SIK1_ORYSJ
ID SIK1_ORYSJ Reviewed; 980 AA.
AC Q658G7; D0U6M6; Q7XB99;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase SIK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:20128882};
DE AltName: Full=ERECTA homolog 2 {ECO:0000303|PubMed:26280413};
DE Short=ER homolog 2 {ECO:0000303|PubMed:26280413};
DE Short=OsER2 {ECO:0000303|PubMed:26280413};
DE AltName: Full=Stress-induced protein kinase 1 {ECO:0000303|PubMed:20128882};
DE Short=OsSIK1 {ECO:0000303|PubMed:20128882};
DE Flags: Precursor;
GN Name=SIK1 {ECO:0000303|PubMed:20128882};
GN Synonyms=ER2 {ECO:0000303|PubMed:26280413}, ERL {ECO:0000305},
GN PK3 {ECO:0000312|EMBL:AAQ01160.1};
GN OrderedLocusNames=Os06g0130100 {ECO:0000312|EMBL:BAS95971.1},
GN LOC_Os06g03970 {ECO:0000305};
GN ORFNames=P0493C11.1 {ECO:0000312|EMBL:BAD67663.1},
GN P0538C01.27 {ECO:0000312|EMBL:BAD44800.1};
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP INDUCTION, AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Taipei 309;
RX PubMed=20128882; DOI=10.1111/j.1365-313x.2010.04146.x;
RA Ouyang S.Q., Liu Y.F., Liu P., Lei G., He S.J., Ma B., Zhang W.K.,
RA Zhang J.S., Chen S.Y.;
RT "Receptor-like kinase OsSIK1 improves drought and salt stress tolerance in
RT rice (Oryza sativa) plants.";
RL Plant J. 62:316-329(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Yao Q., Peng R., Xiong A.;
RT "Isolation of a transmembrane protein kinase from rice.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION.
RX PubMed=26280413; DOI=10.1038/nbt.3321;
RA Shen H., Zhong X., Zhao F., Wang Y., Yan B., Li Q., Chen G., Mao B.,
RA Wang J., Li Y., Xiao G., He Y., Xiao H., Li J., He Z.;
RT "Overexpression of receptor-like kinase ERECTA improves thermotolerance in
RT rice and tomato.";
RL Nat. Biotechnol. 33:996-1003(2015).
CC -!- FUNCTION: Receptor kinase involved in salt drought stress responses
CC (PubMed:20128882). Acts as positive regulator of salt and drought
CC tolerance (PubMed:20128882). May promote salt and drought tolerance
CC through the induction of the activities of antioxidative enzymes, such
CC as peroxidase, superoxide dismutase and catalase (PubMed:20128882). May
CC be involved in the control of stomatal development in leaf epidermis
CC (PubMed:20128882). Possesses kinase activity in vitro
CC (PubMed:20128882). Does not seem to be involved in heat tolerance
CC (PubMed:26280413). {ECO:0000269|PubMed:20128882,
CC ECO:0000269|PubMed:26280413}.
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:0000269|PubMed:20128882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:20128882};
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:0000269|PubMed:20128882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:20128882};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q658G7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q658G7-2; Sequence=VSP_060408;
CC -!- TISSUE SPECIFICITY: Expressed in nodes, vascular bundles of stems, and
CC anthers. {ECO:0000269|PubMed:20128882}.
CC -!- INDUCTION: Induced by salt and drought stresses, and hydrogen peroxide.
CC {ECO:0000269|PubMed:20128882}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:20128882}.
CC -!- DISRUPTION PHENOTYPE: Normal growth, but increased number of stomata in
CC adaxial and abaxial leaf epidermis (PubMed:20128882). Increased
CC sensitivity to salt and drought stresses (PubMed:20128882).
CC {ECO:0000269|PubMed:20128882}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; GQ423058; ACY07616.1; -; mRNA.
DR EMBL; AY332474; AAQ01160.1; -; mRNA.
DR EMBL; AP000391; BAD44800.1; -; Genomic_DNA.
DR EMBL; AP000559; BAD67663.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18601.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95970.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95971.1; -; Genomic_DNA.
DR RefSeq; XP_015641250.1; XM_015785764.1. [Q658G7-1]
DR AlphaFoldDB; Q658G7; -.
DR SMR; Q658G7; -.
DR STRING; 4530.OS06T0130100-02; -.
DR PRIDE; Q658G7; -.
DR EnsemblPlants; Os06t0130100-01; Os06t0130100-01; Os06g0130100. [Q658G7-1]
DR EnsemblPlants; Os06t0130100-02; Os06t0130100-02; Os06g0130100. [Q658G7-2]
DR GeneID; 4340000; -.
DR Gramene; Os06t0130100-01; Os06t0130100-01; Os06g0130100. [Q658G7-1]
DR Gramene; Os06t0130100-02; Os06t0130100-02; Os06g0130100. [Q658G7-2]
DR KEGG; osa:4340000; -.
DR eggNOG; ENOG502QTEP; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q658G7; -.
DR OMA; DEDFCSW; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q658G7; 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:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:2000038; P:regulation of stomatal complex development; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 15.
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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Stress response; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..980
FT /note="LRR receptor-like serine/threonine-protein kinase
FT SIK1"
FT /evidence="ECO:0000255"
FT /id="PRO_5013532896"
FT TOPO_DOM 25..588
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 75..98
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 99..122
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 124..146
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 147..170
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 171..194
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 196..218
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 219..242
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 243..265
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 266..289
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 290..312
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 314..337
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 338..361
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 362..385
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 387..408
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 409..433
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 435..457
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 458..480
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 481..505
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 507..529
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 531..554
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 653..923
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 778
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 659..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 536..558
FT /note="NLSYNNLSGHVPMAKNFSKFPME -> AFQEFVIQQFIWTCPDGKELLEIPN
FT GKHLLISDCNQYINHKC (in isoform 2)"
FT /id="VSP_060408"
FT CONFLICT 69..71
FT /note="TCD -> SCE (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="N -> D (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> S (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="K -> Q (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> P (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="V -> I (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="L -> P (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="P -> V (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="N -> D (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="I -> T (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="N -> D (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="L -> F (in Ref. 1; ACY07616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 106727 MW; 01AF615E3EC5E557 CRC64;
MAAARAPWLW WWVVVVVGVA VAEAASGGGG GGDGEGKALM GVKAGFGNAA NALVDWDGGA
DHCAWRGVTC DNASFAVLAL NLSNLNLGGE ISPAIGELKN LQFVDLKGNK LTGQIPDEIG
DCISLKYLDL SGNLLYGDIP FSISKLKQLE ELILKNNQLT GPIPSTLSQI PNLKTLDLAQ
NQLTGDIPRL IYWNEVLQYL GLRGNSLTGT LSPDMCQLTG LWYFDVRGNN LTGTIPESIG
NCTSFEILDI SYNQISGEIP YNIGFLQVAT LSLQGNRLTG KIPDVIGLMQ ALAVLDLSEN
ELVGPIPSIL GNLSYTGKLY LHGNKLTGVI PPELGNMSKL SYLQLNDNEL VGTIPAELGK
LEELFELNLA NNNLQGPIPA NISSCTALNK FNVYGNKLNG SIPAGFQKLE SLTYLNLSSN
NFKGNIPSEL GHIINLDTLD LSYNEFSGPV PATIGDLEHL LELNLSKNHL DGPVPAEFGN
LRSVQVIDMS NNNLSGSLPE ELGQLQNLDS LILNNNNLVG EIPAQLANCF SLNNLNLSYN
NLSGHVPMAK NFSKFPMESF LGNPLLHVYC QDSSCGHSHG QRVNISKTAI ACIILGFIIL
LCVLLLAIYK TNQPQPLVKG SDKPVQGPPK LVVLQMDMAI HTYEDIMRLT ENLSEKYIIG
YGASSTVYKC ELKSGKAIAV KRLYSQYNHS LREFETELET IGSIRHRNLV SLHGFSLSPH
GNLLFYDYME NGSLWDLLHG PSKKVKLNWD TRLRIAVGAA QGLAYLHHDC NPRIIHRDVK
SSNILLDENF EAHLSDFGIA KCVPSAKSHA STYVLGTIGY IDPEYARTSR LNEKSDVYSF
GIVLLELLTG KKAVDNESNL HQLILSKADD NTVMEAVDSE VSVTCTDMGL VRKAFQLALL
CTKRHPSDRP TMHEVARVLL SLLPASAMTT PKTVDYSRLL ASTTTAADMR GHDVTDIGDN
SSSDEQWFVR FGEVISKHTM
