SERL2_ORYSJ
ID SERL2_ORYSJ Reviewed; 640 AA.
AC Q9FP13;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=LRR receptor kinase SERL2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BRI1-associated receptor kinase 1 homolog 7 {ECO:0000305};
DE Short=OsBAK1-7 {ECO:0000303|PubMed:25711711};
DE AltName: Full=Somatic embryogenesis receptor kinase-like 2 {ECO:0000305};
DE Short=OsSERL2 {ECO:0000305};
DE Flags: Precursor;
GN Name=SERL2 {ECO:0000305}; Synonyms=BAK1-7 {ECO:0000303|PubMed:25711711};
GN OrderedLocusNames=Os06g0274500 {ECO:0000312|EMBL:BAF19290.1},
GN LOC_Os06g16330 {ECO:0000305};
GN ORFNames=P0038C05.17 {ECO:0000312|EMBL:BAB19337.1},
GN P0676F10.28 {ECO:0000312|EMBL:BAD69166.1};
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 INTERACTION WITH MSBP1, AND SUBCELLULAR LOCATION.
RX PubMed=25711711; DOI=10.1093/jxb/erv058;
RA Xu C., Liu Y., Li Y., Xu X., Xu C., Li X., Xiao J., Zhang Q.;
RT "Differential expression of GS5 regulates grain size in rice.";
RL J. Exp. Bot. 66:2611-2623(2015).
CC -!- FUNCTION: LRR receptor kinase that may be involved in defense response.
CC {ECO:0000250|UniProtKB:Q7XV05}.
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 MSBP1. {ECO:0000269|PubMed:25711711}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25711711};
CC Single-pass membrane protein {ECO:0000255}. Note=Localizes in the
CC plasma membrane. {ECO:0000269|PubMed:25711711}.
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; AP003044; BAB19337.1; -; Genomic_DNA.
DR EMBL; AP005813; BAD69166.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19290.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS97218.1; -; Genomic_DNA.
DR RefSeq; XP_015643910.1; XM_015788424.1.
DR AlphaFoldDB; Q9FP13; -.
DR SMR; Q9FP13; -.
DR STRING; 4530.OS06T0274500-01; -.
DR PaxDb; Q9FP13; -.
DR PRIDE; Q9FP13; -.
DR EnsemblPlants; Os06t0274500-01; Os06t0274500-01; Os06g0274500.
DR GeneID; 4340743; -.
DR Gramene; Os06t0274500-01; Os06t0274500-01; Os06g0274500.
DR KEGG; osa:4340743; -.
DR eggNOG; ENOG502QVM7; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q9FP13; -.
DR OMA; VGRSKNH; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; 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; IBA:GO_Central.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Plant defense; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..640
FT /note="LRR receptor kinase SERL2"
FT /evidence="ECO:0000255"
FT /id="PRO_5010510702"
FT TOPO_DOM 23..241
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 95..119
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 120..143
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 145..167
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..191
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 304..583
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 310..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 640 AA; 69309 MW; 9F321366D06B9859 CRC64;
MEPPFFLLLL LLVVSSSSPS AALLSAKGVN NEVQALIVIK NLLKDPHGVL KSWDQNSVDP
CSWAMITCSP DFLVTGLEAP SQHLSGLLSP SIGNLTNLET VLLQNNNITG PIPAEIGRLE
NLKTLDLSSN SFYGEIPSSV GHLESLQYLR LNNNTLSGPF PSASANLSHL VFLDLSYNNL
SGPIPESLAR TYNIVGNPLI CDANREQDCY GTAPMPMSYS LNGSRGGALP PAARDRGHKF
AVAFGSTAGC MGLLLLAAGF LFWWRHRRNR QILFDVDEQQ IENVNLGNVK RFSFRELQAA
TEGFSGKNIL GKGGFGNVYR GQLPDGTLVA VKRLKDGNAA GGEAQFQTEV EMISLALHRN
LLRLYGFCMT ATERLLVYPF MSNGSVASRL KAKPALEWGT RRRIAVGAAR GLVYLHEQCD
PKIIHRDVKA ANVLLDEACE AVVGDFGLAK LLDHRESHVT TAVRGTVGHI APEYLSTGQS
SDRTDVFGFG ILLLELVTGQ TALEFGKSSN HKGAMLDWVK KMQSEKKVEV LVDKGLGGGY
DRVEVEEMVQ VALLCTQYLP AHRPRMSDVV RMLEGDGLAD RWEKASGHST AAADSLSHSH
RTSDPAPPAA DFAAAFGRCF SDLTDDSSLL VQAVELSGPR
