OSK1_ORYSJ
ID OSK1_ORYSJ Reviewed; 505 AA.
AC Q852Q2; Q0DGI1; Q9ZRJ1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine/threonine protein kinase OSK1 {ECO:0000303|PubMed:9870704};
DE Short=OsK1 {ECO:0000303|PubMed:9870704};
DE EC=2.7.11.1 {ECO:0000269|PubMed:9870704};
DE AltName: Full=SUCROSE NON-FERMENTING-1 related protein kinase 1A {ECO:0000303|PubMed:17766403};
DE Short=SNF1-related kinase 1A {ECO:0000303|PubMed:17766403};
DE Short=SnRK1A {ECO:0000303|PubMed:17766403};
GN Name=OSK1 {ECO:0000303|PubMed:16087344, ECO:0000303|PubMed:9870704};
GN Synonyms=SNRK1A {ECO:0000303|PubMed:17766403};
GN OrderedLocusNames=LOC_Os05g45420 {ECO:0000305},
GN Os05g0530500 {ECO:0000312|EMBL:BAS95028.1};
GN ORFNames=OJ1131_E09.11 {ECO:0000312|EMBL:AAS72352.1},
GN OSNPB_050530500 {ECO:0000312|EMBL:BAS95028.1};
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], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, GENE
RP FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Nohrin 8;
RX PubMed=9870704; DOI=10.1007/s004380050908;
RA Takano M., Kajiya-Kanegae H., Funatsuki H., Kikuchi S.;
RT "Rice has two distinct classes of protein kinase genes related to SNF1 of
RT Saccharomyces cerevisiae, which are differently regulated in early seed
RT development.";
RL Mol. Gen. Genet. 260:388-394(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND GENE FAMILY.
RC STRAIN=cv. Nohrin 8;
RX PubMed=16087344; DOI=10.1016/j.plaphy.2005.06.004;
RA Kanegae H., Miyoshi K., Hirose T., Tsuchimoto S., Mori M., Nagato Y.,
RA Takano M.;
RT "Expressions of rice sucrose non-fermenting-1 related protein kinase 1
RT genes are differently regulated during the caryopsis development.";
RL Plant Physiol. Biochem. 43:669-679(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY GLUCOSE STARVATION.
RC STRAIN=cv. Tainung 67;
RX PubMed=17766403; DOI=10.1105/tpc.105.037887;
RA Lu C.-A., Lin C.-C., Lee K.-W., Chen J.-L., Huang L.-F., Ho S.-L.,
RA Liu H.-J., Hsing Y.-I., Yu S.-M.;
RT "The SnRK1A protein kinase plays a key role in sugar signaling during
RT germination and seedling growth of rice.";
RL Plant Cell 19:2484-2499(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in sugar signaling
CC during germination and seedling growth. Negative regulators of sugar
CC response complex (SRC) in alpha-amylase gene promoters, thus relieving
CC SRC sugar repression in a MYBS1-dependent manner. Required for MYBS1
CC and AAMY3 accumulation under glucose starvation.
CC {ECO:0000269|PubMed:17766403}.
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:9870704};
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:9870704};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q852Q1}.
CC -!- TISSUE SPECIFICITY: Expressed in young roots, young shoots, flowers,
CC and immature seeds (PubMed:9870704). Mostly expressed in leaf sheaths
CC and roots, and to a lower extent, in germinating seeds, leaf blades and
CC panicles (PubMed:16087344). {ECO:0000269|PubMed:16087344,
CC ECO:0000269|PubMed:9870704}.
CC -!- DEVELOPMENTAL STAGE: Nearly restricted in the vascular tissues during
CC the caryopsis development. Observed in maturating caryopsis 2 days
CC after flowering (DAF). {ECO:0000269|PubMed:16087344}.
CC -!- INDUCTION: By glucose starvation (at protein level).
CC {ECO:0000269|PubMed:17766403}.
CC -!- DISRUPTION PHENOTYPE: Reduced expression of MYBS1 and AAMY3 under
CC glucose starvation. Accumulation of MYBS1 and AAMY3 in the presence of
CC glucose. Retarded seed germination and seedling growth.
CC {ECO:0000269|PubMed:17766403}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF18042.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D82039; BAA36298.1; -; mRNA.
DR EMBL; AB101655; BAC56588.1; -; Genomic_DNA.
DR EMBL; AC111015; AAS72352.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18042.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS95028.1; -; Genomic_DNA.
DR EMBL; AK067158; BAG90292.1; -; mRNA.
DR RefSeq; XP_015639849.1; XM_015784363.1.
DR RefSeq; XP_015639850.1; XM_015784364.1.
DR AlphaFoldDB; Q852Q2; -.
DR SMR; Q852Q2; -.
DR STRING; 4530.OS05T0530500-02; -.
DR PaxDb; Q852Q2; -.
DR PRIDE; Q852Q2; -.
DR EnsemblPlants; Os05t0530500-02; Os05t0530500-02; Os05g0530500.
DR GeneID; 4339410; -.
DR Gramene; Os05t0530500-02; Os05t0530500-02; Os05g0530500.
DR KEGG; osa:4339410; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; Q852Q2; -.
DR OMA; HHFTRPH; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q852Q2; baseline and differential.
DR GO; GO:0005634; C:nucleus; 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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..505
FT /note="Serine/threonine protein kinase OSK1"
FT /id="PRO_0000438038"
FT DOMAIN 14..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 287..327
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 456..504
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 347..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 505 AA; 57615 MW; 5631D07F591FD951 CRC64;
MEGAGRDGNP LGGYRIGKTL GIGSFGKVKI AEHILTGHKV AIKILNRRKI KSMEMEEKVK
REIKILRLFM HPHIIRLYEV IDTPADIYVV MEYVKSGELF DYIVEKGRLQ EEEARRFFQQ
IISGVEYCHR NMVVHRDLKP ENLLLDSKCN VKIADFGLSN VMRDGHFLKT SCGSPNYAAP
EVISGKLYAG PEVDVWSCGV ILYALLCGTL PFDDENIPNL FKKIKGGIYT LPSHLSPLAR
DLIPRMLVVD PMKRITIREI REHQWFTVGL PRYLAVPPPD TAQQVKKLDD ETLNDVINMG
FDKNQLIESL HKRLQNEATV AYYLLLDNRL RTTSGYLGAE FHESMESSLA QVTPAETPNS
ATDHRQHGHM ESPGFGLRHH FAADRKWALG LQSRAHPREI ITEVLKALQE LNVCWKKIGH
YNMKCRWSPS FPSHESMMHN NHGFGAESAI IETDDSEKST HTVKFEIQLY KTRDEKYLLD
LQRVSGPQLL FLDLCSAFLT QLRVL
