CAMK8_ARATH
ID CAMK8_ARATH Reviewed; 606 AA.
AC Q9FX86;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=CDPK-related kinase 8;
DE Short=AtCRK8;
DE EC=2.7.11.1;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase CRK8;
GN Name=CRK8; OrderedLocusNames=At1g49580; ORFNames=F14J22.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP REVIEW, AND GENE FAMILY.
RX PubMed=12959135;
RA Harmon A.C.;
RT "Calcium-regulated protein kinases of plants.";
RL Gravit. Space Biol. Bull. 16:83-90(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [7]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX AGRICOLA=IND43694487; DOI=10.1016/j.plantsci.2004.12.019;
RA Du W., Wang Y., Liang S., Lu Y.-T.;
RT "Biochemical and expression analysis of an Arabidopsis calcium-dependent
RT protein kinase-related kinase.";
RL Plant Sci. 168:1181-1192(2005).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. {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 -!- ACTIVITY REGULATION: Activated by calcium and calmodulin.
CC Autophosphorylation may play an important role in the regulation of the
CC kinase activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds calmodulin (CaM) in a calcium-dependent manner.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily:
CC a kinase domain, an autoinhibitory (junction) domain and a calmodulin-
CC like domain. The autoinhibitory domain (418-448) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC011807; AAG13044.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32444.1; -; Genomic_DNA.
DR EMBL; BT010597; AAQ89619.1; -; mRNA.
DR EMBL; AK229416; BAF01277.1; -; mRNA.
DR PIR; D96532; D96532.
DR RefSeq; NP_175381.1; NM_103846.4.
DR AlphaFoldDB; Q9FX86; -.
DR SMR; Q9FX86; -.
DR BioGRID; 26607; 4.
DR IntAct; Q9FX86; 2.
DR STRING; 3702.AT1G49580.1; -.
DR iPTMnet; Q9FX86; -.
DR PaxDb; Q9FX86; -.
DR PRIDE; Q9FX86; -.
DR ProteomicsDB; 240282; -.
DR EnsemblPlants; AT1G49580.1; AT1G49580.1; AT1G49580.
DR GeneID; 841382; -.
DR Gramene; AT1G49580.1; AT1G49580.1; AT1G49580.
DR KEGG; ath:AT1G49580; -.
DR Araport; AT1G49580; -.
DR TAIR; locus:2012232; AT1G49580.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_2_1; -.
DR OMA; GNDYPQI; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9FX86; -.
DR PRO; PR:Q9FX86; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX86; baseline and differential.
DR Genevisible; Q9FX86; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ATP-binding; Calcium; Kinase; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SG12"
FT CHAIN 2..606
FT /note="CDPK-related kinase 8"
FT /id="PRO_0000420535"
FT DOMAIN 150..412
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 455..491
FT /note="EF-hand 1"
FT DOMAIN 492..527
FT /note="EF-hand 2"
FT DOMAIN 528..567
FT /note="EF-hand 3"
FT DOMAIN 570..599
FT /note="EF-hand 4"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..448
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 437..457
FT /note="Calmodulin binding (CaMBD)"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..108
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 156..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 583
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 606 AA; 67973 MW; 535329AD5F89B14C CRC64;
MGGCTSKPST SSGRPNPFAP GNDYPQIDDF APDHPGKSPI PTPSAAKASP FFPFYTPSPA
RHRRNKSRDV GGGGESKSLT STPLRQLRRA FHPPSPAKHI RAALRRRKGK KEAALSGVTQ
LTTEVPQREE EEEVGLDKRF GFSKEFHSRV ELGEEIGRGH FGYTCSAKFK KGELKGQVVA
VKIIPKSKMT TAIAIEDVRR EVKILQALSG HKNLVQFYDA FEDNANVYIA MELCEGGELL
DRILARGGKY SENDAKPVII QILNVVAFCH FQGVVHRDLK PENFLYTSKE ENSQLKAIDF
GLSDFVRPDE RLNDIVGSAY YVAPEVLHRS YTTEADVWSI GVIAYILLCG SRPFWARTES
GIFRAVLKAD PSFDEPPWPF LSSDAKDFVK RLLFKDPRRR MSASQALMHP WIRAYNTDMN
IPFDILIFRQ MKAYLRSSSL RKAALRALSK TLIKDEILYL KTQFSLLAPN KDGLITMDTI
RMALASNATE AMKESRIPEF LALLNGLQYR GMDFEEFCAA AINVHQHESL DCWEQSIRHA
YELFDKNGNR AIVIEELASE LGVGPSIPVH SVLHDWIRHT DGKLSFFGFV KLLHGVSVRA
SGKTTR
