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CIPK4_ORYSJ
ID   CIPK4_ORYSJ             Reviewed;         454 AA.
AC   Q2QMI0; Q0IM32;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=CBL-interacting protein kinase 4;
DE            EC=2.7.11.1;
DE   AltName: Full=OsCIPK04;
GN   Name=CIPK4; OrderedLocusNames=Os12g0603700, LOC_Os12g41090;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
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   [3]
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   [4]
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   [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   -!- INDUCTION: By salt stress. {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   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF30233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DP000011; ABA99814.2; -; Genomic_DNA.
DR   EMBL; AP008218; BAF30233.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015618702.1; XM_015763216.1.
DR   AlphaFoldDB; Q2QMI0; -.
DR   SMR; Q2QMI0; -.
DR   STRING; 4530.OS12T0603700-00; -.
DR   PaxDb; Q2QMI0; -.
DR   PRIDE; Q2QMI0; -.
DR   GeneID; 4352728; -.
DR   KEGG; osa:4352728; -.
DR   InParanoid; Q2QMI0; -.
DR   OrthoDB; 1127668at2759; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
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..454
FT                   /note="CBL-interacting protein kinase 4"
FT                   /id="PRO_0000338362"
FT   DOMAIN          25..284
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          311..335
FT                   /note="NAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT   REGION          169..198
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   REGION          341..370
FT                   /note="PPI"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         31..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   454 AA;  49057 MW;  C871D6B83D613656 CRC64;
     MAMAAMDARK KKSGGGGGEP LLGKYELGRM LGRGTFAKVY LARAVAGGEA VAVKVIDKAE
     VMGTAGMAPR VLREVAAMRR LRHPHVLRLH EVLATRARIY LVMELATGGD LLSRLAALPR
     RRLPESAARR VFVQLVDALS YCHARGVAHR DVKPQNVLLD GDGNLKVSDF GLAALPDTLR
     DDGRLHTACG TPAYAAPEVL RRRAYDGAKA DAWSCGVILF VLLAGHLPFD DSNIADMCRK
     AHRREYELPR WVSQPARRLV SRLLDPNPDT RVAVESLAAH HPWFKRSLSV DSQLDGLLNG
     EPERAVAFQA APPPPLNAFD IISMSPGLDL SGLFGEHDKS LREKRFTTTA SPEKTLEQLG
     LAGGKLGYVV VVGKKGVECL PLAGGRLSSG IAAMSVEMSE VAPPLLLVEL RLEVAAGDVD
     GGDGEVKGFG WEQLRMELGD VVRAWHSCED LCEI
 
 
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