OSK4_ORYSI
ID OSK4_ORYSI Reviewed; 509 AA.
AC B8BBT7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Serine/threonine protein kinase OSK4 {ECO:0000250|UniProtKB:Q852Q1};
DE Short=OsK4 {ECO:0000250|UniProtKB:Q852Q1};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q852Q1};
GN Name=OSK4 {ECO:0000250|UniProtKB:Q852Q1};
GN ORFNames=OsI_29652 {ECO:0000312|EMBL:EEC83761.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
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:0000250|UniProtKB:Q852Q1}.
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:Q852Q1};
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:Q852Q1};
CC -!- SUBUNIT: Interacts with HDR1. {ECO:0000250|UniProtKB:Q852Q1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q852Q1}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in immature seeds. Mostly
CC expressed in panicles, leaf sheaths and roots, and to a lower extent,
CC in germinating seeds and leaf blades. {ECO:0000250|UniProtKB:Q852Q1}.
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; CM000133; EEC83761.1; -; Genomic_DNA.
DR AlphaFoldDB; B8BBT7; -.
DR SMR; B8BBT7; -.
DR STRING; 39946.B8BBT7; -.
DR iPTMnet; B8BBT7; -.
DR EnsemblPlants; BGIOSGA028869-TA; BGIOSGA028869-PA; BGIOSGA028869.
DR Gramene; BGIOSGA028869-TA; BGIOSGA028869-PA; BGIOSGA028869.
DR HOGENOM; CLU_000288_59_3_1; -.
DR OMA; DSFMEEP; -.
DR Proteomes; UP000007015; 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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..509
FT /note="Serine/threonine protein kinase OSK4"
FT /id="PRO_0000438042"
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
