CIPKV_ORYSJ
ID CIPKV_ORYSJ Reviewed; 449 AA.
AC Q6X4A2; Q10M86; Q10M87;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=CBL-interacting protein kinase 31;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK31;
DE Short=OsCK1;
GN Name=CIPK31; Synonyms=CK1; OrderedLocusNames=Os03g0319400, LOC_Os03g20380;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DOMAIN,
RP INDUCTION, COFACTOR, PHOSPHORYLATION, AND INTERACTION WITH CBL3.
RC STRAIN=cv. Ilpoom; TISSUE=Leaf;
RX PubMed=14682618; DOI=10.1023/b:plan.0000004330.62660.a2;
RA Kim K.-N., Lee J.-S., Han H., Choi S.A., Go S.J., Yoon I.S.;
RT "Isolation and characterization of a novel rice Ca2+-regulated protein
RT kinase gene involved in responses to diverse signals including cold, light,
RT cytokinins, sugars and salts.";
RL Plant Mol. Biol. 52:1191-1202(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(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 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 [7]
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 cold 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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14682618};
CC -!- SUBUNIT: May interact with CBL3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6X4A2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6X4A2-2; Sequence=VSP_034046;
CC Name=3;
CC IsoId=Q6X4A2-3; Sequence=VSP_034047, VSP_034048;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaf blade and leaf sheath, but
CC not in other tissues. {ECO:0000269|PubMed:14682618}.
CC -!- INDUCTION: By salt, cold, calcium, sucrose and cytokinins in young
CC seedlings, and by light in the shoot of etiolated seedlings. Induction
CC by cold inhibited by the calcium ionophore A23187. Induction by calcium
CC inhibited by the Ca(2+)-channel blocker La(3+), and by A23187.
CC {ECO:0000269|PubMed:14682618, ECO:0000269|PubMed:17535819}.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation/activation by upstream protein kinases (By similarity).
CC The N-terminal region containing the kinase domain is responsible for
CC the autophosphorylation. {ECO:0000250, ECO:0000269|PubMed:14682618}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:14682618}.
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; AY256847; AAP82174.1; -; mRNA.
DR EMBL; DP000009; ABF95647.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF95650.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11863.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83925.1; -; Genomic_DNA.
DR RefSeq; XP_015631096.1; XM_015775610.1. [Q6X4A2-1]
DR AlphaFoldDB; Q6X4A2; -.
DR SMR; Q6X4A2; -.
DR STRING; 4530.OS03T0319400-01; -.
DR PaxDb; Q6X4A2; -.
DR PRIDE; Q6X4A2; -.
DR EnsemblPlants; Os03t0319400-01; Os03t0319400-01; Os03g0319400. [Q6X4A2-1]
DR GeneID; 4332665; -.
DR Gramene; Os03t0319400-01; Os03t0319400-01; Os03g0319400. [Q6X4A2-1]
DR KEGG; osa:4332665; -.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q6X4A2; -.
DR OMA; RNTDDIE; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q6X4A2; baseline and differential.
DR Genevisible; Q6X4A2; 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; IPR028375; KA1/Ssp2_C.
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; SSF103243; SSF103243; 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 Alternative splicing; ATP-binding; Calcium; Kinase; Manganese;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..449
FT /note="CBL-interacting protein kinase 31"
FT /id="PRO_0000085862"
FT DOMAIN 20..275
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 313..337
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 161..190
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 173..190
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034046"
FT VAR_SEQ 379..381
FT /note="MRM -> VFI (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034047"
FT VAR_SEQ 382..449
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034048"
SQ SEQUENCE 449 AA; 50954 MW; 2697224053973D41 CRC64;
MYRAKRAALS PKVKRRVGKY ELGRTIGEGT FAKVRFAKNT ENDEPVAIKI LDKEKVQKHR
LVEQIRREIC TMKLVKHPNV VRLFEVMGSK ARIFIVLEYV TGGELFEIIA TNGRLKEEEA
RKYFQQLINA VDYCHSRGVY HRDLKLENLL LDASGNLKVS DFGLSALTEQ VKADGLLHTT
CGTPNYVAPE VIEDRGYDGA AADIWSCGVI LYVLLAGFLP FEDDNIIALY KKISEAQFTC
PSWFSTGAKK LITRILDPNP TTRITISQIL EDPWFKKGYK PPVFDEKYET SFDDVDAAFG
DSEDRHVKEE TEDQPTSMNA FELISLNQAL NLDNLFEAKK EYKRETRFTS QCPPKEIITK
IEEAAKPLGF DIQKKNYKMR MENLKAGRKG NLNVATEVFQ VAPSLHVVEL KKAKGDTLEF
QKFYRTLSTQ LKDVVWKCDG EVEGNGAAA
