ID CDKD3_ARATH Reviewed; 391 AA. AC Q9LMT0; Q9LM42; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JAN-2024, entry version 163. DE RecName: Full=Cyclin-dependent kinase D-3; DE Short=CDKD;3; DE EC=2.7.11.22; DE EC=2.7.11.23; DE AltName: Full=CDK-activating kinase 2-At; DE Short=CAK2-At; GN Name=CDKD-3; OrderedLocusNames=At1g18040; ORFNames=T10F20.5, T10O22.1; 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 FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH RP CYCH1-1, PHOSPHORYLATION AT SER-161 AND THR-167, AND MUTAGENESIS OF LYS-41; RP SER-161 AND THR-167. 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). RN [8] RP FUNCTION, PHOSPHORYLATION AT TYR-23, INTERACTION WITH CYCH1-1, AND RP MUTAGENESIS OF TYR-23. RX PubMed=16856985; DOI=10.1111/j.1365-313x.2006.02820.x; RA Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C., RA Uchimiya H., Umeda M.; RT "Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase- RT activating kinases in Arabidopsis."; RL Plant J. 47:701-710(2006). CC -!- FUNCTION: May form a stable complex with cyclin CYCH1-1 that CC phosphorylates human CDK2 and the C-terminal domain (CTD) of the large CC subunit of RNA polymerase II. {ECO:0000269|PubMed:15486101, CC ECO:0000269|PubMed:16856985}. 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 -!- ACTIVITY REGULATION: Activated by phosphorylation by CDKF-1. CC {ECO:0000269|PubMed:15486101}. CC -!- SUBUNIT: Interacts with CYCH1-1. Binding to CYCH1-1 activates CDK CC kinase. {ECO:0000269|PubMed:15486101, ECO:0000269|PubMed:16856985}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15486101}. CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots and suspension cell CC culture. {ECO:0000269|PubMed:12527363}. CC -!- PTM: Phosphorylated by CDKF-1 at Ser-161 and Thr-167. Phosphorylated at CC Tyr-23 by WEE1. Autophosphorylated. {ECO:0000269|PubMed:15486101, CC ECO:0000269|PubMed:16856985}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF78394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB047274; BAB62843.1; -; mRNA. DR EMBL; AC034107; AAF97821.1; -; Genomic_DNA. DR EMBL; AC069551; AAF78394.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE29667.1; -; Genomic_DNA. DR EMBL; AY099677; AAM20528.1; -; mRNA. DR EMBL; AY128857; AAM91257.1; -; mRNA. DR PIR; H86315; H86315. DR RefSeq; NP_173244.1; NM_101666.3. DR AlphaFoldDB; Q9LMT0; -. DR SMR; Q9LMT0; -. DR BioGRID; 23623; 33. DR IntAct; Q9LMT0; 6. DR STRING; 3702.Q9LMT0; -. DR iPTMnet; Q9LMT0; -. DR PaxDb; 3702-AT1G18040-1; -. DR ProteomicsDB; 224472; -. DR EnsemblPlants; AT1G18040.1; AT1G18040.1; AT1G18040. DR GeneID; 838384; -. DR Gramene; AT1G18040.1; AT1G18040.1; AT1G18040. DR KEGG; ath:AT1G18040; -. DR Araport; AT1G18040; -. DR TAIR; AT1G18040; CDKD1. DR eggNOG; KOG0659; Eukaryota. DR HOGENOM; CLU_000288_181_0_1; -. DR InParanoid; Q9LMT0; -. DR OMA; TQSYLRM; -. DR OrthoDB; 244018at2759; -. DR PhylomeDB; Q9LMT0; -. DR PRO; PR:Q9LMT0; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9LMT0; baseline and differential. DR GO; GO:0005634; C:nucleus; HDA:TAIR. DR GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004672; F:protein kinase activity; TAS:TAIR. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051726; P:regulation of cell cycle; TAS:TAIR. DR CDD; cd07841; STKc_CDK7; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF553; CYCLIN-DEPENDENT KINASE D-3; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q9LMT0; AT. PE 1: Evidence at protein level; KW ATP-binding; Cell cycle; Cell division; Kinase; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..391 FT /note="Cyclin-dependent kinase D-3" FT /id="PRO_0000293121" FT DOMAIN 12..292 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 294..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 337..391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..391 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 134 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 18..26 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305" FT MOD_RES 23 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16856985" FT MOD_RES 161 FT /note="Phosphoserine; by CAK" FT /evidence="ECO:0000269|PubMed:15486101" FT MOD_RES 167 FT /note="Phosphothreonine; by CAK" FT /evidence="ECO:0000269|PubMed:15486101" FT MUTAGEN 23 FT /note="Y->F: Abolishes phosphorylation by WEE1." FT /evidence="ECO:0000269|PubMed:16856985" FT MUTAGEN 41 FT /note="K->R: Prevents autophosphorylation." FT /evidence="ECO:0000269|PubMed:15486101" FT MUTAGEN 161 FT /note="S->A: Reduces phosphorylation by CDKF-1 by 20%. FT Abolishes phosphorylation by CDKF-1; when associated with FT A-167." FT /evidence="ECO:0000269|PubMed:15486101" FT MUTAGEN 167 FT /note="T->A: Reduces phosphorylation by CDKF-1 by 80%. FT Abolishes phosphorylation by CDKF-1; when associated with FT A-161." FT /evidence="ECO:0000269|PubMed:15486101" SQ SEQUENCE 391 AA; 44530 MW; 3FD4A2293283B656 CRC64; MPEQPKKVAD RYLKQEVLGQ GTYGVVFKAT DTKTEQTVAI KKIRLGKQRE GVNITALREI KMLKELKHPH IILLIDAFPH KENLHLVFEF METDLEAVIR DSNIFLSPAD IKSYLLMTFK GLAYCHDKWV LHRDMKPNNL LIGVDGQLKL ADFGLARIFG SPNRKFTHQV FARWYRAPEL LFGAKQYGAA VDVWAVACIF AELLLRRPFL QGNSDIDQLS KIFAAFGTPK ADQWPDLTKL PDYVEYQFVP APSLRSLFPA VSDDALDLLS KMFTYDPKAR ISIKQALEHR YFTSAPAPTD PAKLPKPVPK QDGKSSYGKH EAITVQSPPR KLRRVMPERG RVDSLKSHVD KDQQAPMSLD FTILAERPPN RPTITSADRS HLKRKLDLEF Q //