CIPKP_ORYSJ
ID CIPKP_ORYSJ Reviewed; 514 AA.
AC Q5Z6X0; A0A0P0WXH2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=CBL-interacting protein kinase 25;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK25;
GN Name=CIPK25; OrderedLocusNames=Os06g0543400, LOC_Os06g35160;
GN ORFNames=B1068H08.30, P0007G12.2;
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 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 [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).
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}.
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DR EMBL; AP003608; BAD53535.1; -; Genomic_DNA.
DR EMBL; AP004810; BAD54299.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19725.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98138.1; -; Genomic_DNA.
DR EMBL; AK065374; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015641263.1; XM_015785777.1.
DR AlphaFoldDB; Q5Z6X0; -.
DR SMR; Q5Z6X0; -.
DR STRING; 4530.OS06T0543400-01; -.
DR PaxDb; Q5Z6X0; -.
DR PRIDE; Q5Z6X0; -.
DR EnsemblPlants; Os06t0543400-01; Os06t0543400-01; Os06g0543400.
DR GeneID; 4341236; -.
DR Gramene; Os06t0543400-01; Os06t0543400-01; Os06g0543400.
DR KEGG; osa:4341236; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q5Z6X0; -.
DR OMA; MFIAPEV; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z6X0; 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Manganese; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..514
FT /note="CBL-interacting protein kinase 25"
FT /id="PRO_0000338383"
FT DOMAIN 21..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 323..395
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 167..196
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 303..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..427
FT /note="PPI"
FT /evidence="ECO:0000250"
FT COMPBIAS 315..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 89
FT /note="A -> V (in Ref. 4; AK065374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 56980 MW; 2079995BD68F6FA0 CRC64;
MFRSMGTGTG TKPPAMTTER YEFGPLVGEG NFAKVYLGRH RATGEEVAIK VMDKEKLVRL
GATELIKREI AVMQRLRHPN VVRIHEVMAN KRRICVVMEY VRGGALYRYF RRGPSGGAAG
LREHEARRFF QQLVSAVAYC HSRGVFHRDI KLDNLLVDEQ GNLKVADFGL SALADMERRE
AHLQTVCGTP LFLAPEVFKR RGYDGAKADV WACGVVLYVL LTGRKPFPDE HVSRLYRLIG
QNQFQCPPSF SPDLARLVRR LLQPDPDRRI TIPEIMEMRW FKRGFKEVTY YIDSNDRLRS
LDGLDGEPEL YDSDTDTIES SSSSESPTPV AGTPRGMHTS VSAPALSELD RMEDSASLPL
PLPLPPRPRM PRPKSLNAFD IIASSPSFDL SGLFEERGER MRFVSGAPVA DIIAKLQEIA
GMVSFTARTK DCQVSIEATR NGQKGALAIS AKVFELTREL VMVQVCKKAG DTAEYRRFCD
NELKAGLRGL VVDALPPPVE GGGHGGAAAA AEAE
