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Receptor kinase-like protein Xa21 (EC 2.7.11.1) [Cleaved into: Receptor kinase-like protein Xa21, processed]

 XA21_ORYSI              Reviewed;        1025 AA.
Q1MX30;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 1.
23-MAY-2018, entry version 94.
RecName: Full=Receptor kinase-like protein Xa21 {ECO:0000303|Ref.1};
EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:11927577};
Contains:
RecName: Full=Receptor kinase-like protein Xa21, processed {ECO:0000250|UniProtKB:Q2R2D5};
Flags: Precursor;
Name=XA21 {ECO:0000303|Ref.1};
Oryza sativa subsp. indica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39946 {ECO:0000312|EMBL:BAE93934.1};
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Xue Q., Xu J.;
"Xa21 gene with bacterial blight resistance from wild rice (Oryza.
longistaminata) to hybrid rice(Oryza.sativa).";
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION.
STRAIN=cv. IRBB21;
PubMed=8525370; DOI=10.1126/science.270.5243.1804;
Song W.-Y., Wang G.-L., Chen L.-L., Kim H.-S., Pi L.-Y., Holsten T.,
Gardner J., Wang B., Zhai W.-X., Zhu L.-H., Fauquet C., Ronald P.;
"A receptor kinase-like protein encoded by the rice disease resistance
gene, Xa21.";
Science 270:1804-1806(1995).
[3]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
AUTOPHOSPHORYLATION, COFACTOR, AND MUTAGENESIS OF LYS-736.
PubMed=11927577; DOI=10.1074/jbc.M110999200;
Liu G.-Z., Pi L.-Y., Walker J.C., Ronald P.C., Song W.-Y.;
"Biochemical characterization of the kinase domain of the rice disease
resistance receptor-like kinase XA21.";
J. Biol. Chem. 277:20264-20269(2002).
[4]
MUTAGENESIS OF 686-SER--SER-689 AND LYS-736, AUTOPHOSPHORYLATION, AND
PHOSPHORYLATION AT SER-686; THR-688 AND SER-689.
PubMed=16460508; DOI=10.1111/j.1365-313X.2005.02638.x;
Xu W.H., Wang Y.S., Liu G.Z., Chen X., Tinjuangjun P., Pi L.Y.,
Song W.Y.;
"The autophosphorylated Ser686, Thr688, and Ser689 residues in the
intracellular juxtamembrane domain of XA21 are implicated in stability
control of rice receptor-like kinase.";
Plant J. 45:740-751(2006).
[5]
FUNCTION, INTERACTION WITH WRKY62, AND MUTAGENESIS OF LYS-736.
PubMed=19825552; DOI=10.1093/mp/ssn024;
Peng Y., Bartley L.E., Chen X., Dardick C., Chern M., Ruan R.,
Canlas P.E., Ronald P.C.;
"OsWRKY62 is a negative regulator of basal and Xa21-mediated defense
against Xanthomonas oryzae pv. oryzae in rice.";
Mol. Plant 1:446-458(2008).
[6]
FUNCTION, PHOSPHORYLATION AT THR-705, MUTAGENESIS OF THR-680;
686-SER--SER-689; SER-697; SER-699; THR-705 AND LYS-736,
AUTOPHOSPHORYLATION, AND INTERACTION WITH WRKY62; XB3; XB15 AND XB24.
PubMed=20118235; DOI=10.1074/jbc.M109.093427;
Chen X., Chern M., Canlas P.E., Jiang C., Ruan D., Cao P.,
Ronald P.C.;
"A conserved threonine residue in the juxtamembrane domain of the XA21
pattern recognition receptor is critical for kinase
autophosphorylation and XA21-mediated immunity.";
J. Biol. Chem. 285:10454-10463(2010).
-!- FUNCTION: Receptor kinase-like protein Xa21: Receptor kinase that
detects X.oryzae pv. oryzae protein Ax21 to promote innate
immunity (PubMed:20118235). Following X.oryzae pv. oryzae protein
Ax21 detection, undergoes cleavage, releasing the processed
protein kinase Xa21 chain (By similarity).
{ECO:0000250|UniProtKB:Q2R2D5, ECO:0000269|PubMed:20118235}.
-!- FUNCTION: Receptor kinase-like protein Xa21, processed: The
processed protein kinase Xa21 chain released by protein cleavage
after X.oryzae pv. oryzae protein Ax21 detection translocates into
the nucleus where it can bind and regulate WRKY62, a transcription
factor (By similarity). Confers resistance to the bacterial
pathogen X.oryzae pv. oryzae (Xoo) (PubMed:8525370,
PubMed:19825552, PubMed:20118235). {ECO:0000250|UniProtKB:Q2R2D5,
ECO:0000269|PubMed:19825552, ECO:0000269|PubMed:20118235,
ECO:0000269|PubMed:8525370}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11927577}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11927577};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11927577};
Note=Enzymatic activity is fifteen time stronger with Mn(2+) than
with Mg(2+). {ECO:0000269|PubMed:11927577};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.3 uM for ATP {ECO:0000269|PubMed:11927577};
Vmax=8.4 nmol/min/mg enzyme with ATP as substrate
{ECO:0000269|PubMed:11927577};
-!- SUBUNIT: Binds to XB3, XB15 and XB24 (PubMed:20118235). Receptor
kinase-like protein Xa21, processed: Interacts with WRKY62/XB10 in
the nucleus (PubMed:19825552, PubMed:20118235).
{ECO:0000269|PubMed:19825552, ECO:0000269|PubMed:20118235}.
-!- SUBCELLULAR LOCATION: Receptor kinase-like protein Xa21: Cell
membrane {ECO:0000250|UniProtKB:Q2R2D5}; Single-pass membrane
protein {ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q2R2D5}; Single-pass membrane protein
{ECO:0000255}. Note=Present in cortical and perinuclear
endoplasmic reticulum. Cleaved upon X.oryzae pv. oryzae protein
Ax21 recognition; the kinase containing fragment is translocated
into the nucleus. {ECO:0000250|UniProtKB:Q2R2D5}.
-!- SUBCELLULAR LOCATION: Receptor kinase-like protein Xa21,
processed: Nucleus {ECO:0000250|UniProtKB:Q2R2D5}.
-!- PTM: Undergoes protein cleavage upon X.oryzae pv. oryzae protein
Ax21 detection, thus releasing the processed protein kinase Xa21
chain. {ECO:0000250|UniProtKB:Q2R2D5}.
-!- PTM: Autophosphorylated on serine and threonine residues; these
phosphorylation prevents proteolytic degradation.
{ECO:0000269|PubMed:11927577, ECO:0000269|PubMed:16460508,
ECO:0000269|PubMed:20118235}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AB212798; BAE93933.1; -; Genomic_DNA.
EMBL; AB212799; BAE93934.1; -; Genomic_DNA.
ProteinModelPortal; Q1MX30; -.
SMR; Q1MX30; -.
iPTMnet; Q1MX30; -.
ExpressionAtlas; Q1MX30; differential.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0031349; P:positive regulation of defense response; IMP:UniProtKB.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR013210; LRR_N_plant-typ.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00560; LRR_1; 1.
Pfam; PF13855; LRR_8; 3.
Pfam; PF08263; LRRNT_2; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 12.
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;
ATP-binding; Cell membrane; Endoplasmic reticulum; Glycoprotein;
Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Plant defense; Receptor; Repeat;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 1025 Receptor kinase-like protein Xa21.
/FTId=PRO_5005930761.
CHAIN ? 1025 Receptor kinase-like protein Xa21,
processed.
/FTId=PRO_0000436963.
TOPO_DOM 24 653 Extracellular. {ECO:0000305}.
TRANSMEM 654 674 Helical. {ECO:0000255}.
TOPO_DOM 675 1025 Cytoplasmic. {ECO:0000305}.
REPEAT 78 101 LRR 1. {ECO:0000255}.
REPEAT 102 126 LRR 2. {ECO:0000255}.
REPEAT 127 150 LRR 3. {ECO:0000255}.
REPEAT 152 174 LRR 4. {ECO:0000255}.
REPEAT 176 199 LRR 5. {ECO:0000255}.
REPEAT 200 223 LRR 6. {ECO:0000255}.
REPEAT 224 247 LRR 7. {ECO:0000255}.
REPEAT 248 271 LRR 8. {ECO:0000255}.
REPEAT 273 296 LRR 9. {ECO:0000255}.
REPEAT 298 319 LRR 10. {ECO:0000255}.
REPEAT 320 343 LRR 11. {ECO:0000255}.
REPEAT 350 373 LRR 12. {ECO:0000255}.
REPEAT 375 399 LRR 13. {ECO:0000255}.
REPEAT 400 423 LRR 14. {ECO:0000255}.
REPEAT 425 447 LRR 15. {ECO:0000255}.
REPEAT 448 470 LRR 16. {ECO:0000255}.
REPEAT 471 495 LRR 17. {ECO:0000255}.
REPEAT 497 520 LRR 18. {ECO:0000255}.
REPEAT 521 544 LRR 19. {ECO:0000255}.
REPEAT 545 568 LRR 20. {ECO:0000255}.
REPEAT 569 592 LRR 21. {ECO:0000255}.
REPEAT 594 617 LRR 22. {ECO:0000255}.
DOMAIN 708 979 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 714 722 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 842 842 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 736 736 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 686 686 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16460508}.
MOD_RES 688 688 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16460508}.
MOD_RES 689 689 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16460508}.
MOD_RES 705 705 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:20118235}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 373 373 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 470 470 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 483 483 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 503 503 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 599 599 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 680 680 T->A: Increased autophosphorylation.
{ECO:0000269|PubMed:20118235}.
MUTAGEN 686 689 SRTS->ARAA: Normal autophosphorylation
but reduced stability leading to
increased proteolytic cleavage and
compromised resistance to X.oryzae pv.
oryzae (Xoo).
{ECO:0000269|PubMed:16460508,
ECO:0000269|PubMed:20118235}.
MUTAGEN 697 697 S->A,D: Slight reduction in
autophosphorylation.
{ECO:0000269|PubMed:20118235}.
MUTAGEN 699 699 S->A: Increased autophosphorylation.
{ECO:0000269|PubMed:20118235}.
MUTAGEN 705 705 T->A,E: Abolished autophosphorylation and
loss of interactions with target proteins
(e.g. WRKY62/XB10, XB3, XB15 and XB24).
Loss of positive impact on innate
immunity toward X.oryzae pv. oryzae
(Xoo). {ECO:0000269|PubMed:20118235}.
MUTAGEN 736 736 K->E: Kinase-deficient mutant lacking
autophosphorylation, impaired interaction
with WRKY62. Reduced stability leading to
increased proteolytic cleavage.
{ECO:0000269|PubMed:11927577,
ECO:0000269|PubMed:16460508,
ECO:0000269|PubMed:19825552,
ECO:0000269|PubMed:20118235}.
SEQUENCE 1025 AA; 111339 MW; B55D4FD938229D9B CRC64;
MISLPLLLFV LLFSALLLCP SSSDDDGDAA GDELALLSFK SSLLYQGGQS LASWNTSGHG
QHCTWVGVVC GRRRRRHPHR VVKLLLRSSN LSGIISPSLG NLSFLRELDL GDNYLSGEIP
PELSRLSRLQ LLELSDNSIQ GSIPAAIGAC TKLTSLDLSH NQLRGMIPRE IGASLKHLSN
LYLYKNGLSG EIPSALGNLT SLQEFDLSFN RLSGAIPSSL GQLSSLLTMN LGQNNLSGMI
PNSIWNLSSL RAFSVRENKL GGMIPTNAFK TLHLLEVIDM GTNRFHGKIP ASVANASHLT
VIQIYGNLFS GIITSGFGRL RNLTELYLWR NLFQTREQDD WGFISDLTNC SKLQTLNLGE
NNLGGVLPNS FSNLSTSLSF LALELNKITG SIPKDIGNLI GLQHLYLCNN NFRGSLPSSL
GRLKNLGILL AYENNLSGSI PLAIGNLTEL NILLLGTNKF SGWIPYTLSN LTNLLSLGLS
TNNLSGPIPS ELFNIQTLSI MINVSKNNLE GSIPQEIGHL KNLVEFHAES NRLSGKIPNT
LGDCQLLRYL YLQNNLLSGS IPSALGQLKG LETLDLSSNN LSGQIPTSLA DITMLHSLNL
SFNSFVGEVP TIGAFAAASG ISIQGNAKLC GGIPDLHLPR CCPLLENRKH FPVLPISVSL
AAALAILSSL YLLITWHKRT KKGAPSRTSM KGHPLVSYSQ LVKATDGFAP TNLLGSGSFG
SVYKGKLNIQ DHVAVKVLKL ENPKALKSFT AECEALRNMR HRNLVKIVTI CSSIDNRGND
FKAIVYDFMP NGSLEDWIHP ETNDQADQRH LNLHRRVTIL LDVACALDYL HRHGPEPVVH
CDIKSSNVLL DSDMVAHVGD FGLARILVDG TSLIQQSTSS MGFIGTIGYA APEYGVGLIA
STHGDIYSYG ILVLEIVTGK RPTDSTFRPD LGLRQYVELG LHGRVTDVVD TKLILDSENW
LNSTNNSPCR RITECIVWLL RLGLSCSQEL PSSRTPTGDI IDELNAIKQN LSGLFPVCEG
GSLEF


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