SERK3_ORYSJ
ID SERK3_ORYSJ Reviewed; 616 AA.
AC Q67X31;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 3 {ECO:0000305};
DE Short=OsBAK1-3 {ECO:0000305};
DE AltName: Full=Somatic embryogenesis receptor kinase 3 {ECO:0000305};
DE Short=OsSERK3 {ECO:0000303|PubMed:19754838};
DE Flags: Precursor;
GN Name=SERK3 {ECO:0000303|PubMed:19754838};
GN OrderedLocusNames=Os06g0225300 {ECO:0000312|EMBL:BAF19110.1},
GN LOC_Os06g12120 {ECO:0000305};
GN ORFNames=OsJ_20659 {ECO:0000312|EMBL:EEE65366.1},
GN OSNPB_060225300 {ECO:0000312|EMBL:BAS96861.1},
GN P0690H04.4 {ECO:0000312|EMBL:BAD37288.1};
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
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).
CC -!- FUNCTION: May be involved in regulation of plant growth through the
CC brassinosteroid (BR) signaling pathway. {ECO:0000269|PubMed:19754838}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
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; AP003513; BAD37288.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19110.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96861.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65366.1; -; Genomic_DNA.
DR EMBL; AK100258; BAG94518.1; -; mRNA.
DR RefSeq; XP_015643547.1; XM_015788061.1.
DR AlphaFoldDB; Q67X31; -.
DR SMR; Q67X31; -.
DR STRING; 4530.OS06T0225300-01; -.
DR PaxDb; Q67X31; -.
DR PRIDE; Q67X31; -.
DR EnsemblPlants; Os06t0225300-01; Os06t0225300-01; Os06g0225300.
DR EnsemblPlants; Os06t0225300-02; Os06t0225300-02; Os06g0225300.
DR GeneID; 4340544; -.
DR Gramene; Os06t0225300-01; Os06t0225300-01; Os06g0225300.
DR Gramene; Os06t0225300-02; Os06t0225300-02; Os06g0225300.
DR KEGG; osa:4340544; -.
DR eggNOG; ENOG502QQ7B; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q67X31; -.
DR OMA; PIVVFAW; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Brassinosteroid signaling pathway; Cell membrane;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..616
FT /note="LRR receptor kinase SERK2"
FT /evidence="ECO:0000255"
FT /id="PRO_5010506424"
FT TOPO_DOM 24..226
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 65..89
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 90..113
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 115..137
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 138..161
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 162..186
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 289..573
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 594..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 295..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
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 CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 616 AA; 67721 MW; 925ABCFB300A3480 CRC64;
MAARRRLLLL LVLLLCRLAA VLPTSEVEAL QGFMAGFAGG NAAFQSWDAS APNPCTWFHV
TCGPGNQVIR LDLGNQSLSG ELKPDIWQLQ ALQSLELYGN SISGKIPSEL GRLASLQTLD
LYLNNFTGEI PNELGNLSKL SNLRLNNNSL SGAIPMSLTT IQNLEVLDLS HNNLSGIIPT
NGSFSHFTPI SFSNNPRTFA NSSDSPSNNS GAAVPSGRSS ASSIGTIAGG AAAGAAMLFA
APIVLFAWWW RRKPHDQFFD LLEEETPEVH LGQLRRFTLR ELQVATDNFS QTNLLGRGGF
GKVYKGRLLD GSLIAIKRLN EDRIGTGERQ FLMEVEIISM AVHQNLLRLQ GYCMTPTERL
LVYPYMENKS LETRLRECSD SQQPLDWPTR RKIALGSARG ISYLHEGCDP KIIHRDVKAA
NILLDEKLEA VVGDFGLARI MDYKVSHVVT GVMGTLGHIP MEYLTAGRTS DKTDVFGYGI
MLFELISGKR GFDLVGLANE ENARVHDWVK KLLEEDRLEV LIDPNLLEIY NGGEQGVREE
MRLLVQIALL CTQESAPSRP RMSTVVTMLE DGIAEHWDAW QRKTIVQASL QGGQGVSEAR
NDSVANLPPD TLSGPR
