CDKD1_ARATH
ID CDKD1_ARATH Reviewed; 398 AA.
AC Q9C9U2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cyclin-dependent kinase D-1;
DE Short=CDKD;1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=CDK-activating kinase 3-At;
DE Short=CAK3-At;
GN Name=CDKD-1; OrderedLocusNames=At1g73690; ORFNames=F25P22.11;
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], AND TISSUE SPECIFICITY.
RX PubMed=12527363; DOI=10.1016/s0014-5793(02)03780-8;
RA Shimotohno A., Matsubayashi S., Yamaguchi M., Uchimiya H., Umeda M.;
RT "Differential phosphorylation activities of CDK-activating kinases in
RT Arabidopsis thaliana.";
RL FEBS Lett. 534:69-74(2003).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11971144; DOI=10.1105/tpc.010445;
RA Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL Plant Cell 14:903-916(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-40.
RX PubMed=15486101; DOI=10.1105/tpc.104.025601;
RA Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.;
RT "The plant-specific kinase CDKF;1 is involved in activating phosphorylation
RT of cyclin-dependent kinase-activating kinases in Arabidopsis.";
RL Plant Cell 16:2954-2966(2004).
RN [7]
RP REVIEW.
RX PubMed=17094738; DOI=10.1146/annurev.genet.40.110405.090431;
RA Inze D., de Veylder L.;
RT "Cell cycle regulation in plant development.";
RL Annu. Rev. Genet. 40:77-105(2006).
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=2.7.11.22;
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=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15486101}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in suspension cell culture,
CC but not in plant organs. {ECO:0000269|PubMed:12527363}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AB047275; BAB62844.1; -; mRNA.
DR EMBL; AC012679; AAG52081.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35498.1; -; Genomic_DNA.
DR EMBL; AY063843; AAL36199.1; -; mRNA.
DR EMBL; AY091227; AAM14166.1; -; mRNA.
DR PIR; A96764; A96764.
DR RefSeq; NP_177510.1; NM_106028.4.
DR AlphaFoldDB; Q9C9U2; -.
DR SMR; Q9C9U2; -.
DR BioGRID; 28923; 19.
DR IntAct; Q9C9U2; 2.
DR STRING; 3702.AT1G73690.1; -.
DR PaxDb; Q9C9U2; -.
DR PRIDE; Q9C9U2; -.
DR ProteomicsDB; 222811; -.
DR EnsemblPlants; AT1G73690.1; AT1G73690.1; AT1G73690.
DR GeneID; 843704; -.
DR Gramene; AT1G73690.1; AT1G73690.1; AT1G73690.
DR KEGG; ath:AT1G73690; -.
DR Araport; AT1G73690; -.
DR TAIR; locus:2027819; AT1G73690.
DR eggNOG; KOG0659; Eukaryota.
DR HOGENOM; CLU_000288_181_0_1; -.
DR InParanoid; Q9C9U2; -.
DR OMA; LLMSMCA; -.
DR OrthoDB; 1367115at2759; -.
DR PhylomeDB; Q9C9U2; -.
DR PRO; PR:Q9C9U2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9U2; baseline and differential.
DR Genevisible; Q9C9U2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; TAS:TAIR.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:TAIR.
DR CDD; cd07841; STKc_CDK7; 1.
DR InterPro; IPR037770; CDK7.
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; 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; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..398
FT /note="Cyclin-dependent kinase D-1"
FT /id="PRO_0000293119"
FT DOMAIN 11..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 296..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 22
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT MUTAGEN 40
FT /note="K->R: Prevents autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15486101"
SQ SEQUENCE 398 AA; 45138 MW; 32BA95E61E6D2C45 CRC64;
MEQPKKVADR YLKREVLGQG TYGVVFKATD TKNGETVAIK KIRLGKEKEG VNVTALREIK
LLKELKHPHI IELIDAFPHK ENLHIVFEFM ETDLEAVIRD RNLYLSPGDV KSYLQMILKG
LEYCHGKWVL HRDMKPNNLL IGPNGQLKLA DFGLARIFGS PGRKFTHQVF ARWYRAPELL
FGAKQYDGAV DVWAAGCIFA ELLLRRPFLQ GNSDIDQLSK IFAAFGTPKA DQWPDMICLP
DYVEYQFVPA PSLRSLLPTV SEDALDLLSK MFTYDPKSRI SIQQALKHRY FTSAPSPTDP
LKLPRPVSKQ DAKSSDSKLE AIKVLSPAHK FRRVMPDRGK SGNGFKDQSV DVMRQASHDG
QAPMSLDFTI LAERPPNRPT ITSADRSHLK RKLDLEFL
