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Receptor-like protein kinase FERONIA (EC 2.7.11.1) (Protein SIRENE)

 FERON_ARATH             Reviewed;         895 AA.
Q9SCZ4; A7U523; Q0WM33; Q94C93; Q9M4G2;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Receptor-like protein kinase FERONIA;
EC=2.7.11.1;
AltName: Full=Protein SIRENE;
Flags: Precursor;
Name=FER; Synonyms=AAK1, SIR, SRN; OrderedLocusNames=At3g51550;
ORFNames=F26O13.190;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF LYS-565,
AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
SUBCELLULAR LOCATION.
STRAIN=cv. Landsberg erecta;
PubMed=17673660; DOI=10.1126/science.1143562;
Escobar-Restrepo J.-M., Huck N., Kessler S., Gagliardini V.,
Gheyselinck J., Yang W.-C., Grossniklaus U.;
"The FERONIA receptor-like kinase mediates male-female interactions
during pollen tube reception.";
Science 317:656-660(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 427-895.
Desbrosses-Fonrouge A.G.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-895.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
DISRUPTION PHENOTYPE.
PubMed=12620194; DOI=10.1016/S0960-9822(03)00093-9;
Rotman N., Rozier F., Boavida L., Dumas C., Berger F., Faure J.-E.;
"Female control of male gamete delivery during fertilization in
Arabidopsis thaliana.";
Curr. Biol. 13:432-436(2003).
[8]
IDENTIFICATION.
PubMed=12668629; DOI=10.1242/dev.00458;
Huck N., Moore J.M., Federer M., Grossniklaus U.;
"The Arabidopsis mutant feronia disrupts the female gametophytic
control of pollen tube reception.";
Development 130:2149-2159(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15308754; DOI=10.1105/tpc.104.023150;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new
phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16618929; DOI=10.1073/pnas.0506958103;
Dunkley T.P.J., Hester S., Shadforth I.P., Runions J., Weimar T.,
Hanton S.L., Griffin J.L., Bessant C., Brandizzi F., Hawes C.,
Watson R.B., Dupree P., Lilley K.S.;
"Mapping the Arabidopsis organelle proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:6518-6523(2006).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=17644812; DOI=10.1074/mcp.M700099-MCP200;
Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
Barbier-Brygoo H., Ephritikhine G.;
"A high content in lipid-modified peripheral proteins and integral
receptor kinases features in the arabidopsis plasma membrane
proteome.";
Mol. Cell. Proteomics 6:1980-1996(2007).
[13]
GENE FAMILY.
PubMed=19529822; DOI=10.1093/mp/ssn083;
Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
"Diverse transcriptional programs associated with environmental stress
and hormones in the Arabidopsis receptor-like kinase gene family.";
Mol. Plant 2:84-107(2009).
[14]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY BRASSINOSTEROIDS.
PubMed=19383785; DOI=10.1073/pnas.0812346106;
Guo H., Li L., Ye H., Yu X., Algreen A., Yin Y.;
"Three related receptor-like kinases are required for optimal cell
elongation in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 106:7648-7653(2009).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=20400488; DOI=10.1093/mp/ssq015;
Deslauriers S.D., Larsen P.B.;
"FERONIA is a key modulator of brassinosteroid and ethylene
responsiveness in Arabidopsis hypocotyls.";
Mol. Plant 3:626-640(2010).
[16]
FUNCTION, AND INTERACTION WITH ROPGEF1.
PubMed=20876100; DOI=10.1073/pnas.1005366107;
Duan Q., Kita D., Li C., Cheung A.Y., Wu H.M.;
"FERONIA receptor-like kinase regulates RHO GTPase signaling of root
hair development.";
Proc. Natl. Acad. Sci. U.S.A. 107:17821-17826(2010).
[17]
FUNCTION IN POWDERY MILDEW INFECTION, DISRUPTION PHENOTYPE, AND
SUBCELLULAR LOCATION.
STRAIN=cv. Landsberg erecta;
PubMed=21071669; DOI=10.1126/science.1195211;
Kessler S.A., Shimosato-Asano H., Keinath N.F., Wuest S.E., Ingram G.,
Panstruga R., Grossniklaus U.;
"Conserved molecular components for pollen tube reception and fungal
invasion.";
Science 330:968-971(2010).
[18]
REVIEW.
PubMed=21963060; DOI=10.1016/j.pbi.2011.09.001;
Cheung A.Y., Wu H.M.;
"THESEUS 1, FERONIA and relatives: a family of cell wall-sensing
receptor kinases?";
Curr. Opin. Plant Biol. 14:632-641(2011).
[19]
AUTOPHOSPHORYLATION [LARGE SCALE ANALYSIS].
PubMed=21477822; DOI=10.1016/j.phytochem.2011.02.029;
Nemoto K., Seto T., Takahashi H., Nozawa A., Seki M., Shinozaki K.,
Endo Y., Sawasaki T.;
"Autophosphorylation profiling of Arabidopsis protein kinases using
the cell-free system.";
Phytochemistry 72:1136-1144(2011).
[20]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22908257; DOI=10.1073/pnas.1212547109;
Yu F., Qian L., Nibau C., Duan Q., Kita D., Levasseur K., Li X.,
Lu C., Li H., Hou C., Li L., Buchanan B.B., Chen L., Cheung A.Y.,
Li D., Luan S.;
"FERONIA receptor kinase pathway suppresses abscisic acid signaling in
Arabidopsis by activating ABI2 phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 109:14693-14698(2012).
[21]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RALF1, IDENTIFICATION
BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-858; SER-871 AND SER-874,
AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=24458638; DOI=10.1126/science.1244454;
Haruta M., Sabat G., Stecker K., Minkoff B.B., Sussman M.R.;
"A peptide hormone and its receptor protein kinase regulate plant cell
expansion.";
Science 343:408-411(2014).
[22]
INTERACTION WITH LRE AND LLG1.
PubMed=26052747; DOI=10.7554/eLife.06587;
Li C., Yeh F.L., Cheung A.Y., Duan Q., Kita D., Liu M.C., Maman J.,
Luu E.J., Wu B.W., Gates L., Jalal M., Kwong A., Carpenter H.,
Wu H.M.;
"Glycosylphosphatidylinositol-anchored proteins as chaperones and co-
receptors for FERONIA receptor kinase signaling in Arabidopsis.";
Elife 4:0-0(2015).
-!- FUNCTION: Receptor-like protein kinase that mediates the female
control of male gamete delivery during fertilization, including
growth cessation of compatible pollen tubes ensuring a
reproductive isolation barriers, by regulating MLO7 subcellular
polarization upon pollen tube perception in the female gametophyte
synergids. Required for cell elongation during vegetative growth,
mostly in a brassinosteroids- (BR-) independent manner. Acts as an
upstream regulator for the Rac/Rop-signaling pathway that controls
ROS-mediated root hair development. Seems to regulate a cross-talk
between brassinosteroids and ethylene signaling pathways during
hypocotyl elongation. Negative regulator of brassinosteroid
response in light-grown hypocotyls, but required for
brassinosteroid response in etiolated seedlings. Mediates
sensitivity to powdery mildew (e.g. Golovinomyces orontii).
Positive regulator of auxin-promoted growth that represses the
abscisic acid (ABA) signaling via the activation of ABI2
phosphatase. Required for RALF1-mediated extracellular
alkalinization in a signaling pathway preventing cell expansion.
{ECO:0000269|PubMed:17673660, ECO:0000269|PubMed:19383785,
ECO:0000269|PubMed:20400488, ECO:0000269|PubMed:20876100,
ECO:0000269|PubMed:21071669, ECO:0000269|PubMed:22908257,
ECO:0000269|PubMed:24458638}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with ROPGEF1 (PubMed:20876100). Interacts with
RALF1; triggering phosphorylation status and subsequent activation
(PubMed:24458638). Interacts with LRE and LLG1 (PubMed:26052747).
{ECO:0000269|PubMed:20876100, ECO:0000269|PubMed:24458638,
ECO:0000269|PubMed:26052747}.
-!- INTERACTION:
Q38919:ARAC4; NbExp=2; IntAct=EBI-15880405, EBI-1548187;
Q9SRY3:RALF1; NbExp=3; IntAct=EBI-15880405, EBI-16091545;
Q93ZY2:ROPGEF1; NbExp=4; IntAct=EBI-15880405, EBI-4425188;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16618929,
ECO:0000269|PubMed:17644812, ECO:0000269|PubMed:17673660,
ECO:0000269|PubMed:21071669, ECO:0000269|PubMed:24458638}; Single-
pass type I membrane protein {ECO:0000269|PubMed:16618929,
ECO:0000269|PubMed:17644812, ECO:0000269|PubMed:17673660,
ECO:0000269|PubMed:21071669, ECO:0000269|PubMed:24458638}.
Note=Accumulates asymmetrically in the female gametophyte synergid
membrane at the filiform apparatus.
-!- TISSUE SPECIFICITY: Expressed in leaves, buds, flowers, siliques,
young ovules primordia, and young anthers with immature pollen,
but not detected in mature pollen. Highest expression in the
synergid cells of the female gametophyte.
{ECO:0000269|PubMed:17673660, ECO:0000269|PubMed:19383785}.
-!- DEVELOPMENTAL STAGE: Detected in floral apices, young ovule
primordia, and young anthers with immature pollen, but not in
older anthers with mature pollen. After fertilization, expressed
in globular embryos. {ECO:0000269|PubMed:17673660}.
-!- INDUCTION: By brassinosteroids (BR).
{ECO:0000269|PubMed:19383785}.
-!- PTM: Autophosphorylated.
-!- PTM: Phosphorylated at Ser-858, Ser-871 and Ser-874 upon
activation by RALF1. {ECO:0000269|PubMed:24458638}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality due to impaired
fertilization. The pollen tube fails to arrest and continues to
grow inside the female gametophyte. Disturbed MLO7 relocalization
to the filiform apparatus upon pollen tube arrival at the
micropyle. Severe cell elongation defect in RNAi mutants with
decreased FER expression. In fer-2 seedlings, altered
responsiveness to brassinosteroids but increased ethylene response
during the regulation of hypocotyl elongation. Increased
resistance to powdery mildew (e.g. Golovinomyces orontii).
Abscisic acid- (ABA)- hypersensitive response. Longer roots.
Insensitivity to RALF1-mediated root-growth inbibition but
hypersensitive to cation lithium inhibition.
{ECO:0000269|PubMed:12620194, ECO:0000269|PubMed:20400488,
ECO:0000269|PubMed:21071669, ECO:0000269|PubMed:22908257,
ECO:0000269|PubMed:24458638}.
-!- MISCELLANEOUS: Female paralog of ANXUR, a male factor expressed in
pollen tube that controls release of the sperm cell.
-!- MISCELLANEOUS: Named after the Etruscan goddess of fertility
Feronia.
-!- MISCELLANEOUS: 'Sirene' means siren in French.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAB92960.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
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EMBL; EF681137; ABT18100.1; -; Genomic_DNA.
EMBL; AL133452; CAB63019.1; -; Genomic_DNA.
EMBL; CP002686; AEE78805.1; -; Genomic_DNA.
EMBL; AY035053; AAK59558.1; -; mRNA.
EMBL; AJ242671; CAB92960.1; ALT_SEQ; mRNA.
EMBL; AK230000; BAF01824.1; -; mRNA.
PIR; T45786; T45786.
RefSeq; NP_190723.1; NM_115014.5.
UniGene; At.656; -.
ProteinModelPortal; Q9SCZ4; -.
BioGrid; 9636; 7.
DIP; DIP-59394N; -.
IntAct; Q9SCZ4; 7.
STRING; 3702.AT3G51550.1; -.
iPTMnet; Q9SCZ4; -.
SwissPalm; Q9SCZ4; -.
PaxDb; Q9SCZ4; -.
EnsemblPlants; AT3G51550.1; AT3G51550.1; AT3G51550.
GeneID; 824318; -.
Gramene; AT3G51550.1; AT3G51550.1; AT3G51550.
KEGG; ath:AT3G51550; -.
Araport; AT3G51550; -.
TAIR; locus:2081895; AT3G51550.
eggNOG; KOG1187; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000238317; -.
InParanoid; Q9SCZ4; -.
OMA; DDGNCKG; -.
OrthoDB; EOG093601SG; -.
PhylomeDB; Q9SCZ4; -.
PRO; PR:Q9SCZ4; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q9SCZ4; AT.
GO; GO:0043680; C:filiform apparatus; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:0010483; P:pollen tube reception; IMP:TAIR.
GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
GO; GO:0009741; P:response to brassinosteroid; IMP:UniProtKB.
GO; GO:0009723; P:response to ethylene; IMP:UniProtKB.
GO; GO:0048364; P:root development; IMP:UniProtKB.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR024788; Malectin-like_Carb-bd_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12819; Malectin_like; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Abscisic acid signaling pathway; ATP-binding;
Brassinosteroid signaling pathway; Cell membrane; Complete proteome;
Developmental protein; Ethylene signaling pathway; Fertilization;
Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 895 Receptor-like protein kinase FERONIA.
/FTId=PRO_0000386556.
TOPO_DOM 28 447 Extracellular. {ECO:0000255}.
TRANSMEM 448 468 Helical. {ECO:0000255}.
TOPO_DOM 469 895 Cytoplasmic. {ECO:0000255}.
DOMAIN 536 810 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 542 550 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 661 661 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 565 565 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 858 858 Phosphoserine.
{ECO:0000269|PubMed:24458638}.
MOD_RES 866 866 Phosphoserine.
{ECO:0000244|PubMed:14506206}.
MOD_RES 871 871 Phosphoserine.
{ECO:0000269|PubMed:24458638}.
MOD_RES 874 874 Phosphoserine.
{ECO:0000269|PubMed:24458638}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 565 565 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:17673660}.
CONFLICT 7 7 R -> Q (in Ref. 1; ABT18100).
{ECO:0000305}.
CONFLICT 17 18 Missing (in Ref. 1; ABT18100).
{ECO:0000305}.
CONFLICT 179 179 A -> S (in Ref. 1; ABT18100).
{ECO:0000305}.
CONFLICT 546 546 G -> V (in Ref. 4; AAK59558).
{ECO:0000305}.
CONFLICT 761 761 M -> V (in Ref. 6; BAF01824).
{ECO:0000305}.
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


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