CIPK3_ORYSJ
ID CIPK3_ORYSJ Reviewed; 445 AA.
AC Q8LIG4; A0A0N7KP33;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=CBL-interacting protein kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK03;
GN Name=CIPK3; OrderedLocusNames=Os07g0687000, LOC_Os07g48760;
GN ORFNames=OJ1150_E04.118, OJ1200_C08.122, OsJ_024629;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP 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: 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; Evidence={ECO:0000250};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF22603.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003813; BAD30291.1; -; Genomic_DNA.
DR EMBL; AP003818; BAC10350.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22603.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014963; BAT03298.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ41146.1; -; Genomic_DNA.
DR RefSeq; XP_015646748.1; XM_015791262.1.
DR AlphaFoldDB; Q8LIG4; -.
DR SMR; Q8LIG4; -.
DR STRING; 4530.OS07T0687000-00; -.
DR PaxDb; Q8LIG4; -.
DR PRIDE; Q8LIG4; -.
DR EnsemblPlants; Os07t0687000-01; Os07t0687000-01; Os07g0687000.
DR GeneID; 4344342; -.
DR Gramene; Os07t0687000-01; Os07t0687000-01; Os07g0687000.
DR KEGG; osa:4344342; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q8LIG4; -.
DR OMA; MNAFEFI; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q8LIG4; 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Manganese; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..445
FT /note="CBL-interacting protein kinase 3"
FT /id="PRO_0000338361"
FT DOMAIN 19..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 309..336
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 160..189
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 342..371
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 445 AA; 50952 MW; 45D0CB10F2D46FAF CRC64;
MYKAKRTAAQ KVRRCLGKYE LGRAIGQGTF AKVRFAKNME TGDHVAIKIL DKAKVQKHRL
VEQIRREICT MKLIQHPNVV HLHEVMGSKT RIFIVLEYVM GGELHDIIAT SGRLKEDEAR
KYFQQLINAV DYCHSRGVYH RDLKLENLLL DTAGNIKVSD FGLSAISEQV KADGLLHTTC
GTPNYVAPEV IEDKGYDGAL ADLWSCGVIL FVLLAGYLPF EDENIVSLYN KISGAQFTCP
SWFSAEAKRL IARILDPNPA TRITTSQVLQ DQWFKKGYES PVFDDKYYPY FHDVYDAFGD
SEEKHVKEAM EEQPTLMNAF ELISLNKGLN LDNFFESDKK YKRETRFTSQ CPPKEIINRI
EEAANLLGFN IQKRNYRMRM ENIKEGRKGH LNIATEVFQV APSLHVVELK KAKGDTLEFQ
KFYQTLSTQL KDVVWELEDA AEDMS
