ID SERK4_ORYSJ Reviewed; 607 AA.
AC Q6K4T4;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 167.
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 5 {ECO:0000305};
DE Short=OsBAK1-5 {ECO:0000305};
DE AltName: Full=Somatic embryogenesis receptor kinase 4 {ECO:0000305};
DE Short=OsSERK4 {ECO:0000303|PubMed:19754838};
DE Flags: Precursor;
GN Name=SERK4 {ECO:0000303|PubMed:19754838};
GN OrderedLocusNames=Os02g0283800 {ECO:0000312|EMBL:BAF08482.1},
GN LOC_Os02g18320 {ECO:0000305};
GN ORFNames=OsJ_06271 {ECO:0000312|EMBL:EAZ22603.1},
GN OSJNBa0018M09.11 {ECO:0000312|EMBL:BAD22198.1};
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 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 the 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; AP005533; BAD22198.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08482.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS78137.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ22603.1; -; Genomic_DNA.
DR RefSeq; XP_015627048.1; XM_015771562.1.
DR AlphaFoldDB; Q6K4T4; -.
DR SMR; Q6K4T4; -.
DR STRING; 39947.Q6K4T4; -.
DR GlyCosmos; Q6K4T4; 6 sites, No reported glycans.
DR PaxDb; 39947-Q6K4T4; -.
DR EnsemblPlants; Os02t0283800-01; Os02t0283800-01; Os02g0283800.
DR GeneID; 4329032; -.
DR Gramene; Os02t0283800-01; Os02t0283800-01; Os02g0283800.
DR KEGG; osa:4329032; -.
DR eggNOG; ENOG502QPJ2; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q6K4T4; -.
DR OMA; CSTNMSY; -.
DR OrthoDB; 1064141at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47988:SF93; LRR RECEPTOR KINASE SERK2; 1.
DR PANTHER; PTHR47988; SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..607
FT /note="LRR receptor kinase SERK2"
FT /evidence="ECO:0000255"
FT /id="PRO_5010506967"
FT TOPO_DOM 22..219
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 87..110
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 111..135
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 136..159
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 160..183
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 284..563
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 411
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 290..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 607 AA; 67659 MW; DB924EB64D0702B8 CRC64;
MRELRVAVLI IAVSLPSFSA SDRQGDALYD MKQKLNVTGN QLSDWNQNQV NPCTWNSVIC
DNNNNVIQVT LAARGFAGVL SPRIGELKYL TVLSLAGNRI SGGIPEQFGN LSSLTSLDLE
DNLLVGEIPA SLGQLSKLQL LILSDNNFNG SIPDSLAKIS SLTDIRLAYN NLSGQIPGPL
FQVARYNFSG NHLNCGTNFP HSCSTNMSYQ SGSHSSKIGI VLGTVGGVIG LLIVAALFLF
CKGRRKSHLR EVFVDVAGED DRRIAFGQLK RFAWRELQIA TDNFSERNVL GQGGFGKVYK
GVLPDGTKIA VKRLTDYESP GGEAAFLREV ELISVAVHRN LLKLIGFCTT QTERLLVYPF
MQNLSVAYRL RDFKPGEPVL NWPERKRVAI GTARGLEYLH EHCNPKIIHR DVKAANVLLD
EDFEPVVGDF GLAKLVDVQK TSVTTQVRGT MGHIAPEYLS TGKSSERTDV FGYGIMLLEL
VTGQRAIDFS RLEEEDDVLL LDHVKKLQRE GQLGSIVDRN LNQNYDDEEV EMMIQIALLC
TQSSPEDRPS MSEVVRMLEG EGLAERWEEW QQVEVTRRQE YERMQRRFDW GEDSVYNQEA
IELSGGR
//
