SIT2_ORYSJ
ID SIT2_ORYSJ Reviewed; 673 AA.
AC Q7XUN6; Q0JBH7;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=L-type lectin-domain containing receptor kinase SIT2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q6H7D2};
DE AltName: Full=Protein SALT INTOLERANCE 2 {ECO:0000303|PubMed:24907341};
DE Flags: Precursor;
GN Name=SIT2 {ECO:0000303|PubMed:24907341};
GN OrderedLocusNames=Os04g0531400 {ECO:0000312|EMBL:BAS90216.1},
GN LOC_Os04g44900 {ECO:0000305};
GN ORFNames=OsJ_15568 {ECO:0000312|EMBL:EEE61393.1},
GN OSJNBa0081C01.16 {ECO:0000312|EMBL:CAD41144.2};
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY SALT STRESS.
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).
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). {ECO:0000269|PubMed:24907341}.
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:0000250|UniProtKB:Q6H7D2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:Q6H7D2};
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:0000250|UniProtKB:Q6H7D2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:Q6H7D2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in root epidermal cells.
CC {ECO:0000269|PubMed:24907341}.
CC -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:24907341}.
CC -!- MISCELLANEOUS: The gain-of-function mutant sit2-D (T-DNA tagging)
CC exhibits reduced tolerance to salt stress.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF15310.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS90216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL662984; CAD41144.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15310.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS90216.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000141; EEE61393.1; -; Genomic_DNA.
DR RefSeq; XP_015635472.1; XM_015779986.1.
DR AlphaFoldDB; Q7XUN6; -.
DR SMR; Q7XUN6; -.
DR STRING; 4530.OS04T0531400-01; -.
DR EnsemblPlants; Os04t0531400-01; Os04t0531400-01; Os04g0531400.
DR GeneID; 4336489; -.
DR Gramene; Os04t0531400-01; Os04t0531400-01; Os04g0531400.
DR KEGG; osa:4336489; -.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q7XUN6; -.
DR OrthoDB; 418528at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS: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; 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; 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; Cell membrane; Glycoprotein; Kinase; Lectin; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..673
FT /note="L-type lectin-domain containing receptor kinase
FT SIT2"
FT /id="PRO_5010144878"
FT TOPO_DOM 28..296
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 352..631
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 32..270
FT /note="Legume-lectin like"
FT /evidence="ECO:0000305"
FT ACT_SITE 477
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 358..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 673 AA; 73872 MW; B102E5D74EAAD233 CRC64;
MVLPKPEMPF FVLLLFLGLG CLRPAAATDE RFVFNGFTGA NLSFDGMATV TSNGLLMLTN
GTNQLKGHAF FPSPLQFQRG PNSTAMQSFS TAFVIGIIGA FEDLSSHGMA FIIAKSKNLT
SALPGQFMGL VNSANNGNAT NHLFAVEFDT ILNSEFNDMS GNHVGIDVNG LNSVDADNAG
YYDDGTGDFK NMSLVSRRPM QVWVDFDGQT MQVNVTMAPL EVARPKKPLL SKIVNISSVI
DDTAYVGFSS ATGILFCRHY VLGWSFKMNG AAPALNISSL PSLPVTFPKP RSKTLEIVLP
IASAVLVFAV AAAVFVFMRR RRMFSELKEE WEVTFGPHRF SYKDLFHATD GFSDKRLLGI
GGFGRVYRGV LPSSKAEVAV KKVAHGSRQG MREFVAEVVS IGRLRHRNLV QLLGYCRRKG
ELLLVYDYMP NGSLDKQLYD QGKITLRWAQ RFRIIRGVAS GLLYLHEDWE QVVVHRDIKA
SNVLLDADMN GRLGDFGLAR LYDHGTDPHT THVVGTMGYL APELGHTGKA SKASDVFAFG
AFMLEVACGR KPVAQDARDN RVVLVDWVLD RWRAGAITDT VDPRLHGDFV ESEASLVLRL
GLLCSHPLPG ARPGTRQLVQ YLEGDVPLPE LSPTYQSFNM LALMQDQGFD PYVMSYPMTS
TSAGTFSDLS GGR
