q9SRY3: RALF1; NbExp=3; IntAct=EBI-15880405, EBI-16091545;
CC Q9SCZ4; Q93ZY2: ROPGEF1; NbExp=4; IntAct=EBI-15880405, EBI-4425188;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17673660,
CC ECO:0000269|PubMed:21071669, ECO:0000269|PubMed:24458638,
CC ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:17673660, ECO:0000269|PubMed:21071669,
CC ECO:0000269|PubMed:24458638, ECO:0000305|PubMed:17644812}.
CC Note=Accumulates asymmetrically in the female gametophyte synergid
CC membrane at the filiform apparatus.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, buds, flowers, siliques, young
CC ovules primordia, and young anthers with immature pollen, but not
CC detected in mature pollen. Highest expression in the synergid cells of
CC the female gametophyte. {ECO:0000269|PubMed:17673660,
CC ECO:0000269|PubMed:19383785}.
CC -!- DEVELOPMENTAL STAGE: Detected in floral apices, young ovule primordia,
CC and young anthers with immature pollen, but not in older anthers with
CC mature pollen. After fertilization, expressed in globular embryos.
CC {ECO:0000269|PubMed:17673660}.
CC -!- INDUCTION: By brassinosteroids (BR). {ECO:0000269|PubMed:19383785}.
CC -!- PTM: Autophosphorylated.
CC -!- PTM: Phosphorylated at Ser-858, Ser-871 and Ser-874 upon activation by
CC RALF1. {ECO:0000269|PubMed:24458638}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to impaired
CC fertilization. The pollen tube fails to arrest and continues to grow
CC inside the female gametophyte. Disturbed MLO7 relocalization to the
CC filiform apparatus upon pollen tube arrival at the micropyle. Severe
CC cell elongation defect in RNAi mutants with decreased FER expression.
CC In fer-2 seedlings, altered responsiveness to brassinosteroids but
CC increased ethylene response during the regulation of hypocotyl
CC elongation. Increased resistance to powdery mildew (e.g. Golovinomyces
CC orontii). Abscisic acid- (ABA)- hypersensitive response. Longer roots.
CC Insensitivity to RALF1-mediated root-growth inbibition but
CC hypersensitive to cation lithium inhibition.
CC {ECO:0000269|PubMed:12620194, ECO:0000269|PubMed:20400488,
CC ECO:0000269|PubMed:21071669, ECO:0000269|PubMed:22908257,
CC ECO:0000269|PubMed:24458638}.
CC -!- MISCELLANEOUS: Female paralog of ANXUR, a male factor expressed in
CC pollen tube that controls release of the sperm cell.
CC -!- MISCELLANEOUS: Named after the Etruscan goddess of fertility Feronia.
CC -!- MISCELLANEOUS: 'Sirene' means siren in French.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB92960.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; EF681137; ABT18100.1; -; Genomic_DNA.
DR EMBL; AL133452; CAB63019.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78805.1; -; Genomic_DNA.
DR EMBL; AY035053; AAK59558.1; -; mRNA.
DR EMBL; AJ242671; CAB92960.1; ALT_SEQ; mRNA.
DR EMBL; AK230000; BAF01824.1; -; mRNA.
DR PIR; T45786; T45786.
DR RefSeq; NP_190723.1; NM_115014.5.
DR PDB; 6A5B; X-ray; 2.21 A; A=21-450.
DR PDB; 6A5E; X-ray; 2.77 A; A/B=28-423.
DR PDBsum; 6A5B; -.
DR PDBsum; 6A5E; -.
DR AlphaFoldDB; Q9SCZ4; -.
DR SMR; Q9SCZ4; -.
DR BioGRID; 9636; 10.
DR DIP; DIP-59394N; -.
DR IntAct; Q9SCZ4; 9.
DR STRING; 3702.AT3G51550.1; -.
DR iPTMnet; Q9SCZ4; -.
DR SwissPalm; Q9SCZ4; -.
DR PaxDb; Q9SCZ4; -.
DR PRIDE; Q9SCZ4; -.
DR ProteomicsDB; 230948; -.
DR EnsemblPlants; AT3G51550.1; AT3G51550.1; AT3G51550.
DR GeneID; 824318; -.
DR Gramene; AT3G51550.1; AT3G51550.1; AT3G51550.
DR KEGG; ath:AT3G51550; -.
DR Araport; AT3G51550; -.
DR TAIR; locus:2081895; AT3G51550.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_5_1; -.
DR InParanoid; Q9SCZ4; -.
DR OMA; KFEYPPG; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SCZ4; -.
DR PRO; PR:Q9SCZ4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCZ4; baseline and differential.
DR Genevisible; Q9SCZ4; AT.
DR GO; GO:0043680; C:filiform apparatus; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0010483; P:pollen tube reception; IMP:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0009741; P:response to brassinosteroid; IMP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0010118; P:stomatal movement; IGI:TAIR.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
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 PANTHER; PTHR27003; PTHR27003; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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 3D-structure; Abscisic acid signaling pathway; ATP-binding;
KW Brassinosteroid signaling pathway; Cell membrane; Developmental protein;
KW Ethylene signaling pathway; Fertilization; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..895
FT /note="Receptor-like protein kinase FERONIA"
FT /id="PRO_0000386556"
FT TOPO_DOM 28..447
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 536..810
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 844..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 661
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 542..550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24458638"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24458638"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24458638"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 565
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:17673660"
FT CONFLICT 7
FT /note="R -> Q (in Ref. 1; ABT18100)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..18
FT /note="Missing (in Ref. 1; ABT18100)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="A -> S (in Ref. 1; ABT18100)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="G -> V (in Ref. 4; AAK59558)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="M -> V (in Ref. 6; BAF01824)"
FT /evidence="ECO:0000305"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6A5B"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6A5E"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:6A5B"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 377..388
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:6A5B"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6A5E"
SQ SEQUENCE 895 AA; 98150 MW; CFAEFE8E5146BC26 CRC64;
MKITEGRFRL SLLLLLLLIS AATLISAADY SPTEKILLNC GGGASNLTDT DNRIWISDVK
SKFLSSSSED SKTSPALTQD PSVPEVPYMT ARVFRSPFTY TFPVASGRKF VRLYFYPNSY
DGLNATNSLF SVSFGPYTLL KNFSASQTAE ALTYAFIIKE FVVNVEGGTL NMTFTPESAP
SNAYAFVNGI EVTSMPDMYS STDGTLTMVG SSGSVTIDNS TALENVYRLN VGGNDISPSA
DTGLYRSWYD DQPYIFGAGL GIPETADPNM TIKYPTGTPT YVAPVDVYST ARSMGPTAQI
NLNYNLTWIF SIDSGFTYLV RLHFCEVSSN ITKINQRVFT IYLNNQTAEP EADVIAWTSS
NGVPFHKDYV VNPPEGNGQQ DLWLALHPNP VNKPEYYDSL LNGVEIFKMN TSDGNLAGTN
PIPGPQVTAD PSKVLRPTTR KSKSNTAIIA GAASGAVVLA LIIGFCVFGA YRRRKRGDYQ
PASDATSGWL PLSLYGNSHS AGSAKTNTTG SYASSLPSNL CRHFSFAEIK AATKNFDESR
VLGVGGFGKV YRGEIDGGTT KVAIKRGNPM SEQGVHEFQT EIEMLSKLRH RHLVSLIGYC
EENCEMILVY DYMAHGTMRE HLYKTQNPSL PWKQRLEICI GAARGLHYLH TGAKHTIIHR
DVKTTNILLD EKWVAKVSDF GLSKTGPTLD HTHVSTVVKG SFGYLDPEYF RRQQLTEKSD
VYSFGVVLFE ALCARPALNP TLAKEQVSLA EWAPYCYKKG MLDQIVDPYL KGKITPECFK
KFAETAMKCV LDQGIERPSM GDVLWNLEFA LQLQESAEEN GKGVCGDMDM DEIKYDDGNC
KGKNDKSSDV YEGNVTDSRS SGIDMSIGGR SLASEDSDGL TPSAVFSQIM NPKGR
