OSK4_ORYSJ
ID OSK4_ORYSJ Reviewed; 509 AA.
AC Q852Q1; Q9ZRJ3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Serine/threonine protein kinase OSK4 {ECO:0000303|PubMed:9870704};
DE Short=OsK4 {ECO:0000303|PubMed:9870704};
DE EC=2.7.11.1 {ECO:0000269|PubMed:9870704};
DE AltName: Full=SUCROSE NON-FERMENTING-1 related protein kinase 1B {ECO:0000303|PubMed:17766403};
DE Short=SNF1-related kinase 1B {ECO:0000303|PubMed:17766403};
DE Short=SnRK1B {ECO:0000303|PubMed:17766403};
DE AltName: Full=Serine/threonine protein kinase OSK24 {ECO:0000303|PubMed:16087344};
DE Short=OsK24 {ECO:0000303|PubMed:16087344};
GN Name=OSK4 {ECO:0000303|PubMed:9870704};
GN Synonyms=OSK24 {ECO:0000303|PubMed:16087344},
GN SNRK1B {ECO:0000303|PubMed:17766403};
GN OrderedLocusNames=LOC_Os08g37800 {ECO:0000305},
GN Os08g0484600 {ECO:0000312|EMBL:BAF23997.1};
GN ORFNames=OsJ_27714 {ECO:0000312|EMBL:EEE68886.1},
GN OSNPB_080484600 {ECO:0000312|EMBL:BAT05960.1},
GN P0419H09.18 {ECO:0000312|EMBL:BAD10710.1};
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,
RP DEVELOPMENTAL STAGE, GENE 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=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 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 [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 DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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).
RN [9]
RP FUNCTION, INTERACTION WITH HDR1, AND SUBCELLULAR LOCATION.
RX PubMed=26954091; DOI=10.1371/journal.pgen.1005927;
RA Sun X., Zhang Z., Wu J., Cui X., Feng D., Wang K., Xu M., Zhou L., Han X.,
RA Gu X., Lu T.;
RT "The Oryza sativa regulator HDR1 associates with the kinase OsK4 to control
RT photoperiodic flowering.";
RL PLoS Genet. 12:E1005927-E1005927(2016).
CC -!- FUNCTION: Suppressor of flowering in long days (LD) via the that up-
CC regulation of HD1 and the down-regulation of EHD1. Can phosphorylate
CC HD1 in the presence of HDR1. {ECO:0000269|PubMed:26954091}.
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 -!- SUBUNIT: Interacts with HDR1. {ECO:0000269|PubMed:26954091}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26954091}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in immature seeds
CC (PubMed:9870704). Mostly expressed in panicles, leaf sheaths and roots,
CC and to a lower extent, in germinating seeds and leaf blades
CC (PubMed:16087344). {ECO:0000269|PubMed:16087344,
CC ECO:0000269|PubMed:9870704}.
CC -!- DEVELOPMENTAL STAGE: Accumulates transiently in the early stages of
CC seed maturation (PubMed:9870704). Observed in maturating caryopsis 1
CC week after flowering (DAF). Expressed in tissues where and when starch
CC granules appear. Detected in the pericarp at the early stage with a
CC shift to the endosperm as the endosperm cells are formed. Confined to
CC both aleurone layer and endosperm cells around 15 days after flowering.
CC Also present in the basal part of leaf sheath (PubMed:16087344).
CC {ECO:0000269|PubMed:16087344, ECO:0000269|PubMed:9870704}.
CC -!- DISRUPTION PHENOTYPE: Normal expression of MYBS1 and AAMY3 in response
CC to glucose levels. Normal 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}.
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DR EMBL; D82035; BAA36299.1; -; mRNA.
DR EMBL; AB101656; BAC56589.1; -; Genomic_DNA.
DR EMBL; AP005918; BAD10710.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23997.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05960.1; -; Genomic_DNA.
DR EMBL; CM000145; EEE68886.1; -; Genomic_DNA.
DR EMBL; AK072723; BAG93115.1; -; mRNA.
DR EMBL; AK100591; BAG94669.1; -; mRNA.
DR RefSeq; XP_015650152.1; XM_015794666.1.
DR AlphaFoldDB; Q852Q1; -.
DR SMR; Q852Q1; -.
DR STRING; 4530.OS08T0484600-01; -.
DR PaxDb; Q852Q1; -.
DR PRIDE; Q852Q1; -.
DR EnsemblPlants; Os08t0484600-01; Os08t0484600-01; Os08g0484600.
DR GeneID; 4345873; -.
DR Gramene; Os08t0484600-01; Os08t0484600-01; Os08g0484600.
DR KEGG; osa:4345873; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; Q852Q1; -.
DR OMA; DSFMEEP; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
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 Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 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..509
FT /note="Serine/threonine protein kinase OSK4"
FT /id="PRO_0000438041"
FT DOMAIN 17..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 290..330
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 460..508
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 23..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 509 AA; 58471 MW; 6E82566D715A1B48 CRC64;
MEGNARGGGH SEALKNYNLG RTLGIGSFGK VKIAEHKLTG HRVAIKILNR RQMRNMEMEE
KAKREIKILR LFIHPHIIRL YEVIYTPTDI YVVMEYCKFG ELFDYIVEKG RLQEDEARRI
FQQIISGVEY CHRNMVVHRD LKPENLLLDS KYNVKLADFG LSNVMHDGHF LKTSCGSPNY
AAPEVISGKL YAGPEVDVWS CGVILYALLC GTLPFDDENI PNLFKKIKGG IYTLPSHLSA
LARDLIPRML VVDPMKRITI REIREHQWFQ IRLPRYLAVP PPDTAQQAKM IDEDTLQDVV
NLGYEKDHVC ESLRNRLQNE ATVAYYLLLD NRFRATSGYL GADYQESLER NLNRFASSES
ASSNTRHYLP GSSDPHASGL RPHYPVERKW ALGLQSRAQP REIMIEVLKA LEDLNVCWKK
NGQYNMKCRW SVGYPQATDM LDVNHSFVDD SIIMDNGDVN GRLPAVIKFE IQLYKSRDEK
YLLDMQRVTG PQLLFLDFCA AFLTKLRVL
