CCAMK_LOTJA
ID CCAMK_LOTJA Reviewed; 518 AA.
AC A0AAR7; I3SBM2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase;
DE Short=LjCCaMK;
DE EC=2.7.11.17;
GN Name=CCAMK;
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF SER-25;
RP GLY-30 AND THR-265, PHOSPHORYLATION AT THR-265, TISSUE SPECIFICITY, AND
RP ACTIVITY REGULATION.
RX PubMed=16810257; DOI=10.1038/nature04862;
RA Tirichine L., Imaizumi-Anraku H., Murakami Y., Yoshida S., Madsen L.H.,
RA Miwa H., Nakagawa T., Sandal N., Albrektsen A.S., Kawaguchi M., Downie A.,
RA Sato S., Tabata S., Kouchi H., Parniske M., Kawasaki S., Stougaard J.;
RT "Deregulation of a Ca2+/calmodulin-dependent kinase leads to spontaneous
RT nodule development.";
RL Nature 441:1153-1156(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MUTAGENESIS OF THR-265.
RX PubMed=18852152; DOI=10.1093/pcp/pcn153;
RA Banba M., Gutjahr C., Miyao A., Hirochika H., Paszkowski U., Kouchi H.,
RA Imaizumi-Anraku H.;
RT "Divergence of evolutionary ways among common sym genes: CASTOR and CCaMK
RT show functional conservation between two symbiosis systems and constitute
RT the root of a common signaling pathway.";
RL Plant Cell Physiol. 49:1659-1671(2008).
RN [4]
RP FUNCTION, INTERACTION WITH IPD3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-30 AND LYS-44.
RX PubMed=19074278; DOI=10.1073/pnas.0806858105;
RA Yano K., Yoshida S., Mueller J., Singh S., Banba M., Vickers K.,
RA Markmann K., White C., Schuller B., Sato S., Asamizu E., Tabata S.,
RA Murooka Y., Perry J., Wang T.L., Kawaguchi M., Imaizumi-Anraku H.,
RA Hayashi M., Parniske M.;
RT "CYCLOPS, a mediator of symbiotic intracellular accommodation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20540-20545(2008).
RN [5]
RP FUNCTION, INTERACTION WITH CIP73 AND IPD3, AND SUBCELLULAR LOCATION.
RX PubMed=21209278; DOI=10.1104/pp.110.167965;
RA Kang H., Zhu H., Chu X., Yang Z., Yuan S., Yu D., Wang C., Hong Z.,
RA Zhang Z.;
RT "A novel interaction between CCaMK and a protein containing the Scythe_N
RT ubiquitin-like domain in Lotus japonicus.";
RL Plant Physiol. 155:1312-1324(2011).
CC -!- FUNCTION: Calcium- and calmodulin-dependent protein kinase necessary
CC and sufficient for dedifferentiation of root cortical cells into nodule
CC initials. Not required for calcium spiking (PubMed:16810257). Acts as
CC central regulator of the nodule organogenesis program. Required for
CC root hair curling and infection thread (IT) formation upon rhizobial
CC infection, and arbuscule formation during arbuscular mycorrhiza (AM)
CC fungal infection. Phosphorylates the downstream target IPD3, a protein
CC required for root infection by symbiotic rhizobia and AM fungi
CC (PubMed:19074278). Phosphorylates the downstream target CIP73, a
CC protein required for root nodule organogenesis (PubMed:21209278).
CC {ECO:0000269|PubMed:16810257, ECO:0000269|PubMed:19074278,
CC ECO:0000269|PubMed:21209278}.
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 calcium/calmodulin binding after
CC calcium-induced autophosphorylation. {ECO:0000269|PubMed:16810257}.
CC -!- SUBUNIT: Interacts with IPD3 (PubMed:19074278, PubMed:21209278).
CC Interacts with CIP73 (PubMed:21209278). {ECO:0000269|PubMed:19074278,
CC ECO:0000269|PubMed:21209278}.
CC -!- INTERACTION:
CC A0AAR7; A9XMT3: IPD3; NbExp=4; IntAct=EBI-15746225, EBI-15746220;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19074278,
CC ECO:0000269|PubMed:21209278}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots and nodules. Detected in
CC leaves, stems and cotyledons. {ECO:0000269|PubMed:16810257}.
CC -!- INDUCTION: Very low up-regulation 8 days after inoculation with
CC bacteria.
CC -!- PTM: Autophosphorylation stimulated by calcium. Occurs probably by an
CC intermolecular mechanism. {ECO:0000269|PubMed:16810257}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AM230792; CAJ76699.1; -; Genomic_DNA.
DR EMBL; AM230793; CAJ76700.1; -; mRNA.
DR EMBL; BT137869; AFK37664.1; -; mRNA.
DR AlphaFoldDB; A0AAR7; -.
DR SMR; A0AAR7; -.
DR DIP; DIP-48655N; -.
DR IntAct; A0AAR7; 1.
DR iPTMnet; A0AAR7; -.
DR PRIDE; A0AAR7; -.
DR OMA; KQQMIMA; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0009608; P:response to symbiont; IDA:UniProtKB.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
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; Calcium; Calmodulin-binding; Coiled coil; Kinase;
KW Metal-binding; Nodulation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..518
FT /note="Calcium and calcium/calmodulin-dependent
FT serine/threonine-protein kinase"
FT /id="PRO_0000395510"
FT DOMAIN 13..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 394..429
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 430..465
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 472..507
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 323..336
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COILED 344..365
FT /evidence="ECO:0000255"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 487
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16810257"
FT MUTAGEN 25
FT /note="S->F: In ccamk-4. Loss of function; no nodulation."
FT /evidence="ECO:0000269|PubMed:16810257"
FT MUTAGEN 30
FT /note="G->E: In ccamk-3; Loss of autophosphorylation and
FT loss of function; no nodulation. Abolishes binding to
FT IPD3."
FT /evidence="ECO:0000269|PubMed:16810257,
FT ECO:0000269|PubMed:19074278"
FT MUTAGEN 44
FT /note="K->A: Loss of catalytic activity. Abolishes binding
FT to IPD3."
FT /evidence="ECO:0000269|PubMed:19074278"
FT MUTAGEN 265
FT /note="T->I,D: Constitutive activity and loss of
FT calcium/calmodulin regulation. Loss of autophosphorylation.
FT Spontaneous nodulation in the absence of rhizobial
FT infection."
FT /evidence="ECO:0000269|PubMed:16810257,
FT ECO:0000269|PubMed:18852152"
FT CONFLICT 167
FT /note="K -> E (in Ref. 2; AFK37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="G -> W (in Ref. 2; AFK37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="K -> E (in Ref. 2; AFK37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="I -> M (in Ref. 2; AFK37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="M -> I (in Ref. 2; AFK37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="L -> F (in Ref. 2; AFK37664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57480 MW; 6477BC0B3069DC7B CRC64;
MGYDQTRKLS DEYEISEILG RGGFSVVRKG TKKSGNEKTQ VAIKTLRRLG SSPSGTGGGQ
KSTATVMGFP SLRQVSVSDA LLTNEILVMR RIVENVSPHP NVIDLYDVCE DSNGVHLVLE
LCSGGELFDR IVAQDKYAET EAAAVVRQIA AGLEAVHKAD IVHRDLKPEN CLFLDSRKDS
PLKIMDFGLS SVEEFTDPVV GLFGSIDYVS PEALSQGKIT AKSDMWSLGV ILYILLSGYP
PFIAQNNRQK QQMIINGNFS FYEKTWKGIT QSAKQLISSL LTVDPSKRPS AQELLSHPWV
RGDKAKDEQM DPEIVSRLQS FNARRKLRAA AIASVWSSTI FLRTKKLRSL VGTYDLKEEE
IESLRIHFKK ICGNGDNATL SEFVEVLKAM KMPSLIPLAP RIFDLFDNNR DGTIDMREIL
CGFSSLKNSK GDDALRLCFQ MYDTDRSGCI TKEEVASMLC ALPEECLPAD ITEPGKLDEI
FDLMDANSDG KVTFEEFKAA MQRDSSLQDM LLSSLRPS
