CDC2C_ARATH
ID CDC2C_ARATH Reviewed; 644 AA.
AC B5X564; Q8W2N0; Q9FLZ4; Q9SBZ2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cyclin-dependent kinase C-2 C {ECO:0000303|PubMed:10366720};
DE Short=CDC2CAt {ECO:0000303|PubMed:10366720};
DE Short=Protein cdc2 C {ECO:0000303|PubMed:10366720};
DE EC=2.7.11.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Cyclin-dependent kinase-like protein 1 {ECO:0000303|PubMed:15686519};
DE Short=CDK-like protein 1 {ECO:0000303|PubMed:15686519};
GN Name=CDC2C {ECO:0000303|PubMed:10366720};
GN Synonyms=CKL1 {ECO:0000303|PubMed:15686519};
GN OrderedLocusNames=At5g39420 {ECO:0000312|Araport:AT5G39420};
GN ORFNames=MUL8.100 {ECO:0000312|EMBL:AED94431.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Lessard P., Petit-Jean X., Kreis M., Thomas M.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10366720; DOI=10.1016/s0167-4781(99)00059-7;
RA Lessard P., Bouly J.-P., Jouannic S., Kreis M., Thomas M.;
RT "Identification of cdc2cAt: a new cyclin-dependent kinase expressed in
RT Arabidopsis thaliana flowers.";
RL Biochim. Biophys. Acta 1445:351-358(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15686519; DOI=10.1111/j.1365-313x.2004.02319.x;
RA Menges M., de Jager S.M., Gruissem W., Murray J.A.H.;
RT "Global analysis of the core cell cycle regulators of Arabidopsis
RT identifies novel genes, reveals multiple and highly specific profiles of
RT expression and provides a coherent model for plant cell cycle control.";
RL Plant J. 41:546-566(2005).
RN [7]
RP AUTOPHOSPHORYLATION.
RX PubMed=21477822; DOI=10.1016/j.phytochem.2011.02.029;
RA Nemoto K., Seto T., Takahashi H., Nozawa A., Seki M., Shinozaki K.,
RA Endo Y., Sawasaki T.;
RT "Autophosphorylation profiling of Arabidopsis protein kinases using the
RT cell-free system.";
RL Phytochemistry 72:1136-1144(2011).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=24023856; DOI=10.1371/journal.pone.0073291;
RA Savage L.J., Imre K.M., Hall D.A., Last R.L.;
RT "Analysis of essential Arabidopsis nuclear genes encoding plastid-targeted
RT proteins.";
RL PLoS ONE 8:e73291-e73291(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in flowers and pollen.
CC {ECO:0000269|PubMed:10366720, ECO:0000269|PubMed:15686519}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:21477822}.
CC -!- DISRUPTION PHENOTYPE: Light green to yellow seeds.
CC {ECO:0000269|PubMed:24023856}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF21469.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB11015.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U83118; AAF21469.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF120153; AAL56635.1; -; mRNA.
DR EMBL; AB009054; BAB11015.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94431.1; -; Genomic_DNA.
DR EMBL; BT046183; ACI49782.1; -; mRNA.
DR RefSeq; NP_198758.2; NM_123304.4.
DR AlphaFoldDB; B5X564; -.
DR SMR; B5X564; -.
DR STRING; 3702.AT5G39420.1; -.
DR PaxDb; B5X564; -.
DR PRIDE; B5X564; -.
DR ProteomicsDB; 181257; -.
DR EnsemblPlants; AT5G39420.1; AT5G39420.1; AT5G39420.
DR GeneID; 833938; -.
DR Gramene; AT5G39420.1; AT5G39420.1; AT5G39420.
DR KEGG; ath:AT5G39420; -.
DR Araport; AT5G39420; -.
DR TAIR; locus:2175743; AT5G39420.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_78_4_1; -.
DR InParanoid; B5X564; -.
DR OMA; PADSFWK; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; B5X564; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B5X564; baseline and differential.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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..644
FT /note="Cyclin-dependent kinase C-2 C"
FT /id="PRO_0000454241"
FT DOMAIN 105..389
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 565..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 420..427
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 111..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT CONFLICT 8
FT /note="N -> S (in Ref. 2; AAL56635)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="L -> I (in Ref. 2; AAL56635)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..68
FT /note="SLGS -> TLGL (in Ref. 1; AAF21469)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="K -> Q (in Ref. 2; AAL56635)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="M -> T (in Ref. 2; AAL56635)"
FT /evidence="ECO:0000305"
FT CONFLICT 640..644
FT /note="EQDDR -> GKPEIT (in Ref. 1; AAF21469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 72425 MW; 8DE909D87C0ED8E0 CRC64;
MGCISSKNVS CLTDQGDSPL PEPGLLSTSQ QHRVLIDHSL EASHNSKRSR KSRRLGGSDL
RIGVSLGSSH RNIEAEQAAA GWPAWLCSAA AEAVHGWVPL KAEAFQKLEK IGQGTYSSVF
RAREVETGKM VALKKVKFDN LQPESIRFMA REILILRKLN HPNIMKLEGI VTSRASSSIY
LVFEYMEHDL AGLSSNPDIR FTEPQIKCYM KQLLWGLEHC HMRGVIHRDI KASNILVNNK
GVLKLGDFGL ANVVTPSNKN QLTSRVVTLW YRAPELLMGS TSYGVSVDLW SVGCVFAEIL
MGKPILKGRT EIEQLHKIYK LCGSPQDSFW KRTKLPHATS FKPQHTYEAT LRERCKDLSA
TGVYLLETLL SMEPDKRGTA SSALNSEYFL TRPYACDPSS LPKYPPNKEM DAKYRDDMRR
KRANLKLRDS GVGRKHKRPH RAEYDPKNYA KLPIRKDTLE VKNIPNEASR ATTTTHGNYY
KVSDLPMTTG PASGFAWAVK RRKDPDNIST LTYYQPSSKS QLSGTSVAFA KNTFGLNLKP
DNDSVWEVQG NNYDDVIEEV PSHESKLSRI GERHGSLDGS GLDFSQREED SPKKTLEHLQ
FGKQSISGPL IFKSGKIDEI LQRNESNIRQ AVRKSHLQRE QDDR
