SIT1_ORYSJ
ID SIT1_ORYSJ Reviewed; 674 AA.
AC Q6H7D2;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=L-type lectin-domain containing receptor kinase SIT1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:24907341};
DE AltName: Full=Protein SALT INTOLERANCE 1 {ECO:0000303|PubMed:24907341};
DE Flags: Precursor;
GN Name=SIT1 {ECO:0000303|PubMed:24907341};
GN OrderedLocusNames=Os02g0640500 {ECO:0000312|EMBL:BAF09461.1},
GN LOC_Os02g42780 {ECO:0000305};
GN ORFNames=P0010C01.40 {ECO:0000312|EMBL:BAD25367.1};
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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION BY SALT STRESS, AND MUTAGENESIS OF LYS-386
RP AND ASP-482.
RX PubMed=24907341; DOI=10.1105/tpc.114.125187;
RA Li C.H., Wang G., Zhao J.L., Zhang L.Q., Ai L.F., Han Y.F., Sun D.Y.,
RA Zhang S.W., Sun Y.;
RT "The receptor-like kinase SIT1 mediates salt sensitivity by activating
RT MAPK3/6 and regulating ethylene homeostasis in rice.";
RL Plant Cell 26:2538-2553(2014).
RN [6]
RP FUNCTION, INTERACTION WITH B'KAPPA, PHOSPHORYLATION AT THR-511; THR-515;
RP THR-516 AND THR-521, AND MUTAGENESIS OF THR-511 AND 515-THR-THR-516.
RX PubMed=31221736; DOI=10.1105/tpc.18.00706;
RA Zhao J.L., Zhang L.Q., Liu N., Xu S.L., Yue Z.L., Zhang L.L., Deng Z.P.,
RA Burlingame A.L., Sun D.Y., Wang Z.Y., Sun Y., Zhang S.W.;
RT "Mutual regulation of receptor-like kinase SIT1 and B'kappa-PP2A shapes the
RT early response of rice to salt stress.";
RL Plant Cell 31:2131-2151(2019).
CC -!- FUNCTION: Lectin-domain containing receptor kinase involved in salt
CC stress response (PubMed:24907341). Acts as negative regulator of salt
CC tolerance (PubMed:24907341). Mediates salt sensitivity by
CC phosphorylating and activating MPK3 and MPK6 (PubMed:24907341).
CC Promotes ethylene production and mediates salt-induced ethylene
CC signaling (PubMed:24907341). Promotes the accumulation of reactive
CC oxygen species (ROS) under salt stress conditions (PubMed:24907341).
CC Its kinase activity is triggered by salt stress and is required for its
CC function in salt stress response (PubMed:24907341). Phosphorylates
CC B'KAPPA, a B regulatory subunit of phosphatase 2A (PP2A)
CC (PubMed:31221736). {ECO:0000269|PubMed:24907341,
CC ECO:0000269|PubMed:31221736}.
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:24907341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:24907341};
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:24907341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:24907341};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation in response to
CC salt stress. {ECO:0000269|PubMed:24907341}.
CC -!- SUBUNIT: Interacts with B'KAPPA. {ECO:0000269|PubMed:31221736}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24907341};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in root epidermal cells.
CC {ECO:0000269|PubMed:24907341}.
CC -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:24907341}.
CC -!- PTM: Autophosphorylated at THR-511, THR-515 or THR-516, and THR-521 in
CC response to salt stress (PubMed:31221736). Dephosphorylated by
CC phosphatase 2A in response to salt stress (PubMed:31221736).
CC {ECO:0000269|PubMed:31221736}.
CC -!- MISCELLANEOUS: Plants silencing SIT1 exhibit increased tolerance to
CC salt stress. {ECO:0000269|PubMed:24907341}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000305}.
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DR EMBL; AP004768; BAD25367.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09461.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79982.1; -; Genomic_DNA.
DR EMBL; AK107491; BAG98063.1; -; mRNA.
DR RefSeq; XP_015624170.1; XM_015768684.1.
DR AlphaFoldDB; Q6H7D2; -.
DR SMR; Q6H7D2; -.
DR STRING; 4530.OS02T0640500-01; -.
DR PaxDb; Q6H7D2; -.
DR PRIDE; Q6H7D2; -.
DR EnsemblPlants; Os02t0640500-01; Os02t0640500-01; Os02g0640500.
DR GeneID; 4330111; -.
DR Gramene; Os02t0640500-01; Os02t0640500-01; Os02g0640500.
DR KEGG; osa:4330111; -.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q6H7D2; -.
DR OMA; RVWVDFD; -.
DR OrthoDB; 418528at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate 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:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IBA:GO_Central.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 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; Lectin; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Stress response; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..674
FT /note="L-type lectin-domain containing receptor kinase
FT SIT1"
FT /id="PRO_5013533136"
FT TOPO_DOM 28..301
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 357..636
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 31..275
FT /note="Legume-lectin like"
FT /evidence="ECO:0000305"
FT ACT_SITE 482
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 363..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT MOD_RES 515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31221736"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 386
FT /note="K->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:24907341"
FT MUTAGEN 482
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000305"
FT MUTAGEN 511
FT /note="T->A: Abolishes autophosphorylation and activation
FT of kinase activity."
FT /evidence="ECO:0000269|PubMed:31221736"
FT MUTAGEN 515..516
FT /note="TT->AA: Abolishes autophosphorylation and activation
FT of kinase activity."
FT /evidence="ECO:0000269|PubMed:31221736"
SQ SEQUENCE 674 AA; 73240 MW; 465C8D07AF226678 CRC64;
MRRPELIMRS LPLILFLSLG SFHLAAAAVD DQFTFDGFAG VNLTLDGTAV VTPGGLLMLT
NGTTLLKGHA FYPSPLRFFH EATSGGGSST VRSFSTAFVF GIVSEYADLS SPGLAFVVAK
SRDFSSALQS QYMGLANARN NGNASNHFLA VELDTIVNAE FGDMSDNHVG IDVDGLASAA
ADDAGYHDDR TGAFVNMSLL SRAAARVWVD FDARTSLVNV TMAPLELPKP TTPLLSAAVN
LSAVIEDEAY VGFSSSTGVV ASRHYVLAWS FKMDGPAPSL NVSKLPALPV TIARAPSNVL
KILLPIASAA LVSALAIAVL VIHRRRRRYA ELKEEWEVAF GPHRFSYKDL FRATNGFSDE
RLLGFGGFGR VYKGVLLVSR VEIAVKKVSH ESRQGMKEFI AEVVSIGQLR HRNLVQLLGY
CRQKGELLLV YDYMPNGSLD KYLYAENSKI LSWAQRFRII KGIASSILYL HEDWEQVVLH
RDIKASNVLL DAEMNCRLGD FGLARLYDRG TDPHTTHVVG TIGYLAPELG HTGRPSKASD
IFAFGVFMLE VTCGRRPVLQ DTNGGQLLLV DMVLEHWRQG TVTDAVDPRL QGDFAVEEAS
LVLKLCLLCS HPLPSARPGI RQVVQLLDGA MPLPELSQAH LSCNMLALMQ NQMGNSCSVA
SSVAGNISDI PRAR
