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KRP7_ARATH
ID   KRP7_ARATH              Reviewed;         195 AA.
AC   Q94CL9; Q9FX90;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 7;
DE   AltName: Full=Inhibitor/interactor of CDK protein 5;
DE   AltName: Full=KIP-related protein 7;
GN   Name=KRP7; Synonyms=ICK5; OrderedLocusNames=At1g49620; ORFNames=F14J22.14;
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], TISSUE SPECIFICITY, AND INTERACTION WITH CDKA-1
RP   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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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   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   [5]
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   [6]
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   [7]
RP   PHOSPHORYLATION AT THR-151, AND IDENTIFICATION BY MASS SPECTROMETRY.
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       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   -!- INTERACTION:
CC       Q94CL9; P24100: CDKA-1; NbExp=3; IntAct=EBI-1773344, EBI-371713;
CC       Q94CL9; Q8LGA1: CYCD4-1; NbExp=2; IntAct=EBI-1773344, EBI-1253202;
CC       Q94CL9; Q8W104: FBL17; NbExp=4; IntAct=EBI-1773344, EBI-2026732;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:17253089, ECO:0000269|PubMed:18948957}.
CC       Note=Homogeneously distributed. Accumulates strongly in vegetative cell
CC       nuclei immediately after asymmetric division and disappears later.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers, in developing pollen, and at
CC       lower levels in roots and leaves. {ECO:0000269|PubMed:11449057,
CC       ECO:0000269|PubMed:18948957}.
CC   -!- DEVELOPMENTAL STAGE: Present in uninucleate microspore and bicellular
CC       pollen. {ECO:0000269|PubMed:18948957}.
CC   -!- PTM: Ubiquitinated by SCF(FBL17). Ubiquitination leads to its
CC       subsequent degradation, thus controlling cell cycle progression.
CC       {ECO:0000269|PubMed:18948957}.
CC   -!- SIMILARITY: Belongs to the CDI family. ICK/KRP subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ301558; CAC41621.1; -; mRNA.
DR   EMBL; AC011807; AAG13048.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32450.1; -; Genomic_DNA.
DR   PIR; H96532; H96532.
DR   RefSeq; NP_175385.1; NM_103850.2.
DR   AlphaFoldDB; Q94CL9; -.
DR   SMR; Q94CL9; -.
DR   BioGRID; 26611; 25.
DR   DIP; DIP-40167N; -.
DR   IntAct; Q94CL9; 12.
DR   STRING; 3702.AT1G49620.1; -.
DR   iPTMnet; Q94CL9; -.
DR   PaxDb; Q94CL9; -.
DR   PRIDE; Q94CL9; -.
DR   EnsemblPlants; AT1G49620.1; AT1G49620.1; AT1G49620.
DR   GeneID; 841386; -.
DR   Gramene; AT1G49620.1; AT1G49620.1; AT1G49620.
DR   KEGG; ath:AT1G49620; -.
DR   Araport; AT1G49620; -.
DR   TAIR; locus:2012186; AT1G49620.
DR   eggNOG; ENOG502R7GZ; Eukaryota.
DR   HOGENOM; CLU_083146_2_0_1; -.
DR   InParanoid; Q94CL9; -.
DR   OMA; DEMESPA; -.
DR   PhylomeDB; Q94CL9; -.
DR   PRO; PR:Q94CL9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q94CL9; baseline and differential.
DR   Genevisible; Q94CL9; AT.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:UniProtKB.
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: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   Cell cycle; Nucleus; Phosphoprotein; Protein kinase inhibitor;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..195
FT                   /note="Cyclin-dependent kinase inhibitor 7"
FT                   /id="PRO_0000294091"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="Phosphothreonine; by KIN10"
FT                   /evidence="ECO:0000269|PubMed:23617622"
FT   CONFLICT        67
FT                   /note="L -> R (in Ref. 1; CAC41621)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  21965 MW;  6A7E0867B752E5FF CRC64;
     MSETKPKRDS EYEGSNIKRM RLDDDDDVLR SPTRTLSSSS SSSLAYSVSD SGGFCSVALS
     EEEDDHLSSS ISSGCSSSET NEIATRLPFS DLEAHEISET EISTLLTNNF RKQGISSSEN
     LGETAEMDSA TTEMRDQRKT EKKKKMEKSP TQAELDDFFS AAERYEQKRF TEKYNYDIVN
     DTPLEGRYQW VSLKP
 
 
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