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CCD31_ARATH
ID   CCD31_ARATH             Reviewed;         376 AA.
AC   P42753; O49489; Q56XG2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Cyclin-D3-1;
DE   AltName: Full=Cyclin-delta-3;
DE            Short=Cyclin-d3;
DE   AltName: Full=G1/S-specific cyclin-D3-1;
DE            Short=CycD3;1;
GN   Name=CYCD3-1; Synonyms=CYCD3; OrderedLocusNames=At4g34160;
GN   ORFNames=F28A23.80;
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 INDUCTION.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX   PubMed=7696881; DOI=10.2307/3869840;
RA   Soni R., Carmichael J.P., Shah Z.H., Murray J.A.H.;
RT   "A family of cyclin D homologs from plants differentially controlled by
RT   growth regulators and containing the conserved retinoblastoma protein
RT   interaction motif.";
RL   Plant Cell 7:85-103(1995).
RN   [2]
RP   SEQUENCE REVISION TO 371.
RA   Murray J.A.H.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8938409; DOI=10.1104/pp.112.3.1023;
RA   Fuerst R.A.U., Soni R., Murray J.A.H., Lindsey K.;
RT   "Modulation of cyclin transcript levels in cultured cells of Arabidopsis
RT   thaliana.";
RL   Plant Physiol. 112:1023-1033(1996).
RN   [7]
RP   INTERACTION WITH CDKA-1 AND KRP1/ICK1.
RX   PubMed=9753775; DOI=10.1046/j.1365-313x.1998.00231.x;
RA   Wang H., Qi Q., Schorr P., Cutler A.J., Crosby W.L., Fowke L.C.;
RT   "ICK1, a cyclin-dependent protein kinase inhibitor from Arabidopsis
RT   thaliana interacts with both Cdc2a and CycD3, and its expression is induced
RT   by abscisic acid.";
RL   Plant J. 15:501-510(1998).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=10066178; DOI=10.1126/science.283.5407.1541;
RA   Riou-Khamlichi C., Huntley R., Jacqmard A., Murray J.A.H.;
RT   "Cytokinin activation of Arabidopsis cell division through a D-type
RT   cyclin.";
RL   Science 283:1541-1544(1999).
RN   [9]
RP   INDUCTION.
RX   PubMed=10848578; DOI=10.1128/mcb.20.13.4513-4521.2000;
RA   Riou-Khamlichi C., Menges M., Healy J.M.S., Murray J.A.H.;
RT   "Sugar control of the plant cell cycle: differential regulation of
RT   Arabidopsis D-type cyclin gene expression.";
RL   Mol. Cell. Biol. 20:4513-4521(2000).
RN   [10]
RP   INDUCTION.
RX   PubMed=11123807; DOI=10.1046/j.1365-313x.2000.00915.x;
RA   Hu Y., Bao F., Li J.;
RT   "Promotive effect of brassinosteroids on cell division involves a distinct
RT   CycD3-induction pathway in Arabidopsis.";
RL   Plant J. 24:693-701(2000).
RN   [11]
RP   INTERACTION WITH CDKA-1.
RX   PubMed=11096103; DOI=10.1074/jbc.m009074200;
RA   Healy J.M.S., Menges M., Doonan J.H., Murray J.A.H.;
RT   "The Arabidopsis D-type cyclins CycD2 and CycD3 both interact in vivo with
RT   the PSTAIRE cyclin-dependent kinase Cdc2a but are differentially
RT   controlled.";
RL   J. Biol. Chem. 276:7041-7047(2001).
RN   [12]
RP   FUNCTION.
RX   PubMed=11983922; DOI=10.1073/pnas.092657299;
RA   Schnittger A., Schoebinger U., Bouyer D., Weinl C., Stierhof Y.-D.,
RA   Huelskamp M.;
RT   "Ectopic D-type cyclin expression induces not only DNA replication but also
RT   cell division in Arabidopsis trichomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:6410-6415(2002).
RN   [13]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12509523; DOI=10.1105/tpc.004838;
RA   Dewitte W., Riou-Khamlichi C., Scofield S., Healy J.M.S., Jacqmard A.,
RA   Kilby N.J., Murray J.A.H.;
RT   "Altered cell cycle distribution, hyperplasia, and inhibited
RT   differentiation in Arabidopsis caused by the D-type cyclin CYCD3.";
RL   Plant Cell 15:79-92(2003).
RN   [14]
RP   INTERACTION WITH KRP1/ICK1.
RX   PubMed=12566574; DOI=10.1105/tpc.008342;
RA   Schnittger A., Weinl C., Bouyer D., Schoebinger U., Huelskamp M.;
RT   "Misexpression of the cyclin-dependent kinase inhibitor ICK1/KRP1 in
RT   single-celled Arabidopsis trichomes reduces endoreduplication and cell size
RT   and induces cell death.";
RL   Plant Cell 15:303-315(2003).
RN   [15]
RP   INDUCTION, AND PHOSPHORYLATION.
RX   PubMed=15125768; DOI=10.1111/j.0960-7412.2004.02071.x;
RA   Planchais S., Samland A.K., Murray J.A.H.;
RT   "Differential stability of Arabidopsis D-type cyclins: CYCD3;1 is a highly
RT   unstable protein degraded by a proteasome-dependent mechanism.";
RL   Plant J. 38:616-625(2004).
RN   [16]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15208425; DOI=10.1104/pp.104.040436;
RA   Wang G., Kong H., Sun Y., Zhang X., Zhang W., Altman N., dePamphilis C.W.,
RA   Ma H.;
RT   "Genome-wide analysis of the cyclin family in Arabidopsis and comparative
RT   phylogenetic analysis of plant cyclin-like proteins.";
RL   Plant Physiol. 135:1084-1099(2004).
RN   [17]
RP   FUNCTION.
RX   PubMed=16227434; DOI=10.1073/pnas.0507581102;
RA   Masubelele N.H., Dewitte W., Menges M., Maughan S., Collins C., Huntley R.,
RA   Nieuwland J., Scofield S., Murray J.A.H.;
RT   "D-type cyclins activate division in the root apex to promote seed
RT   germination in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:15694-15699(2005).
RN   [18]
RP   FUNCTION, PHOSPHORYLATION, INTERACTION WITH CDKA-1, AND MUTAGENESIS OF
RP   SER-343.
RX   PubMed=16517759; DOI=10.1105/tpc.105.039636;
RA   Menges M., Samland A.K., Planchais S., Murray J.A.H.;
RT   "The D-type cyclin CYCD3;1 is limiting for the G1-to-S-phase transition in
RT   Arabidopsis.";
RL   Plant Cell 18:893-906(2006).
RN   [19]
RP   INTERACTION WITH KRP6.
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).
RN   [20]
RP   FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=24687979; DOI=10.1093/jxb/eru139;
RA   Yang K., Wang H., Xue S., Qu X., Zou J., Le J.;
RT   "Requirement for A-type cyclin-dependent kinase and cyclins for the
RT   terminal division in the stomatal lineage of Arabidopsis.";
RL   J. Exp. Bot. 65:2449-2461(2014).
CC   -!- FUNCTION: Involved in the control of the cell cycle at the G1/S (start)
CC       transition. Activates the G1/S phase transition in response to
CC       cytokinin hormone signal, but declines in response to sucrose
CC       starvation leading to G1 arrest. Involved in the induction of mitotic
CC       cell division. Plays an important role in the switch from cell
CC       proliferation to the final stages of differentiation during plant
CC       development. May not be involved in the activation of cell cycle in the
CC       root apical meristem (RAM) in the early phase of seed germination.
CC       Promotes divisions in the guard cells (GCs) after the guard mother
CC       cells (GMC) symmetric division (PubMed:24687979).
CC       {ECO:0000269|PubMed:10066178, ECO:0000269|PubMed:11983922,
CC       ECO:0000269|PubMed:12509523, ECO:0000269|PubMed:16227434,
CC       ECO:0000269|PubMed:16517759, ECO:0000269|PubMed:24687979}.
CC   -!- SUBUNIT: Interacts with the C-terminal domain of CDKA-1. Interacts with
CC       KRP1/ICK1. Interacts with KRP6 (PubMed:23617622).
CC       {ECO:0000269|PubMed:11096103, ECO:0000269|PubMed:12566574,
CC       ECO:0000269|PubMed:16517759, ECO:0000269|PubMed:23617622,
CC       ECO:0000269|PubMed:9753775}.
CC   -!- INTERACTION:
CC       P42753; P24100: CDKA-1; NbExp=5; IntAct=EBI-1253610, EBI-371713;
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC       leaves and flowers. Expressed in vegetative shoot meristem and
CC       inflorescence. {ECO:0000269|PubMed:10066178,
CC       ECO:0000269|PubMed:12509523, ECO:0000269|PubMed:7696881}.
CC   -!- DEVELOPMENTAL STAGE: Expressed 2 hours before the S phase and remains
CC       constant therafter. {ECO:0000269|PubMed:10066178,
CC       ECO:0000269|PubMed:8938409}.
CC   -!- INDUCTION: By cytokinin. Induction by cytokinin is blocked by auxin,
CC       but not by cycloheximide. Induced by sucrose and glucose. Induced by
CC       24-epi-brassinolide. Down-regulated by sucrose starvation.
CC       {ECO:0000269|PubMed:10066178, ECO:0000269|PubMed:10848578,
CC       ECO:0000269|PubMed:11123807, ECO:0000269|PubMed:15125768,
CC       ECO:0000269|PubMed:7696881}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15125768,
CC       ECO:0000269|PubMed:16517759}.
CC   -!- MISCELLANEOUS: Plants overexpressing CYCD3-1 show extensive leaf
CC       curling, disorganized meristems, increased leaf number, late flowering
CC       and delayed senescence. CYCD3-1 is a highly unstable protein whose
CC       proteolysis is mediated by a proteasome-dependent pathway, and whose
CC       levels are highly dependent on the rate of protein synthesis.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X83371; CAA58287.1; -; mRNA.
DR   EMBL; AL021961; CAA17556.1; -; Genomic_DNA.
DR   EMBL; AL161584; CAB80133.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86335.1; -; Genomic_DNA.
DR   EMBL; AK221712; BAD95437.1; -; mRNA.
DR   PIR; T05420; T05420.
DR   RefSeq; NP_195142.1; NM_119579.3.
DR   AlphaFoldDB; P42753; -.
DR   SMR; P42753; -.
DR   BioGRID; 14846; 14.
DR   ELM; P42753; -.
DR   IntAct; P42753; 9.
DR   STRING; 3702.AT4G34160.1; -.
DR   PaxDb; P42753; -.
DR   PRIDE; P42753; -.
DR   EnsemblPlants; AT4G34160.1; AT4G34160.1; AT4G34160.
DR   GeneID; 829564; -.
DR   Gramene; AT4G34160.1; AT4G34160.1; AT4G34160.
DR   KEGG; ath:AT4G34160; -.
DR   Araport; AT4G34160; -.
DR   TAIR; locus:2124331; AT4G34160.
DR   eggNOG; KOG0656; Eukaryota.
DR   HOGENOM; CLU_048040_0_0_1; -.
DR   InParanoid; P42753; -.
DR   OMA; RKYDENP; -.
DR   OrthoDB; 1234739at2759; -.
DR   PhylomeDB; P42753; -.
DR   PRO; PR:P42753; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P42753; baseline and differential.
DR   Genevisible; P42753; AT.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:TAIR.
DR   GO; GO:0010444; P:guard mother cell differentiation; IMP:UniProtKB.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR   GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR   GO; GO:0048316; P:seed development; IGI:TAIR.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Mitosis; Reference proteome.
FT   CHAIN           1..376
FT                   /note="Cyclin-D3-1"
FT                   /id="PRO_0000080447"
FT   REGION          298..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         343
FT                   /note="S->A: Alteration of the cell cycle regulatory
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:16517759"
FT   CONFLICT        288
FT                   /note="G -> C (in Ref. 1; CAA58287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  42702 MW;  FFC95F2B8031BEC2 CRC64;
     MAIRKEEESR EEQSNSFLLD ALYCEEEKWD DEGEEVEENS SLSSSSSPFV VLQQDLFWED
     EDLVTLFSKE EEQGLSCLDD VYLSTDRKEA VGWILRVNAH YGFSTLAAVL AITYLDKFIC
     SYSLQRDKPW MLQLVSVACL SLAAKVEETQ VPLLLDFQVE ETKYVFEAKT IQRMELLILS
     TLEWKMHLIT PISFVDHIIR RLGLKNNAHW DFLNKCHRLL LSVISDSRFV GYLPSVVAAA
     TMMRIIEQVD PFDPLSYQTN LLGVLNLTKE KVKTCYDLIL QLPVDRIGLQ IQIQSSKKRK
     SHDSSSSLNS PSCVIDANPF NSDESSNDSW SASSCNPPTS SSSPQQQPPL KKMRGAEENE
     KKKPILHLPW AIVATP
 
 
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