CIPKJ_ORYSJ
ID CIPKJ_ORYSJ Reviewed; 508 AA.
AC Q68Y49; B7EGG2; Q9SLZ6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=CBL-interacting protein kinase 19;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK19;
DE AltName: Full=OsPK4;
GN Name=CIPK19; OrderedLocusNames=Os05g0514200, LOC_Os05g43840;
GN ORFNames=P0022D06.5;
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 [GENOMIC DNA], COFACTOR, TISSUE SPECIFICITY, INDUCTION,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-66.
RC STRAIN=cv. Toride;
RX PubMed=10778756; DOI=10.1007/s004380051179;
RA Ohba H., Steward N., Kawasaki S., Berberich T., Ikeda Y., Koizumi N.,
RA Kusano T., Sano H.;
RT "Diverse response of rice and maize genes encoding homologs of WPK4, an
RT SNF1-related protein kinase from wheat, to light, nutrients, low
RT temperature and cytokinins.";
RL Mol. Gen. Genet. 263:359-366(2000).
RN [2]
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 [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 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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14730064; DOI=10.1104/pp.103.033068;
RA Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT "Calcium sensors and their interacting protein kinases: genomics of the
RT Arabidopsis and rice CBL-CIPK signaling networks.";
RL Plant Physiol. 134:43-58(2004).
CC -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK
CC protein lead to the activation of the kinase in a calcium-dependent
CC manner (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10778756};
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf blades and sheaths and
CC panicles. {ECO:0000269|PubMed:10778756}.
CC -!- INDUCTION: By light, nutrient deprivation and N(6)-benzylaminopurine
CC (BA). {ECO:0000269|PubMed:10778756}.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation/activation by upstream protein kinases. The PPI motif
CC mediates the interaction with the ABI (abscisic acid-insensitive)
CC phosphatases (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AB011967; BAA83688.1; -; Genomic_DNA.
DR EMBL; AC132485; AAU03103.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17946.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94871.1; -; Genomic_DNA.
DR EMBL; AK069486; BAG91459.1; -; mRNA.
DR RefSeq; XP_015638753.1; XM_015783267.1.
DR AlphaFoldDB; Q68Y49; -.
DR SMR; Q68Y49; -.
DR STRING; 4530.OS05T0514200-01; -.
DR PaxDb; Q68Y49; -.
DR PRIDE; Q68Y49; -.
DR EnsemblPlants; Os05t0514200-01; Os05t0514200-01; Os05g0514200.
DR GeneID; 4339306; -.
DR Gramene; Os05t0514200-01; Os05t0514200-01; Os05g0514200.
DR KEGG; osa:4339306; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q68Y49; -.
DR OMA; HGESIFE; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q68Y49; OS.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018451; NAF/FISL_domain.
DR InterPro; IPR004041; NAF_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03822; NAF; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50816; NAF; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Manganese; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..508
FT /note="CBL-interacting protein kinase 19"
FT /id="PRO_0000338377"
FT DOMAIN 37..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 354..398
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..206
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 311..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..430
FT /note="PPI"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 66
FT /note="K->D: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:10778756"
SQ SEQUENCE 508 AA; 56913 MW; A033604ED9479A42 CRC64;
MAATPPSSQH RRPLSSSASA ASLAGKPRGG GLLLGRYELG RLLGHGTFAK VYQARSADSG
EPVAIKVLDK EKAMRHGLVP HIKREIAILR RVRHPNIVRL FEVMATKSKI YFVMELVRGG
ELFGRVAKGR LKEDTARRYF QQLVSAVGFC HARGVFHRDL KPENLLVDEH GDLKVSDFGL
SAVADQFHPD GLLHTFCGTP SYVAPEVLAR RGYDGAKADI WSCGIILFVL MAGYLPFHDQ
NLMAMYRKIY RGEFRCPRWF SKDLSSLLNR ILDTNPETRI TVKEVMESRW FQKGFRPVRF
YVEDDQVHSL ADGDNDMPEL EPSEPPPPPP FPPPPPQQDD DGEESGWESD SSVASCPATL
SSEERRQRPL GSLTRPASLN AFDIISFSKG FDLSGLFEER GSEVRFISAE PMQTIITKLE
EIAKVKSFFV RRKDWRVSIE GTREGLKGPL TIGAEIFELT PSLVVVEVKK KAGDKEEYDD
FCNRELKPGM QHLVHHMGSV PNIPSDTE
