CAMK5_ARATH
ID CAMK5_ARATH Reviewed; 601 AA.
AC Q9SCS2; F4J0N4; O04290; Q0WRC1;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=CDPK-related kinase 5;
DE Short=AtCRK5;
DE EC=2.7.11.1;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase 1;
GN Name=CRK5; Synonyms=CaMK1; OrderedLocusNames=At3g50530;
GN ORFNames=T20E23.130;
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 [MRNA] (ISOFORM 1), AND 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Salchert K.D.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
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 [7]
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SCS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SCS2-2; Sequence=VSP_044531;
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 (415-445) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF00328.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF435446; AAL30814.1; -; mRNA.
DR EMBL; Y09418; CAA70572.1; -; mRNA.
DR EMBL; AL133363; CAB62482.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78676.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78677.1; -; Genomic_DNA.
DR EMBL; AK228391; BAF00328.1; ALT_FRAME; mRNA.
DR PIR; T46084; T46084.
DR RefSeq; NP_001190048.1; NM_001203119.1. [Q9SCS2-2]
DR RefSeq; NP_190622.1; NM_114913.4. [Q9SCS2-1]
DR AlphaFoldDB; Q9SCS2; -.
DR SMR; Q9SCS2; -.
DR STRING; 3702.AT3G50530.2; -.
DR iPTMnet; Q9SCS2; -.
DR PaxDb; Q9SCS2; -.
DR PRIDE; Q9SCS2; -.
DR ProteomicsDB; 239150; -. [Q9SCS2-1]
DR EnsemblPlants; AT3G50530.1; AT3G50530.1; AT3G50530. [Q9SCS2-1]
DR EnsemblPlants; AT3G50530.2; AT3G50530.2; AT3G50530. [Q9SCS2-2]
DR GeneID; 824217; -.
DR Gramene; AT3G50530.1; AT3G50530.1; AT3G50530. [Q9SCS2-1]
DR Gramene; AT3G50530.2; AT3G50530.2; AT3G50530. [Q9SCS2-2]
DR KEGG; ath:AT3G50530; -.
DR Araport; AT3G50530; -.
DR TAIR; locus:2098705; AT3G50530.
DR eggNOG; KOG0032; Eukaryota.
DR OMA; NSHNIEV; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9SCS2; -.
DR PRO; PR:Q9SCS2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCS2; baseline and differential.
DR Genevisible; Q9SCS2; 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 Alternative splicing; ATP-binding; Calcium; Kinase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SG12"
FT CHAIN 2..601
FT /note="CDPK-related kinase 5"
FT /id="PRO_0000420532"
FT DOMAIN 148..410
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 452..488
FT /note="EF-hand 1"
FT DOMAIN 489..524
FT /note="EF-hand 2"
FT DOMAIN 525..564
FT /note="EF-hand 3"
FT DOMAIN 567..596
FT /note="EF-hand 4"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..445
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 434..454
FT /note="Calmodulin binding (CaMBD)"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 154..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 306
FT /note="P -> PGKALRLYAICKLRFQNLETSICLYALTIAFA (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044531"
FT CONFLICT 72
FT /note="T -> S (in Ref. 5; BAF00328)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="V -> I (in Ref. 5; BAF00328)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="L -> Q (in Ref. 1; AAL30814 and 2; CAA70572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 66991 MW; 61B4502B53C25DBF CRC64;
MGLCTSKPNS SNSDQTPARN SPLPASESVK PSSSSVNGED QCVTTTNNEG KKSPFFPFYS
PSPAHYFFSK KTPARSPATN STNSTPKRFF KRPFPPPSPA KHIRAVLARR HGSVKPNSSA
IPEGSEAEGG GVGLDKSFGF SKSFASKYEL GDEVGRGHFG YTCAAKFKKG DNKGQQVAVK
VIPKAKMTTA IAIEDVRREV KILRALSGHN NLPHFYDAYE DHDNVYIVME LCEGGELLDR
ILSRGGKYTE EDAKTVMIQI LNVVAFCHLQ GVVHRDLKPE NFLFTSKEDT SQLKAIDFGL
SDYVRPDERL NDIVGSAYYV APEVLHRSYS TEADIWSVGV IVYILLCGSR PFWARTESGI
FRAVLKADPS FDDPPWPLLS SEARDFVKRL LNKDPRKRLT AAQALSHPWI KDSNDAKVPM
DILVFKLMRA YLRSSSLRKA ALRALSKTLT VDELFYLREQ FALLEPSKNG TISLENIKSA
LMKMATDAMK DSRIPEFLGQ LSALQYRRMD FEEFCAAALS VHQLEALDRW EQHARCAYEL
FEKEGNRPIM IDELASELGL GPSVPVHAVL HDWLRHTDGK LSFLGFVKLL HGVSSRTIKA
H
