KRP6_ARATH
ID KRP6_ARATH Reviewed; 196 AA.
AC Q0WNX9; A8MRW2; Q8W2K3; Q9LJL5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cyclin-dependent kinase inhibitor 6;
DE AltName: Full=Cyclin-dependent kinase inhibitor p22ack1;
DE AltName: Full=Inhibitor/interactor of CDK protein 4;
DE AltName: Full=KIP-related protein 6;
GN Name=KRP6; Synonyms=ACK1, ICK4; OrderedLocusNames=At3g19150;
GN ORFNames=MVI11.5;
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), TISSUE SPECIFICITY, AND INTERACTION
RP WITH CDKA-1 AND CYCD4-1.
RC STRAIN=cv. Columbia;
RX PubMed=11449057; DOI=10.2307/3871392;
RA de Veylder L., Beeckman T., Beemster G.T.S., Krols L., Terras F.,
RA Landrieu I., van der Schueren E., Maes S., Naudts M., Inze D.;
RT "Functional analysis of cyclin-dependent kinase inhibitors of
RT Arabidopsis.";
RL Plant Cell 13:1653-1667(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH CYCD1-1.
RX PubMed=15464981; DOI=10.1016/j.bbrc.2004.08.233;
RA Cho J.W., Park S.C., Shin E.A., Kim C.K., Han W., Sohn S.-I., Song P.S.,
RA Wang M.-H.;
RT "Cyclin D1 and p22ack1 play opposite roles in plant growth and
RT development.";
RL Biochem. Biophys. Res. Commun. 324:52-57(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=15809079; DOI=10.1016/j.bbrc.2005.03.056;
RA Han W., Rhee H., Cho J.W., Ku M.S.B., Song P.S., Wang M.-H.;
RT "Overexpression of Arabidopsis ACK1 alters leaf morphology and retards
RT growth and development.";
RL Biochem. Biophys. Res. Commun. 330:887-890(2005).
RN [8]
RP FUNCTION.
RX PubMed=16376885; DOI=10.1016/j.febslet.2005.12.018;
RA Nakai T., Kato K., Shinmyo A., Sekine M.;
RT "Arabidopsis KRPs have distinct inhibitory activity toward cyclin D2-
RT associated kinases, including plant-specific B-type cyclin-dependent
RT kinase.";
RL FEBS Lett. 580:336-340(2006).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17253089; DOI=10.1007/s00299-006-0294-3;
RA Bird D.A., Buruiana M.M., Zhou Y., Fowke L.C., Wang H.;
RT "Arabidopsis cyclin-dependent kinase inhibitors are nuclear-localized and
RT show different localization patterns within the nucleoplasm.";
RL Plant Cell Rep. 26:861-872(2007).
RN [10]
RP UBIQUITINATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18948957; DOI=10.1038/nature07289;
RA Kim H.J., Oh S.A., Brownfield L., Hong S.H., Ryu H., Hwang I., Twell D.,
RA Nam H.G.;
RT "Control of plant germline proliferation by SCF(FBL17) degradation of cell
RT cycle inhibitors.";
RL Nature 455:1134-1137(2008).
RN [11]
RP FUNCTION, INTERACTION WITH RHF1A, DEVELOPMENTAL STAGE, AND UBIQUITINATION.
RX PubMed=18552199; DOI=10.1105/tpc.108.059741;
RA Liu J., Zhang Y., Qin G., Tsuge T., Sakaguchi N., Luo G., Sun K., Shi D.,
RA Aki S., Zheng N., Aoyama T., Oka A., Yang W., Umeda M., Xie Q., Gu H.,
RA Qu L.J.;
RT "Targeted degradation of the cyclin-dependent kinase inhibitor ICK4/KRP6 by
RT RING-type E3 ligases is essential for mitotic cell cycle progression during
RT Arabidopsis gametogenesis.";
RL Plant Cell 20:1538-1554(2008).
RN [12]
RP PHOSPHORYLATION AT THR-152, IDENTIFICATION BY MASS SPECTROMETRY,
RP MUTAGENESIS OF THR-152, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH KIN10 AND CYCD3-1.
RX PubMed=23617622; DOI=10.1111/tpj.12218;
RA Guerinier T., Millan L., Crozet P., Oury C., Rey F., Valot B., Mathieu C.,
RA Vidal J., Hodges M., Thomas M., Glab N.;
RT "Phosphorylation of p27(KIP1) homologs KRP6 and 7 by SNF1-related protein
RT kinase-1 links plant energy homeostasis and cell proliferation.";
RL Plant J. 75:515-525(2013).
CC -!- FUNCTION: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity.
CC Regulates cell division which is crucial for plant growth, development
CC and morphogenesis. May inhibit CDK kinases specifically involved in the
CC G1/S phase transition. {ECO:0000269|PubMed:15464981,
CC ECO:0000269|PubMed:15809079, ECO:0000269|PubMed:16376885,
CC ECO:0000269|PubMed:18552199}.
CC -!- ACTIVITY REGULATION: Down-regulated by KIN10 under a phosphorylation-
CC dependent manner. {ECO:0000269|PubMed:23617622}.
CC -!- SUBUNIT: Specifically interacts with CDKA-1, but not with CDKB1-1.
CC Interacts with CYCD1-1, CYCD4-1 and RHF1A. Binds to FBL17. Interacts
CC with KIN10 (PubMed:23617622). Interacts with CYCD3-1 (PubMed:23617622).
CC {ECO:0000269|PubMed:11449057, ECO:0000269|PubMed:15464981,
CC ECO:0000269|PubMed:18552199, ECO:0000269|PubMed:23617622}.
CC -!- INTERACTION:
CC Q0WNX9; P24100: CDKA-1; NbExp=3; IntAct=EBI-1253171, EBI-371713;
CC Q0WNX9; Q8W104: FBL17; NbExp=3; IntAct=EBI-1253171, EBI-2026732;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17253089, ECO:0000269|PubMed:18948957,
CC ECO:0000269|PubMed:23617622}. Note=Homogeneously distributed. Present
CC in microspores and accumulates strongly in vegetative cell nuclei
CC immediately after asymmetric division and disappears later.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0WNX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WNX9-2; Sequence=VSP_036333;
CC -!- TISSUE SPECIFICITY: Expressed in newly formed organs such as the shoot
CC apex. Expressed in cotyledon, primary root and marginal region of the
CC leaves as well as in developing pollen. {ECO:0000269|PubMed:11449057,
CC ECO:0000269|PubMed:15464981, ECO:0000269|PubMed:18948957}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both ovules and anthers during
CC meiosis and disappears before gametophytic mitosis. Present in
CC uninucleate microspore and bicellular pollen, and, to a lower extent,
CC in immature tricellular pollen and mature tricellular pollen.
CC {ECO:0000269|PubMed:18552199, ECO:0000269|PubMed:18948957}.
CC -!- PTM: Ubiquitinated by RHF1A and SCF(FBL17). Ubiquitination leads to its
CC subsequent degradation, thus controlling cell cycle progression.
CC {ECO:0000269|PubMed:18552199, ECO:0000269|PubMed:18948957}.
CC -!- PTM: The phosphorylation at Thr-152 by KIN10 represses its activity.
CC {ECO:0000269|PubMed:23617622}.
CC -!- SIMILARITY: Belongs to the CDI family. ICK/KRP subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ301557; CAC41620.1; -; mRNA.
DR EMBL; AF106705; AAF77612.2; -; mRNA.
DR EMBL; AF208692; AAL35985.1; -; Genomic_DNA.
DR EMBL; AP000419; BAB02955.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76198.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76199.1; -; Genomic_DNA.
DR EMBL; BX826140; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK229307; BAF01170.1; -; mRNA.
DR RefSeq; NP_188546.1; NM_112802.4. [Q0WNX9-1]
DR RefSeq; NP_974338.1; NM_202609.3. [Q0WNX9-2]
DR AlphaFoldDB; Q0WNX9; -.
DR BioGRID; 6782; 25.
DR DIP; DIP-38668N; -.
DR IntAct; Q0WNX9; 9.
DR STRING; 3702.AT3G19150.1; -.
DR iPTMnet; Q0WNX9; -.
DR PaxDb; Q0WNX9; -.
DR PRIDE; Q0WNX9; -.
DR ProteomicsDB; 250766; -. [Q0WNX9-1]
DR EnsemblPlants; AT3G19150.1; AT3G19150.1; AT3G19150. [Q0WNX9-1]
DR EnsemblPlants; AT3G19150.2; AT3G19150.2; AT3G19150. [Q0WNX9-2]
DR GeneID; 821449; -.
DR Gramene; AT3G19150.1; AT3G19150.1; AT3G19150. [Q0WNX9-1]
DR Gramene; AT3G19150.2; AT3G19150.2; AT3G19150. [Q0WNX9-2]
DR KEGG; ath:AT3G19150; -.
DR Araport; AT3G19150; -.
DR TAIR; locus:2094118; AT3G19150.
DR HOGENOM; CLU_083146_2_0_1; -.
DR InParanoid; Q0WNX9; -.
DR OMA; STQGRCS; -.
DR PhylomeDB; Q0WNX9; -.
DR PRO; PR:Q0WNX9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WNX9; baseline and differential.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IEA:InterPro.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:TAIR.
DR Gene3D; 4.10.365.10; -; 1.
DR InterPro; IPR003175; CDI_dom.
DR InterPro; IPR044898; CDI_dom_sf.
DR InterPro; IPR044275; KRP.
DR PANTHER; PTHR46776; PTHR46776; 1.
DR Pfam; PF02234; CDI; 1.
DR PIRSF; PIRSF017811; CDK_inhib_pln; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Nucleus; Phosphoprotein;
KW Protein kinase inhibitor; Reference proteome; Ubl conjugation.
FT CHAIN 1..196
FT /note="Cyclin-dependent kinase inhibitor 6"
FT /id="PRO_0000294090"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphothreonine; by KIN10"
FT /evidence="ECO:0000269|PubMed:23617622"
FT VAR_SEQ 177..196
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036333"
FT MUTAGEN 152
FT /note="T->A: Abolishes its phosphorylation."
FT /evidence="ECO:0000269|PubMed:23617622"
FT MUTAGEN 152
FT /note="T->D: Abolishes its phosphorylation. Reduces its
FT ability to interact with CYCD3-1."
FT /evidence="ECO:0000269|PubMed:23617622"
FT CONFLICT 87
FT /note="A -> S (in Ref. 6; BAF01170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 21454 MW; AC543304CE6B92C4 CRC64;
MSERKRELAE EASSTSFSPL KKTKLNDSSD SSPDSHDVIV FAVSSSSVAS SAALASDECS
VTIGGEESDQ SSSISSGCFT SESKEIAKNS SSFGVDLEDH QIETETETST FITSNFRKET
SPVSEGLGET TTEMESSSAT KRKQPGVRKT PTAAEIEDLF SELESQDDKK KQFIEKYNFD
IVNDEPLEGR YKWDRL
