CCAMK_LILLO
ID CCAMK_LILLO Reviewed; 520 AA.
AC Q43531;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase;
DE Short=LlCCaMK;
DE EC=2.7.11.17;
GN Name=CCAMK;
OS Lilium longiflorum (Trumpet lily).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX NCBI_TaxID=4690;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Nellie white; TISSUE=Anther;
RX PubMed=7761420; DOI=10.1073/pnas.92.11.4897;
RA Patil S., Takezawa D., Poovaiah B.W.;
RT "Chimeric plant calcium/calmodulin-dependent protein kinase gene with a
RT neural visinin-like calcium-binding domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4897-4901(1995).
RN [2]
RP FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF ASP-417; SER-453 AND THR-495, AND
RP ACTIVITY REGULATION.
RX PubMed=8626500; DOI=10.1074/jbc.271.14.8126;
RA Takezawa D., Ramachandiran S., Paranjape V., Poovaiah B.W.;
RT "Dual regulation of a chimeric plant serine/threonine kinase by calcium and
RT calcium/calmodulin.";
RL J. Biol. Chem. 271:8126-8132(1996).
RN [3]
RP PHOSPHORYLATION AT THR-267, MUTAGENESIS OF THR-267, AND CALMODULIN BINDING.
RX PubMed=11399751; DOI=10.1074/jbc.m009648200;
RA Sathyanarayanan P.V., Siems W.F., Jones J.P., Poovaiah B.W.;
RT "Calcium-stimulated autophosphorylation site of plant chimeric
RT calcium/calmodulin-dependent protein kinase.";
RL J. Biol. Chem. 276:32940-32947(2001).
RN [4]
RP ACTIVITY REGULATION.
RX PubMed=12027883; DOI=10.1046/j.1432-1033.2002.02904.x;
RA Sathyanarayanan P.V., Poovaiah B.W.;
RT "Autophosphorylation-dependent inactivation of plant chimeric
RT calcium/calmodulin-dependent protein kinase.";
RL Eur. J. Biochem. 269:2457-2463(2002).
CC -!- FUNCTION: Protein kinase that may be involved in microsporogenesis.
CC {ECO:0000269|PubMed:8626500}.
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. Autophosphorylation is associated
CC with a time-dependent loss of kinase activity sensitive to reaction pH
CC and ATP concentration. In vitro inactivation leads to the formation of
CC network-like structures. {ECO:0000269|PubMed:12027883,
CC ECO:0000269|PubMed:8626500}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during anther development.
CC {ECO:0000269|PubMed:7761420}.
CC -!- PTM: Autophosphorylation stimulated by calcium and inhibited by
CC calcium/calmodulin. Occurs probably by an intermolecular mechanism.
CC {ECO:0000269|PubMed:11399751, ECO:0000269|PubMed:8626500}.
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; U24188; AAC49008.1; -; mRNA.
DR AlphaFoldDB; Q43531; -.
DR SMR; Q43531; -.
DR iPTMnet; Q43531; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; 4.
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; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..520
FT /note="Calcium and calcium/calmodulin-dependent
FT serine/threonine-protein kinase"
FT /id="PRO_0000085698"
FT TRANSMEM 227..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 13..302
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 361..395
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 396..431
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 432..467
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 474..509
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 325..338
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000305|PubMed:11399751"
FT COILED 346..368
FT /evidence="ECO:0000255"
FT ACT_SITE 167
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 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 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 267
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11399751"
FT MUTAGEN 267
FT /note="T->A: Loss of calcium/calmodulin-stimulated kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:11399751"
FT MUTAGEN 417
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:8626500"
FT MUTAGEN 453
FT /note="S->A: Decreased calcium binding."
FT /evidence="ECO:0000269|PubMed:8626500"
FT MUTAGEN 495
FT /note="T->A: No calcium binding."
FT /evidence="ECO:0000269|PubMed:8626500"
SQ SEQUENCE 520 AA; 57887 MW; 6D583FD61C1453C4 CRC64;
MSRHESRKLS DDYEVVDVLG KGGFSVVRRG ISKSRGKNND VAIKTLRRYG YTLPGAQRSQ
PGQRGLSPLG MPTLKQVSVS DALLTNEILV MRRIVEDVSP HPNVIHLHDV YEDANGVHLV
LELCSGGELF DRIVAQDRYS ESEAAEVVQQ IASGLAALHK STIIHRDLKP ENCLFLNQEK
RSTLKIMDFG LSSVEDFTDP IVALFGSIDY VSPEALSQRQ VSSASDMWSL GVILYILLSG
CPPFHAPSNR EKQQRILAGD FSFEEHTWKT ITSSAKDLIS SLLSVDPYKR PTANDLLKHP
WVIGDSAKQE LIEPEVVSRL RSFNARRKLR AAAIASVLSS KVLLRTKKLK NLLGSHDMKS
EELENLRAHF KRICANGDNA TLPEFEEVLK AMKMNSLIPL APRVFDLFDN NRDGTIDMRE
ILCGLSNLRN SQGDDALQLC FQMYDADRSG CISKEELASM LRALPEDCVP ADITEPGKLD
EIFDQMDANS DGVVTFDEFK AAMQRDSSLQ DVVLSSLRTI
