CDKG1_ARATH
ID CDKG1_ARATH Reviewed; 612 AA.
AC Q9FGW5; F4K9C1; Q0WW64;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cyclin-dependent kinase G1;
DE EC=2.7.11.22;
GN Name=CDKG1; OrderedLocusNames=At5g63370; ORFNames=K9H21.7;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-612.
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 FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RS2Z33, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23404887; DOI=10.1105/tpc.112.107896;
RA Huang X.Y., Niu J., Sun M.X., Zhu J., Gao J.F., Yang J., Zhou Q.,
RA Yang Z.N.;
RT "CYCLIN-DEPENDENT KINASE G1 is associated with the spliceosome to regulate
RT CALLOSE SYNTHASE5 splicing and pollen wall formation in Arabidopsis.";
RL Plant Cell 25:637-648(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CYCL1-1.
RC STRAIN=cv. Columbia;
RX PubMed=24469829; DOI=10.1073/pnas.1318460111;
RA Zheng T., Nibau C., Phillips D.W., Jenkins G., Armstrong S.J., Doonan J.H.;
RT "CDKG1 protein kinase is essential for synapsis and male meiosis at high
RT ambient temperature in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2182-2187(2014).
CC -!- FUNCTION: Cyclin-dependent kinase involved in pre-mRNA splicing.
CC Required for the correct splicing of the sixth intron of CALS5 pre-
CC mRNA. May stabilize the binding of U1 snRNP to this rare type of intron
CC with a GC 5'SS. Involved in chromosome pairing and is required for the
CC completion of synapsis in male meiocytes at high ambient temperatures.
CC {ECO:0000269|PubMed:23404887, ECO:0000269|PubMed:24469829}.
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 -!- SUBUNIT: Forms a complex with CYCL1-1. Associated with the spliceosome.
CC Interacts with RS2Z33. {ECO:0000269|PubMed:23404887,
CC ECO:0000269|PubMed:24469829}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:23404887}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FGW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FGW5-2; Sequence=VSP_055206;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and inflorescences. Lower
CC levels of expression in roots and stems. {ECO:0000269|PubMed:23404887}.
CC -!- DISRUPTION PHENOTYPE: Aberrant callose deposition, defective pollen
CC wall formation during microspore development, and severely reduced male
CC fertility. {ECO:0000269|PubMed:23404887, ECO:0000269|PubMed:24469829}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB023035; BAB10741.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97737.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97738.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97739.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97740.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69859.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69860.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69862.1; -; Genomic_DNA.
DR EMBL; AY060555; AAL31185.1; -; mRNA.
DR EMBL; AY062461; AAL32539.1; -; mRNA.
DR EMBL; AY093285; AAM13284.1; -; mRNA.
DR EMBL; AY141988; AAM98252.1; -; mRNA.
DR EMBL; AK226492; BAE98634.1; -; mRNA.
DR RefSeq; NP_001119484.1; NM_001126012.2. [Q9FGW5-2]
DR RefSeq; NP_001119485.1; NM_001126013.2. [Q9FGW5-2]
DR RefSeq; NP_001190605.1; NM_001203676.2. [Q9FGW5-1]
DR RefSeq; NP_001331507.1; NM_001345588.1. [Q9FGW5-1]
DR RefSeq; NP_001331508.1; NM_001345587.1. [Q9FGW5-1]
DR RefSeq; NP_001331510.1; NM_001345589.1. [Q9FGW5-1]
DR RefSeq; NP_201142.1; NM_125732.3. [Q9FGW5-1]
DR AlphaFoldDB; Q9FGW5; -.
DR SMR; Q9FGW5; -.
DR BioGRID; 21699; 7.
DR IntAct; Q9FGW5; 6.
DR STRING; 3702.AT5G63370.1; -.
DR iPTMnet; Q9FGW5; -.
DR PaxDb; Q9FGW5; -.
DR PRIDE; Q9FGW5; -.
DR ProteomicsDB; 223979; -. [Q9FGW5-1]
DR EnsemblPlants; AT5G63370.1; AT5G63370.1; AT5G63370. [Q9FGW5-1]
DR EnsemblPlants; AT5G63370.2; AT5G63370.2; AT5G63370. [Q9FGW5-2]
DR EnsemblPlants; AT5G63370.3; AT5G63370.3; AT5G63370. [Q9FGW5-2]
DR EnsemblPlants; AT5G63370.4; AT5G63370.4; AT5G63370. [Q9FGW5-1]
DR EnsemblPlants; AT5G63370.6; AT5G63370.6; AT5G63370. [Q9FGW5-1]
DR EnsemblPlants; AT5G63370.7; AT5G63370.7; AT5G63370. [Q9FGW5-1]
DR EnsemblPlants; AT5G63370.8; AT5G63370.8; AT5G63370. [Q9FGW5-1]
DR GeneID; 836456; -.
DR Gramene; AT5G63370.1; AT5G63370.1; AT5G63370. [Q9FGW5-1]
DR Gramene; AT5G63370.2; AT5G63370.2; AT5G63370. [Q9FGW5-2]
DR Gramene; AT5G63370.3; AT5G63370.3; AT5G63370. [Q9FGW5-2]
DR Gramene; AT5G63370.4; AT5G63370.4; AT5G63370. [Q9FGW5-1]
DR Gramene; AT5G63370.6; AT5G63370.6; AT5G63370. [Q9FGW5-1]
DR Gramene; AT5G63370.7; AT5G63370.7; AT5G63370. [Q9FGW5-1]
DR Gramene; AT5G63370.8; AT5G63370.8; AT5G63370. [Q9FGW5-1]
DR KEGG; ath:AT5G63370; -.
DR Araport; AT5G63370; -.
DR TAIR; locus:2158554; AT5G63370.
DR eggNOG; KOG0663; Eukaryota.
DR InParanoid; Q9FGW5; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q9FGW5; -.
DR PRO; PR:Q9FGW5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGW5; baseline and differential.
DR Genevisible; Q9FGW5; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032953; P:regulation of (1->3)-beta-D-glucan biosynthetic process; IMP:TAIR.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR CDD; cd07843; STKc_CDC2L1; 1.
DR InterPro; IPR045267; CDK11/PITSLRE_STKc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Meiosis; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Spliceosome;
KW Transferase.
FT CHAIN 1..612
FT /note="Cyclin-dependent kinase G1"
FT /id="PRO_0000429770"
FT DOMAIN 297..593
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 303..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 308
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT VAR_SEQ 1..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055206"
FT CONFLICT 593
FT /note="F -> L (in Ref. 4; BAE98634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 69620 MW; 99E28A670AE81B11 CRC64;
MAAGGVDVSR SSVAVKKDYD FYRNGSRDVY VRQSGRDDER RQIKRPSDHD LRRNDGRHRS
RLAYEKGELR EEAEVQRPSE KRRKFSPIVW NAEKVGRAPS REKTKSPFPV PTTTVISNQA
VAGKTTSNDQ VNALMSPEPS YLAPVQPSEA LLAVKHPVDD LEEGQLEEEQ VMQEDVKEGL
LEEEQVMQEP NIKTSRWGTG LTSPKEELIS VNVSKTNRWN RSSLTPECEE VMVSEEQQCY
SSGSGSGHLS VEKLSADGNS GREYYSSDHD ELEHEDQDSL TPGEMNMMFG SRSVNEFQKL
NKINEGTYGI VYKARDEKTK EIVALKKIKM KEDRFEEEYG FPLTSLREIN ILLSCNHPAI
VNVKEVVVGG KNDNDVYMVM EHLEHDLRGV MDRRKEPFST SEVKCLMMQL LDGLKYLHTN
WIIHRDLKPS NLLMNNCGEL KICDFGMARQ YGSPIKPYTQ MVITQWYRPP ELLLGAKEYS
TAVDMWSVGC IMAELLSQKP LFPGKSELDQ LQKIFAVLGT PNEAIWPGFS SFPNAKAKFP
TQPYNMLRKK FPAISFVGGQ ILSERGFDLL NSLLTLDPEK RLTVEDALNH GWFHEVPLPK
SKDFMPTYPP KR
