STRK1_ORYSJ
ID STRK1_ORYSJ Reviewed; 361 AA.
AC Q7XR88; Q01IP5;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Salt tolerance receptor-like cytoplasmic kinase 1 {ECO:0000303|PubMed:29581216};
DE EC=2.7.12.1 {ECO:0000269|PubMed:29581216};
DE AltName: Full=Receptor-like cytoplasmic kinase 154 {ECO:0000303|PubMed:19825577};
DE Short=OsRLCK154 {ECO:0000303|PubMed:19825577};
GN Name=STRK1 {ECO:0000303|PubMed:29581216};
GN Synonyms=RLCK154 {ECO:0000303|PubMed:19825577};
GN OrderedLocusNames=LOC_Os04g45730 {ECO:0000303|PubMed:19825577},
GN Os04g0540900 {ECO:0000312|EMBL:BAF15357.1};
GN ORFNames=H0115B09.7 {ECO:0000312|EMBL:CAH67395.1},
GN OsJ_15629 {ECO:0000312|EMBL:EAZ31493.1},
GN OSJNBa0011L07.13 {ECO:0000312|EMBL:CAE02789.2},
GN OSNPB_040540900 {ECO:0000312|EMBL:BAS90293.1};
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=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 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 [7]
RP TISSUE SPECIFICITY, INDUCTION BY ABIOTIC STRESSES, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=19825577; DOI=10.1093/mp/ssn047;
RA Vij S., Giri J., Dansana P.K., Kapoor S., Tyagi A.K.;
RT "The receptor-like cytoplasmic kinase (OsRLCK) gene family in rice:
RT organization, phylogenetic relationship, and expression during development
RT and stress.";
RL Mol. Plant 1:732-750(2008).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-5; CYS-10; CYS-14 AND
RP LYS-95, PALMITOYLATION, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION,
RP INDUCTION BY SALT STRESS, TISSUE SPECIFICITY, INTERACTION WITH CATA; CATB
RP AND CATC, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Kitaake;
RX PubMed=29581216; DOI=10.1105/tpc.17.01000;
RA Zhou Y.-B., Liu C., Tang D.-Y., Yan L., Wang D., Yang Y.-Z., Gui J.-S.,
RA Zhao X.-Y., Li L.-G., Tang X.-D., Yu F., Li J.-L., Liu L.-L., Zhu Y.-H.,
RA Lin J.-Z., Liu X.-M.;
RT "The receptor-like cytoplasmic kinase STRK1 phosphorylates and activates
RT CatC, thereby regulating H2O2 homeostasis and improving salt tolerance in
RT rice.";
RL Plant Cell 30:1100-1118(2018).
CC -!- FUNCTION: Acts probably as a dual specificity protein kinase
CC (Probable). Regulates hydrogen peroxide (H(2)O(2)) homeostasis and
CC improves salt tolerance by phosphorylating tyrosine residues of CATC
CC thus activating its catalase activity. Promotes growth at the seedling
CC stage and prevents grain yield loss under salt stress conditions
CC (PubMed:29581216). {ECO:0000269|PubMed:29581216, ECO:0000305}.
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=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:29581216};
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=2.7.12.1; Evidence={ECO:0000269|PubMed:29581216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:29581216};
CC -!- SUBUNIT: Self-interacts. Interacts with CATA, CATB and CATC at the
CC plasma membrane. {ECO:0000269|PubMed:29581216}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29581216};
CC Lipid-anchor {ECO:0000269|PubMed:29581216}.
CC -!- TISSUE SPECIFICITY: Accumulates in seeds (PubMed:19825577). Mainly
CC expressed in young roots, and, to a lower extent, in leaf veins,
CC seedlings, stems, leaf sheath and young spikelet (PubMed:29581216).
CC {ECO:0000269|PubMed:19825577, ECO:0000269|PubMed:29581216}.
CC -!- INDUCTION: By cold and dehydration (PubMed:19825577). Induced by salt
CC (NaCl) and oxidative (H(2)O(2)) stresses (PubMed:29581216,
CC PubMed:19825577). {ECO:0000269|PubMed:19825577,
CC ECO:0000269|PubMed:29581216}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:29581216}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:29581216}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to salt (NaCl) stress with
CC increased oxidative attack on membrane lipids and higher intracellular
CC Na(+)/K(+) ratio associated with reduced phosphorylation of CATC.
CC {ECO:0000269|PubMed:29581216}.
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; AL606587; CAE02789.2; -; Genomic_DNA.
DR EMBL; CR855197; CAH67395.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF15357.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90293.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ31493.1; -; Genomic_DNA.
DR EMBL; AK066397; BAG89950.1; -; mRNA.
DR RefSeq; XP_015634281.1; XM_015778795.1.
DR AlphaFoldDB; Q7XR88; -.
DR SMR; Q7XR88; -.
DR STRING; 4530.OS04T0540900-01; -.
DR PaxDb; Q7XR88; -.
DR PRIDE; Q7XR88; -.
DR EnsemblPlants; Os04t0540900-01; Os04t0540900-01; Os04g0540900.
DR GeneID; 4336539; -.
DR Gramene; Os04t0540900-01; Os04t0540900-01; Os04g0540900.
DR KEGG; osa:4336539; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q7XR88; -.
DR OMA; LGNCDNG; -.
DR OrthoDB; 833025at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:UniProtKB.
DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:1901000; P:regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..361
FT /note="Salt tolerance receptor-like cytoplasmic kinase 1"
FT /id="PRO_0000445631"
FT DOMAIN 67..347
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 5
FT /note="C->A: Abnormal cytoplasmic localization and reduced
FT salt tolerance; when associated with A-5 and A-14."
FT /evidence="ECO:0000269|PubMed:29581216"
FT MUTAGEN 10
FT /note="C->A: Abnormal cytoplasmic localization and reduced
FT salt tolerance; when associated with A-10 and A-14."
FT /evidence="ECO:0000269|PubMed:29581216"
FT MUTAGEN 14
FT /note="C->A: Abnormal cytoplasmic localization and reduced
FT salt tolerance; when associated with A-5 and A-10."
FT /evidence="ECO:0000269|PubMed:29581216"
FT MUTAGEN 95
FT /note="K->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:29581216"
SQ SEQUENCE 361 AA; 38394 MW; 35E5A77F9F1B6750 CRC64;
MFTGCGLFAC VRRCDGGDVR KRGEAGAMSS RVAADPAGVE EEGSCKNVAA ASARQLAWAD
VESVTGGFSS RVIGHGGFST VYLASLSSSR LGAVKVHCSS ERLHRAFRQE LEVLLSLRHP
HIVRLLGYCD ERDEGVLVFE YAPNGDLHER LHCSEVAGGV ASVLPWARRV AIAFQVAMAL
EYLHESRHPA VIHGDIKASN VLLDANMNAK LCDFGFAHVG FSATVGCRPS ARAVMGSPGY
VDPHLIRSGV ATKKSDVYSF GVLLLELVTG KEAVCRDTGR RLTAAVGPML SEGKVADVVD
RRLGGEHDGA EAAVMAELAM QCIGDSPGLR PSMADVVRAL QEKTSALASA VGSRLDRKMM
F
