KRP4_ARATH
ID KRP4_ARATH Reviewed; 289 AA.
AC Q8GYJ3; O48846; Q94CM0; Q9FR83;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Cyclin-dependent kinase inhibitor 4;
DE AltName: Full=Inhibitor/interactor of CDK protein 7;
DE AltName: Full=KIP-related protein 4;
GN Name=KRP4; Synonyms=ACK2, ICK7; OrderedLocusNames=At2g32710;
GN ORFNames=F24L7.15;
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 2), 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 [MRNA] (ISOFORM 1).
RA Park S.C., Cho J.W.;
RT "A novel cyclin-dependent kinase inhibitor (ACK2) interacting with G1
RT specific cyclin.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
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 [8]
RP INTERACTION WITH FBL17.
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).
CC -!- FUNCTION: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity.
CC May target specifically CDKA-1. {ECO:0000269|PubMed:16376885}.
CC -!- SUBUNIT: Specifically interacts with CDKA-1, but not with CDKB1-1.
CC Interacts with CYCD4-1. Binds to FBL17. {ECO:0000269|PubMed:11449057,
CC ECO:0000269|PubMed:18948957}.
CC -!- INTERACTION:
CC Q8GYJ3; P24100: CDKA-1; NbExp=4; IntAct=EBI-1253225, EBI-371713;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17253089}. Note=Distributed in a ponctuate pattern.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GYJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GYJ3-2; Sequence=VSP_026589;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers and at lower levels
CC in roots. {ECO:0000269|PubMed:11449057}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CDI family. ICK/KRP subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ301555; CAC41618.1; -; mRNA.
DR EMBL; AF123315; AAG41215.1; -; mRNA.
DR EMBL; AC003974; AAC04492.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08727.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08728.1; -; Genomic_DNA.
DR EMBL; AK117586; BAC42243.1; -; mRNA.
DR PIR; T00797; T00797.
DR RefSeq; NP_565750.1; NM_128830.4. [Q8GYJ3-1]
DR RefSeq; NP_850196.1; NM_179865.2. [Q8GYJ3-2]
DR AlphaFoldDB; Q8GYJ3; -.
DR BioGRID; 3178; 40.
DR DIP; DIP-38682N; -.
DR IntAct; Q8GYJ3; 17.
DR STRING; 3702.AT2G32710.1; -.
DR iPTMnet; Q8GYJ3; -.
DR PaxDb; Q8GYJ3; -.
DR PRIDE; Q8GYJ3; -.
DR ProteomicsDB; 237108; -. [Q8GYJ3-1]
DR EnsemblPlants; AT2G32710.1; AT2G32710.1; AT2G32710. [Q8GYJ3-1]
DR EnsemblPlants; AT2G32710.2; AT2G32710.2; AT2G32710. [Q8GYJ3-2]
DR GeneID; 817831; -.
DR Gramene; AT2G32710.1; AT2G32710.1; AT2G32710. [Q8GYJ3-1]
DR Gramene; AT2G32710.2; AT2G32710.2; AT2G32710. [Q8GYJ3-2]
DR KEGG; ath:AT2G32710; -.
DR Araport; AT2G32710; -.
DR TAIR; locus:2046427; AT2G32710.
DR eggNOG; ENOG502QXA1; Eukaryota.
DR InParanoid; Q8GYJ3; -.
DR OMA; SREMDEF; -.
DR PhylomeDB; Q8GYJ3; -.
DR PRO; PR:Q8GYJ3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GYJ3; baseline and differential.
DR Genevisible; Q8GYJ3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IGI:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; TAS: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 Alternative splicing; Cell cycle; Nucleus; Protein kinase inhibitor;
KW Reference proteome.
FT CHAIN 1..289
FT /note="Cyclin-dependent kinase inhibitor 4"
FT /id="PRO_0000294093"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 193..195
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11449057,
FT ECO:0000303|PubMed:11910074"
FT /id="VSP_026589"
FT CONFLICT 90
FT /note="K -> R (in Ref. 5; BAC42243)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="D -> G (in Ref. 5; BAC42243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32068 MW; BD7F524A308E11CF CRC64;
MGKYIRKSKI DGAGAGAGGG GGGGGGGESS IALMDVVSPS SSSSLGVLTR AKSLALQQQQ
QRCLLQKPSS PSSLPPTSAS PNPPSKQKMK KKQQQMNDCG SYLQLRSRRL QKKPPIVVIR
STKRRKQQRR NETCGRNPNP RSNLDSIRGD GSRSDSVSES VVFGKDKDLI SEINKDPTFG
QNFFDLEEEH TQSFNRTTRE STPCSLIRRP EIMTTPGSST KLNICVSESN QREDSLSRSH
RRRPTTPEMD EFFSGAEEEQ QKQFIEKYNF DPVNEQPLPG RFEWTKVDD
