CAMK7_ARATH
ID CAMK7_ARATH Reviewed; 577 AA.
AC Q9LET1;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=CDPK-related kinase 7;
DE Short=AtCRK7;
DE EC=2.7.11.1;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase CRK7;
GN Name=CRK7; OrderedLocusNames=At3g56760; ORFNames=T8M16.90;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 [4]
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 [5]
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).
RN [6]
RP PHOSPHORYLATION AT SER-334.
RX PubMed=22645532; DOI=10.3389/fpls.2011.00036;
RA Curran A., Chang I.-F., Chang C.-L., Garg S., Miguel R.M., Barron Y.D.,
RA Li Y., Romanowsky S., Cushman J.C., Gribskov M., Harmon A.C., Harper J.F.;
RT "Calcium-dependent protein kinases from Arabidopsis show substrate
RT specificity differences in an analysis of 103 substrates.";
RL Front. Plant Sci. 2:36-36(2011).
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 (391-421) 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; AL390921; CAC00739.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79562.1; -; Genomic_DNA.
DR PIR; T51264; T51264.
DR RefSeq; NP_191235.1; NM_115535.3.
DR AlphaFoldDB; Q9LET1; -.
DR SMR; Q9LET1; -.
DR STRING; 3702.AT3G56760.1; -.
DR iPTMnet; Q9LET1; -.
DR PaxDb; Q9LET1; -.
DR PRIDE; Q9LET1; -.
DR ProteomicsDB; 240318; -.
DR EnsemblPlants; AT3G56760.1; AT3G56760.1; AT3G56760.
DR GeneID; 824843; -.
DR Gramene; AT3G56760.1; AT3G56760.1; AT3G56760.
DR KEGG; ath:AT3G56760; -.
DR Araport; AT3G56760; -.
DR TAIR; locus:2103655; AT3G56760.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_2_1; -.
DR OMA; CHGKPSQ; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9LET1; -.
DR PRO; PR:Q9LET1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LET1; baseline and differential.
DR Genevisible; Q9LET1; 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 1: Evidence at protein 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..577
FT /note="CDPK-related kinase 7"
FT /id="PRO_0000420534"
FT DOMAIN 124..386
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 428..464
FT /note="EF-hand 1"
FT DOMAIN 465..500
FT /note="EF-hand 2"
FT DOMAIN 501..540
FT /note="EF-hand 3"
FT DOMAIN 543..572
FT /note="EF-hand 4"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..421
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 410..430
FT /note="Calmodulin binding (CaMBD)"
FT /evidence="ECO:0000250"
FT COMPBIAS 12..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 130..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT MOD_RES 334
FT /note="Phosphoserine; by CPK1, CPK10 and CPK34"
FT /evidence="ECO:0000269|PubMed:22645532"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 577 AA; 64547 MW; 7E1EAA8E48E8C934 CRC64;
MGLCHGKPIE QQSKNLPISN EIEETPKNSS QKAKSSGFPF YSPSPLPSLF KTSPAVSSSS
VSSTPLRIFK RPFPPPSPAK HIRALLARRH GSVKPNEASI PEGSECEVGL DKKFGFSKQF
ASHYEIDGEV GRGHFGYTCS AKGKKGSLKG QDVAVKVIPK SKMTTAIAIE DVRREVKILR
ALTGHKNLVQ FYDAFEDDEN VYIVMELCQG GELLDKILQR GGKYSEVDAK KVMIQILSVV
AYCHLQGVVH RDLKPENFLF TTKDESSPLK AIDFGLSDYV RPDERLNDIV GSAYYVAPEV
LHRTYGTEAD MWSIGVIAYI LLCGSRPFWA RSESGIFRAV LKAEPNFEEA PWPSLSPDAV
DFVKRLLNKD YRKRLTAAQA LCHPWLVGSH ELKIPSDMII YKLVKVYIMS SSLRKSALAA
LAKTLTVPQL TYLQEQFNLL GPSKNGYISM QNYKTAILKS STEATKDSRV LDFVHMISCL
QYKKLDFEEF CASALSVYQL EAMETWEQHA RRAYELYEKD GNRVIMIEEL ATELGLGPSV
PVHVVLQDWI RHSDGKLSFL GFVRLLHGVS SRTLQKA
