CAMK1_ORYSJ
ID CAMK1_ORYSJ Reviewed; 600 AA.
AC Q10KY3; Q0DRP5; Q94KC3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Calcium/calmodulin-dependent serine/threonine-protein kinase 1;
DE EC=2.7.11.17;
DE AltName: Full=Calcium/calmodulin-binding serine/threonine-protein kinase;
DE Short=CaM-binding protein kinase;
DE AltName: Full=OsCBK;
GN Name=CAMK1; OrderedLocusNames=Os03g0366200, LOC_Os03g25070;
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], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND AUTOPHOSPHORYLATION.
RX PubMed=12160464; DOI=10.1042/bj20020780;
RA Zhang L., Liu B.-F., Liang S., Jones R.L., Lu Y.-T.;
RT "Molecular and biochemical characterization of a calcium/calmodulin-binding
RT protein kinase from rice.";
RL Biochem. J. 368:145-157(2002).
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 FUNCTION, ACTIVITY REGULATION, AND AUTOPHOSPHORYLATION.
RX PubMed=16842786; DOI=10.1016/j.febslet.2006.06.090;
RA Li D.-F., Li J., Ma L., Zhang L., Lu Y.-T.;
RT "Calmodulin isoform-specific activation of a rice calmodulin-binding kinase
RT conferred by only three amino-acids of OsCaM61.";
RL FEBS Lett. 580:4325-4331(2006).
CC -!- FUNCTION: Possesses kinase activity in vitro.
CC {ECO:0000269|PubMed:12160464, ECO:0000269|PubMed:16842786}.
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=2.7.11.17;
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=2.7.11.17;
CC -!- ACTIVITY REGULATION: Activated by the binding of calmodulin-like
CC protein 1 (CML1) in the presence of Ca(2+).
CC {ECO:0000269|PubMed:16842786}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots in the zone of cell
CC division. Expressed in leaf mesophyll cells and at lower levels in
CC mature stems. {ECO:0000269|PubMed:12160464}.
CC -!- DEVELOPMENTAL STAGE: Expressed at early stages of anther development in
CC sporogenous cells and tapetum of anthers. Expression decreases in
CC tapetum and increases in sporogenous cells at meiosis. At mature pollen
CC stage, expressed in stigma, and then in proembryo after fertilization.
CC {ECO:0000269|PubMed:12160464}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF12093.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF368282; AAK54157.1; -; mRNA.
DR EMBL; DP000009; ABF96128.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12093.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015632251.1; XM_015776765.1.
DR AlphaFoldDB; Q10KY3; -.
DR SMR; Q10KY3; -.
DR IntAct; Q10KY3; 2.
DR MINT; Q10KY3; -.
DR STRING; 4530.OS03T0366200-01; -.
DR PaxDb; Q10KY3; -.
DR PRIDE; Q10KY3; -.
DR GeneID; 4332914; -.
DR KEGG; osa:4332914; -.
DR eggNOG; KOG0032; Eukaryota.
DR InParanoid; Q10KY3; -.
DR OrthoDB; 330091at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Calmodulin-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..600
FT /note="Calcium/calmodulin-dependent serine/threonine-
FT protein kinase 1"
FT /id="PRO_0000338447"
FT DOMAIN 147..409
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 153..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 49..51
FT /note="Missing (in Ref. 1; AAK54157)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="E -> G (in Ref. 1; AAK54157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 66279 MW; C4AF86739ED5E701 CRC64;
MGLCHGKSAA VLEPTVEEEE EGATRVAEAA AAPAKPASPA PSAAAAAAAP AKPGTPKQHK
FPFYLPSPLP ASSYKGSPAN SSVASTPARG GFKRPFPPPS PAKHIRALLA RRHGSVKPNE
ASIPESGEPG VALDKGFGFS RHFAAKYELG REVGRGHFGY TCAATCKKGE LKGDDVAVKV
IPKAKMTTAI AIEDVRREVR ILSSLAGHSN LVQFYDAYED EENVYIVMEL CKGGELLDRI
LARGGKYSEE DAKVVMRQIL SVASFCHLQG VVHRDLKPEN FLFSSKDENS AMKVIDFGLS
DFVKPDERLN DIVGSAYYVA PEVLHRSYGT EADMWSIGVI VYILLCGSRP FWARTESGIF
RAVLKADPSF EEAPWPTLSA EAKDFVRRLL NKDYRKRMTA AQALCHPWIR GTEEVKLPLD
MIIYRLMRAY ISSSSLRRAA LRALAKTLTT DQIYYLREQF ELIGPNKSDL ITLQNLKTAL
MKNSTNAMKD SRVVDFVNTI SNIQYRKLDF EEFSAAAISV YQMEGLETWE QHARQAYEFF
DKEGNRPIVI DELASELGLG PSVPLHVVLQ DWIRHPDGKL SFLGFMKLLH GVSSRTIPKT
