SERK2_ORYSJ
ID SERK2_ORYSJ Reviewed; 628 AA.
AC Q7XV05; Q5Y8C8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=LRR receptor kinase SERK2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BRI1-associated receptor kinase 1 homolog 2 {ECO:0000305};
DE Short=OsBAK1-2 {ECO:0000303|PubMed:22058019};
DE AltName: Full=Somatic embryogenesis receptor kinase 2 {ECO:0000305};
DE Short=OsSERK2 {ECO:0000303|PubMed:16081169};
DE Flags: Precursor;
GN Name=SERK2 {ECO:0000303|PubMed:16081169};
GN Synonyms=SERK1 {ECO:0000303|PubMed:15968510};
GN OrderedLocusNames=Os04g0457800 {ECO:0000312|EMBL:BAF14889.1},
GN LOC_Os04g38480 {ECO:0000305};
GN ORFNames=OsJ_15037 {ECO:0000312|EMBL:EAZ30959.1},
GN OSJNBa0036B21.13 {ECO:0000312|EMBL:CAD40895.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Drew;
RX PubMed=15968510; DOI=10.1007/s00425-005-1534-4;
RA Hu H., Xiong L., Yang Y.;
RT "Rice SERK1 gene positively regulates somatic embryogenesis of cultured
RT cell and host defense response against fungal infection.";
RL Planta 222:107-117(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP INDUCTION BY MAGNAPORTHE ORYZAE.
RX PubMed=11332734; DOI=10.1094/mpmi.2001.14.5.685;
RA Xiong L., Lee M.W., Qi M., Yang Y.;
RT "Identification of defense-related rice genes by suppression subtractive
RT hybridization and differential screening.";
RL Mol. Plant Microbe Interact. 14:685-692(2001).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16081169; DOI=10.1016/j.bbaexp.2005.06.007;
RA Ito Y., Takaya K., Kurata N.;
RT "Expression of SERK family receptor-like protein kinase genes in rice.";
RL Biochim. Biophys. Acta 1730:253-258(2005).
RN [9]
RP FUNCTION.
RC STRAIN=cv. Zhonghua 11;
RX PubMed=19754838; DOI=10.1111/j.1467-7652.2009.00444.x;
RA Li D., Wang L., Wang M., Xu Y.Y., Luo W., Liu Y.J., Xu Z.H., Li J.,
RA Chong K.;
RT "Engineering OsBAK1 gene as a molecular tool to improve rice architecture
RT for high yield.";
RL Plant Biotechnol. J. 7:791-806(2009).
RN [10]
RP INTERACTION WITH BRI1.
RX PubMed=22058019; DOI=10.1007/s10059-011-0178-4;
RA Park H.S., Ryu H.Y., Kim B.H., Kim S.Y., Yoon I.S., Nam K.H.;
RT "A subset of OsSERK genes, including OsBAK1, affects normal growth and leaf
RT development of rice.";
RL Mol. Cells 32:561-569(2011).
RN [11]
RP FUNCTION, INTERACTION WITH XA21; XA26/XA3; FLS2 AND BRI1, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION AT THR-303; SER-329; THR-350; SER-356;
RP SER-387; THR-463; THR-466; THR-472; SER-615; THR-616 AND SER-625.
RX PubMed=24482436; DOI=10.1093/mp/ssu003;
RA Chen X., Zuo S., Schwessinger B., Chern M., Canlas P.E., Ruan D., Zhou X.,
RA Wang J., Daudi A., Petzold C.J., Heazlewood J.L., Ronald P.C.;
RT "An XA21-associated kinase (OsSERK2) regulates immunity mediated by the
RT XA21 and XA3 immune receptors.";
RL Mol. Plant 7:874-892(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 32-198, GLYCOSYLATION AT ASN-120,
RP DISULFIDE BONDS, AND MUTAGENESIS OF ASP-128.
RX PubMed=25372696; DOI=10.1107/s1399004714021178;
RA McAndrew R., Pruitt R.N., Kamita S.G., Pereira J.H., Majumdar D.,
RA Hammock B.D., Adams P.D., Ronald P.C.;
RT "Structure of the OsSERK2 leucine-rich repeat extracellular domain.";
RL Acta Crystallogr. D 70:3080-3086(2014).
CC -!- FUNCTION: LRR receptor kinase involved in positive regulation of
CC somatic embryogenesis and defense response against the rice blast
CC fungus pathogen Magnaporthe oryzae (PubMed:15968510). Involved in the
CC positive regulation of receptor kinase-mediated immunity. Required for
CC immunity mediated by the LRR receptor kinases XA21 and XA26/XA3 which
CC recognize effectors from the bacterial pathogen Xanthomonas oryzae pv.
CC oryzae (Xoo). Required for the immune response mediated by the LRR
CC receptor kinase FLS2 which recognizes specifically the bacterial
CC flagellin (flg22) effector. Kinase activity and direct interaction with
CC the immune receptors is critical for their function (PubMed:24482436).
CC Involved in the regulation of plant growth through the brassinosteroid
CC (BR) signaling pathway (PubMed:19754838, PubMed:24482436).
CC {ECO:0000269|PubMed:15968510, ECO:0000269|PubMed:19754838,
CC ECO:0000269|PubMed:24482436}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Interacts with BRI1 (PubMed:22058019, PubMed:24482436).
CC Interacts with XA21, XA26/XA3 and FLS2 (PubMed:25372696).
CC {ECO:0000269|PubMed:22058019, ECO:0000269|PubMed:24482436,
CC ECO:0000269|PubMed:25372696}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flag leaves (PubMed:11332734).
CC Expressed in roots, shoot apex, leaf blades, leaf sheaths, panicles and
CC flowers (PubMed:16081169). Expressed leaves, stems, sheaths and flowers
CC (PubMed:24482436). {ECO:0000269|PubMed:11332734,
CC ECO:0000269|PubMed:16081169, ECO:0000269|PubMed:24482436}.
CC -!- INDUCTION: Induced by infection with the rice blast fungus Magnaporthe
CC oryzae (PubMed:11332734, PubMed:15968510). Induced by salicylate (SA),
CC jasmonate (JA), abscisic acid (ABA) and benzothiadiazole (BTH)
CC (PubMed:15968510). {ECO:0000269|PubMed:11332734,
CC ECO:0000269|PubMed:15968510}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:24482436}.
CC -!- MISCELLANEOUS: Plants silencing SERK2 exhibit strong reduction of
CC percentage of shoot regeneration from callus. Plants over-expressing
CC SERK2 show enhanced resistance to the rice blast fungus Magnaporthe
CC oryzae (PubMed:15968510). Plants silencing SERK2 have compromised
CC XA21- and XA3/XA26-mediated immunity to the bacterial leaf blight
CC pathogen Xanthomonas oryzae pv. oryzae (Xoo). Plants silencing SERK2
CC display altered morphology and reduced sensitivity to the hormone
CC brassinolide (PubMed:24482436). {ECO:0000269|PubMed:15968510,
CC ECO:0000269|PubMed:24482436}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AY652735; AAU88198.1; -; mRNA.
DR EMBL; AL606636; CAD40895.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89517.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF14889.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ30959.1; -; Genomic_DNA.
DR RefSeq; XP_015636497.1; XM_015781011.1.
DR PDB; 4Q3G; X-ray; 2.79 A; A/B=32-198.
DR PDB; 4Q3I; X-ray; 2.35 A; A/B=32-198.
DR PDBsum; 4Q3G; -.
DR PDBsum; 4Q3I; -.
DR AlphaFoldDB; Q7XV05; -.
DR SMR; Q7XV05; -.
DR STRING; 4530.OS04T0457800-01; -.
DR iPTMnet; Q7XV05; -.
DR PaxDb; Q7XV05; -.
DR PRIDE; Q7XV05; -.
DR EnsemblPlants; Os04t0457800-01; Os04t0457800-01; Os04g0457800.
DR GeneID; 4336035; -.
DR Gramene; Os04t0457800-01; Os04t0457800-01; Os04g0457800.
DR KEGG; osa:4336035; -.
DR eggNOG; ENOG502QQ7B; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q7XV05; -.
DR OMA; WETRARI; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7XV05; baseline and differential.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
DR GO; GO:0010262; P:somatic embryogenesis; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
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; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 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; ATP-binding; Brassinosteroid signaling pathway;
KW Cell membrane; Differentiation; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..628
FT /note="LRR receptor kinase SERK2"
FT /id="PRO_5010508816"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 97..121
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 123..144
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 145..169
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 170..194
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 306..593
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 433
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 312..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 616
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24482436"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:25372696, ECO:0007744|PDB:4Q3G,
FT ECO:0007744|PDB:4Q3I"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 128
FT /note="D->N: Abolishes binding capacity to BRI1."
FT /evidence="ECO:0000269|PubMed:25372696"
FT CONFLICT 17..18
FT /note="PF -> AV (in Ref. 1; AAU88198 and 6; EAZ30959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 69588 MW; F4F63F3D5879904C CRC64;
MAEARLLRRR RLCLAVPFVW VVAVAVSRVG ANTEGDALYS LRQSLKDANN VLQSWDPTLV
NPCTWFHVTC NPDNSVIRVD LGNAQLSGAL VPQLGQLKNL QYLELYSNNI SGTIPNELGN
LTNLVSLDLY LNNFTGFIPE TLGQLYKLRF LRLNNNSLSG SIPKSLTNIT TLQVLDLSNN
NLSGEVPSTG SFSLFTPISF ANNKDLCGPG TTKPCPGAPP FSPPPPFNPP TPTVSQGDSK
TGAIAGGVAA AAALLFAVPA IGFAWWRRRK PEEHFFDVPA EEDPEVHLGQ LKRFSLRELQ
VATDNFSNKN ILGRGGFGKV YKGRLADGSL VAVKRLKEER TPGGELQFQT EVEMISMAVH
RNLLRLRGFC MTPTERLLVY PYMANGSVAS RLRERQPNDP PLEWQTRTRI ALGSARGLSY
LHDHCDPKII HRDVKAANIL LDEDFEAVVG DFGLAKLMDY KDTHVTTAVR GTIGHIAPEY
LSTGKSSEKT DVFGYGIMLL ELITGQRAFD LARLANDDDV MLLDWVKGLL KEKKVEMLVD
PDLQSGFVEH EVESLIQVAL LCTQGSPMDR PKMSEVVRML EGDGLAERWE EWQKVEVVRQ
EAELAPRHND WIVDSTYNLR AMELSGPR
