KRP2_ARATH
ID KRP2_ARATH Reviewed; 209 AA.
AC Q9SCR2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cyclin-dependent kinase inhibitor 2;
DE AltName: Full=Inhibitor/interactor of CDK protein 2;
DE AltName: Full=KIP-related protein 2;
GN Name=KRP2; Synonyms=ICK2; OrderedLocusNames=At3g50630; ORFNames=T3A5.10;
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 INTERACTION WITH CDKA-1.
RX PubMed=10758489; DOI=10.1046/j.1365-313x.2000.00688.x;
RA Lui H., Wang H., Delong C., Fowke L.C., Crosby W.L., Fobert P.R.;
RT "The Arabidopsis Cdc2a-interacting protein ICK2 is structurally related to
RT ICK1 and is a potent inhibitor of cyclin-dependent kinase activity in
RT vitro.";
RL Plant J. 21:379-385(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CDKA-1.
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 [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=12000456; DOI=10.1046/j.1365-313x.2002.01274.x;
RA Menges M., Murray J.A.H.;
RT "Synchronous Arabidopsis suspension cultures for analysis of cell-cycle
RT gene activity.";
RL Plant J. 30:203-212(2002).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12368490; DOI=10.1105/tpc.004960;
RA Himanen K., Boucheron E., Vanneste S., de Almeida Engler J., Inze D.,
RA Beeckman T.;
RT "Auxin-mediated cell cycle activation during early lateral root
RT initiation.";
RL Plant Cell 14:2339-2351(2002).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND INTERACTION WITH
RP CDKA-1.
RX PubMed=15863515; DOI=10.1105/tpc.105.032383;
RA Verkest A., de Oliveira Manes C.L., Vercruysse S., Maes S.,
RA van der Schueren E., Beeckman T., Genschik P., Kuiper M., Inze D.,
RA de Veylder L.;
RT "The cyclin-dependent kinase inhibitor KRP2 controls the onset of the
RT endoreduplication cycle during Arabidopsis leaf development through
RT inhibition of mitotic CDKA;1 kinase complexes.";
RL Plant Cell 17:1723-1736(2005).
RN [11]
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 [12]
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).
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 regulate early lateral root initiation by
CC blocking the G1/S phase transition. Controls the mitosis-to-endocycle
CC transition and the onset of the endoreduplication cycle during leaf
CC development through inhibition of mitotic CDKA-1 kinase complexes.
CC Specifically targets CDKA-1. {ECO:0000269|PubMed:11449057,
CC ECO:0000269|PubMed:12368490, ECO:0000269|PubMed:15863515,
CC ECO:0000269|PubMed:16376885}.
CC -!- SUBUNIT: Specifically interacts with CDKA-1, but not with CDKB1-1.
CC {ECO:0000269|PubMed:10758489, ECO:0000269|PubMed:11449057,
CC ECO:0000269|PubMed:15863515}.
CC -!- INTERACTION:
CC Q9SCR2; P24100: CDKA-1; NbExp=6; IntAct=EBI-1636748, EBI-371713;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17253089}. Note=Homogeneously distributed.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in root pericycle and cell
CC suspension culture during cell cycle arrest. Expressed early in the G1
CC phase and then disappears. More abundant in endoreduplicating than in
CC mitotically dividing tissues (at protein level).
CC {ECO:0000269|PubMed:12000456, ECO:0000269|PubMed:12368490,
CC ECO:0000269|PubMed:15863515}.
CC -!- INDUCTION: Down-regulated by auxin in roots.
CC {ECO:0000269|PubMed:12368490}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15863515}.
CC -!- MISCELLANEOUS: Treatment with auxin induces lateral root initiation.
CC ICK2/KRP2 protein abundance is regulated post-transcriptionally through
CC CDK phosphorylation and proteasomal degradation.
CC -!- SIMILARITY: Belongs to the CDI family. ICK/KRP subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ251851; CAB76424.1; -; mRNA.
DR EMBL; AL132979; CAB62432.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78687.1; -; Genomic_DNA.
DR EMBL; AK176528; BAD44291.1; -; mRNA.
DR EMBL; AK176728; BAD44491.1; -; mRNA.
DR EMBL; BT028944; ABI49491.1; -; mRNA.
DR EMBL; AY088290; AAM65829.1; -; mRNA.
DR PIR; T46140; T46140.
DR RefSeq; NP_190632.1; NM_114923.4.
DR AlphaFoldDB; Q9SCR2; -.
DR BioGRID; 9544; 42.
DR IntAct; Q9SCR2; 29.
DR STRING; 3702.AT3G50630.1; -.
DR PaxDb; Q9SCR2; -.
DR PRIDE; Q9SCR2; -.
DR ProteomicsDB; 250709; -.
DR EnsemblPlants; AT3G50630.1; AT3G50630.1; AT3G50630.
DR GeneID; 824226; -.
DR Gramene; AT3G50630.1; AT3G50630.1; AT3G50630.
DR KEGG; ath:AT3G50630; -.
DR Araport; AT3G50630; -.
DR TAIR; locus:2101679; AT3G50630.
DR eggNOG; ENOG502R7BY; Eukaryota.
DR HOGENOM; CLU_110872_0_0_1; -.
DR InParanoid; Q9SCR2; -.
DR OMA; LECSMKY; -.
DR OrthoDB; 1498410at2759; -.
DR PhylomeDB; Q9SCR2; -.
DR PRO; PR:Q9SCR2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCR2; baseline and differential.
DR Genevisible; Q9SCR2; AT.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IGI:TAIR.
DR GO; GO:0019210; F:kinase inhibitor activity; IDA:TAIR.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
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 Cell cycle; Nucleus; Phosphoprotein; Protein kinase inhibitor;
KW Reference proteome.
FT CHAIN 1..209
FT /note="Cyclin-dependent kinase inhibitor 2"
FT /id="PRO_0000294088"
FT REGION 1..32
FT /note="Required for nuclear localization"
SQ SEQUENCE 209 AA; 24037 MW; 0E5EEFE9ED256B53 CRC64;
MAAVRRRERD VVEENGVTTT TVKRRKMEEE VDLVESRIIL SPCVQATNRG GIVARNSAGA
SETSVVIVRR RDSPPVEEQC QIEEEDSSVS CCSTSEEKSK RRIEFVDLEE NNGDDRETET
SWIYDDLNKS EESMNMDSSS VAVEDVESRR RLRKSLHETV KEAELEDFFQ VAEKDLRNKL
LECSMKYNFD FEKDEPLGGG RYEWVKLNP