CIPKC_ORYSJ
ID CIPKC_ORYSJ Reviewed; 540 AA.
AC Q5JLS2; Q7F595; Q9SLZ5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=CBL-interacting protein kinase 12;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK12;
DE AltName: Full=OsPK7;
GN Name=CIPK12; OrderedLocusNames=Os01g0759400, LOC_Os01g55450;
GN ORFNames=B1131G08.38, P0460E08.9;
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, AND
RP AUTOPHOSPHORYLATION.
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=17535819; DOI=10.1104/pp.107.101295;
RA Xiang Y., Huang Y., Xiong L.;
RT "Characterization of stress-responsive CIPK genes in rice for stress
RT tolerance improvement.";
RL Plant Physiol. 144:1416-1428(2007).
CC -!- FUNCTION: Involved in drought stress tolerance. CIPK serine-threonine
CC protein kinases interact with CBL proteins. Binding of a CBL protein to
CC the regulatory NAF domain of CIPK protein lead to the activation of the
CC kinase in a calcium-dependent manner. {ECO:0000269|PubMed:17535819}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10778756};
CC -!- TISSUE SPECIFICITY: Expressed at low levels in leaf blades.
CC {ECO:0000269|PubMed:10778756}.
CC -!- INDUCTION: By drought stress and abscisic acid (ABA).
CC {ECO:0000269|PubMed:17535819}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83689.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB61201.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB011968; BAA83689.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP003256; BAB61201.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP003409; BAD87598.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06225.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS74440.1; -; Genomic_DNA.
DR EMBL; AK101442; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015616887.1; XM_015761401.1.
DR AlphaFoldDB; Q5JLS2; -.
DR SMR; Q5JLS2; -.
DR STRING; 4530.OS01T0759400-02; -.
DR PaxDb; Q5JLS2; -.
DR PRIDE; Q5JLS2; -.
DR EnsemblPlants; Os01t0759400-02; Os01t0759400-02; Os01g0759400.
DR GeneID; 4325613; -.
DR Gramene; Os01t0759400-02; Os01t0759400-02; Os01g0759400.
DR KEGG; osa:4325613; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q5JLS2; -.
DR OMA; HDQNVMV; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q5JLS2; baseline and differential.
DR Genevisible; Q5JLS2; 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..540
FT /note="CBL-interacting protein kinase 12"
FT /id="PRO_0000338370"
FT DOMAIN 46..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 370..406
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..215
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 333..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..438
FT /note="PPI"
FT /evidence="ECO:0000250"
FT COMPBIAS 333..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 52..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 540 AA; 59808 MW; 338C6E62C9CC70E6 CRC64;
MLMATVSPAR REPTPQAVRA SPMPSAAAAL VRRGGGGSGG TVLGKYELGR VLGQGSFAKV
YQARHLETDE CVAIKVLDKE KAVKGGMVHL VKREINVLRR VRHPNIVQLF EVMASKTKIY
FVMEYVRGGE LFSRVSKGRL REDTARRYFQ QLVSAVDFCH ARGVFHRDLK PENLLVDENG
DLKVSDFGLA AGPDQFDPDG LLHTFCGTPA YVAPEVLRRR GYDGAKADIW SCGVILFALM
AGYLPFHDHN IMVLYRKIYN GEFRCPRWFS KDFTRLITRL LDANPKTRIT VPEIIESDWF
KKGYKPVKFY IEDDKLYNLS DDVLNLEPAD PVPPPLGLAP PVPPPPQGDD PDGSGSESDS
SVVSCPATLS TGESQRVRGS LPRPASLNAF DIISFSKGFN LSGLFEERGN EIRFVSGEPM
SDIVKKLEEI AKVKSFTVRR KDWRVSIEGT REGVKGPLTI GAEIFELTPS LVVVEVKRKA
GDNEEYEDFC NMELKPGMQH LVHQMLPAPN GTPVSEKVER SSSLQAPLTL KLIGTEGSMS
