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Protein

Cyclin-D3-1

Gene

CYCD3-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the control of the cell cycle at the G1/S (start) transition. Activates the G1/S phase transition in response to cytokinin hormone signal, but declines in response to sucrose starvation leading to G1 arrest. Involved in the induction of mitotic cell division. Plays an important role in the switch from cell proliferation to the final stages of differentiation during plant development. May not be involved in the activation of cell cycle in the root apical meristem (RAM) in the early phase of seed germination.5 Publications

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • G1/S transition of mitotic cell cycle Source: TAIR
  • mitotic nuclear division Source: UniProtKB-KW
  • response to cytokinin Source: TAIR
  • response to sucrose Source: TAIR
  • seed development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-D3-1
Alternative name(s):
Cyclin-delta-3
Short name:
Cyclin-d3
G1/S-specific cyclin-D3-1
Short name:
CycD3;1
Gene namesi
Name:CYCD3-1
Synonyms:CYCD3
Ordered Locus Names:At4g34160
ORF Names:F28A23.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G34160.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi343 – 3431S → A: Alteration of the cell cycle regulatory activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Cyclin-D3-1PRO_0000080447Add
BLAST

Post-translational modificationi

Phosphorylated.2 Publications

Proteomic databases

PaxDbiP42753.

PTM databases

iPTMnetiP42753.

Expressioni

Tissue specificityi

Highly expressed in roots and at lower levels in leaves and flowers. Expressed in vegetative shoot meristem and inflorescence.3 Publications

Developmental stagei

Expressed 2 hours before the S phase and remains constant therafter.2 Publications

Inductioni

By cytokinin. Induction by cytokinin is blocked by auxin, but not by cycloheximide. Induced by sucrose and glucose. Induced by 24-epi-brassinolide. Down-regulated by sucrose starvation.5 Publications

Gene expression databases

GenevisibleiP42753. AT.

Interactioni

Subunit structurei

Interacts with the C-terminal domain of CDKA-1. Interacts with KRP1/ICK1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDKA-1P241005EBI-1253610,EBI-371713

Protein-protein interaction databases

BioGridi14846. 14 interactions.
IntActiP42753. 9 interactions.
STRINGi3702.AT4G34160.1.

Structurei

3D structure databases

ProteinModelPortaliP42753.
SMRiP42753. Positions 87-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin D subfamily.Curated

Phylogenomic databases

eggNOGiKOG0656. Eukaryota.
ENOG410XRKC. LUCA.
HOGENOMiHOG000242458.
InParanoidiP42753.
KOiK14505.
OMAiFLNKCHR.
PhylomeDBiP42753.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIRKEEESR EEQSNSFLLD ALYCEEEKWD DEGEEVEENS SLSSSSSPFV
60 70 80 90 100
VLQQDLFWED EDLVTLFSKE EEQGLSCLDD VYLSTDRKEA VGWILRVNAH
110 120 130 140 150
YGFSTLAAVL AITYLDKFIC SYSLQRDKPW MLQLVSVACL SLAAKVEETQ
160 170 180 190 200
VPLLLDFQVE ETKYVFEAKT IQRMELLILS TLEWKMHLIT PISFVDHIIR
210 220 230 240 250
RLGLKNNAHW DFLNKCHRLL LSVISDSRFV GYLPSVVAAA TMMRIIEQVD
260 270 280 290 300
PFDPLSYQTN LLGVLNLTKE KVKTCYDLIL QLPVDRIGLQ IQIQSSKKRK
310 320 330 340 350
SHDSSSSLNS PSCVIDANPF NSDESSNDSW SASSCNPPTS SSSPQQQPPL
360 370
KKMRGAEENE KKKPILHLPW AIVATP
Length:376
Mass (Da):42,702
Last modified:February 15, 2005 - v3
Checksum:iFFC95F2B8031BEC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881G → C in CAA58287 (PubMed:7696881).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83371 mRNA. Translation: CAA58287.1.
AL021961 Genomic DNA. Translation: CAA17556.1.
AL161584 Genomic DNA. Translation: CAB80133.1.
CP002687 Genomic DNA. Translation: AEE86335.1.
AK221712 mRNA. Translation: BAD95437.1.
PIRiT05420.
RefSeqiNP_195142.1. NM_119579.2.
UniGeneiAt.22721.

Genome annotation databases

EnsemblPlantsiAT4G34160.1; AT4G34160.1; AT4G34160.
GeneIDi829564.
GrameneiAT4G34160.1; AT4G34160.1; AT4G34160.
KEGGiath:AT4G34160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83371 mRNA. Translation: CAA58287.1.
AL021961 Genomic DNA. Translation: CAA17556.1.
AL161584 Genomic DNA. Translation: CAB80133.1.
CP002687 Genomic DNA. Translation: AEE86335.1.
AK221712 mRNA. Translation: BAD95437.1.
PIRiT05420.
RefSeqiNP_195142.1. NM_119579.2.
UniGeneiAt.22721.

3D structure databases

ProteinModelPortaliP42753.
SMRiP42753. Positions 87-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14846. 14 interactions.
IntActiP42753. 9 interactions.
STRINGi3702.AT4G34160.1.

PTM databases

iPTMnetiP42753.

Proteomic databases

PaxDbiP42753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G34160.1; AT4G34160.1; AT4G34160.
GeneIDi829564.
GrameneiAT4G34160.1; AT4G34160.1; AT4G34160.
KEGGiath:AT4G34160.

Organism-specific databases

TAIRiAT4G34160.

Phylogenomic databases

eggNOGiKOG0656. Eukaryota.
ENOG410XRKC. LUCA.
HOGENOMiHOG000242458.
InParanoidiP42753.
KOiK14505.
OMAiFLNKCHR.
PhylomeDBiP42753.

Miscellaneous databases

PROiP42753.

Gene expression databases

GenevisibleiP42753. AT.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of cyclin D homologs from plants differentially controlled by growth regulators and containing the conserved retinoblastoma protein interaction motif."
    Soni R., Carmichael J.P., Shah Z.H., Murray J.A.H.
    Plant Cell 7:85-103(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Landsberg erecta.
    Tissue: Seedling.
  2. Murray J.A.H.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 371.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Modulation of cyclin transcript levels in cultured cells of Arabidopsis thaliana."
    Fuerst R.A.U., Soni R., Murray J.A.H., Lindsey K.
    Plant Physiol. 112:1023-1033(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  7. "ICK1, a cyclin-dependent protein kinase inhibitor from Arabidopsis thaliana interacts with both Cdc2a and CycD3, and its expression is induced by abscisic acid."
    Wang H., Qi Q., Schorr P., Cutler A.J., Crosby W.L., Fowke L.C.
    Plant J. 15:501-510(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKA-1 AND KRP1/ICK1.
  8. "Cytokinin activation of Arabidopsis cell division through a D-type cyclin."
    Riou-Khamlichi C., Huntley R., Jacqmard A., Murray J.A.H.
    Science 283:1541-1544(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
  9. "Sugar control of the plant cell cycle: differential regulation of Arabidopsis D-type cyclin gene expression."
    Riou-Khamlichi C., Menges M., Healy J.M.S., Murray J.A.H.
    Mol. Cell. Biol. 20:4513-4521(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Promotive effect of brassinosteroids on cell division involves a distinct CycD3-induction pathway in Arabidopsis."
    Hu Y., Bao F., Li J.
    Plant J. 24:693-701(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "The Arabidopsis D-type cyclins CycD2 and CycD3 both interact in vivo with the PSTAIRE cyclin-dependent kinase Cdc2a but are differentially controlled."
    Healy J.M.S., Menges M., Doonan J.H., Murray J.A.H.
    J. Biol. Chem. 276:7041-7047(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKA-1.
  12. "Ectopic D-type cyclin expression induces not only DNA replication but also cell division in Arabidopsis trichomes."
    Schnittger A., Schoebinger U., Bouyer D., Weinl C., Stierhof Y.-D., Huelskamp M.
    Proc. Natl. Acad. Sci. U.S.A. 99:6410-6415(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Altered cell cycle distribution, hyperplasia, and inhibited differentiation in Arabidopsis caused by the D-type cyclin CYCD3."
    Dewitte W., Riou-Khamlichi C., Scofield S., Healy J.M.S., Jacqmard A., Kilby N.J., Murray J.A.H.
    Plant Cell 15:79-92(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  14. "Misexpression of the cyclin-dependent kinase inhibitor ICK1/KRP1 in single-celled Arabidopsis trichomes reduces endoreduplication and cell size and induces cell death."
    Schnittger A., Weinl C., Bouyer D., Schoebinger U., Huelskamp M.
    Plant Cell 15:303-315(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KRP1/ICK1.
  15. "Differential stability of Arabidopsis D-type cyclins: CYCD3;1 is a highly unstable protein degraded by a proteasome-dependent mechanism."
    Planchais S., Samland A.K., Murray J.A.H.
    Plant J. 38:616-625(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, PHOSPHORYLATION.
  16. "Genome-wide analysis of the cyclin family in Arabidopsis and comparative phylogenetic analysis of plant cyclin-like proteins."
    Wang G., Kong H., Sun Y., Zhang X., Zhang W., Altman N., dePamphilis C.W., Ma H.
    Plant Physiol. 135:1084-1099(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  17. "D-type cyclins activate division in the root apex to promote seed germination in Arabidopsis."
    Masubelele N.H., Dewitte W., Menges M., Maughan S., Collins C., Huntley R., Nieuwland J., Scofield S., Murray J.A.H.
    Proc. Natl. Acad. Sci. U.S.A. 102:15694-15699(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "The D-type cyclin CYCD3;1 is limiting for the G1-to-S-phase transition in Arabidopsis."
    Menges M., Samland A.K., Planchais S., Murray J.A.H.
    Plant Cell 18:893-906(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH CDKA-1, MUTAGENESIS OF SER-343.

Entry informationi

Entry nameiCCD31_ARATH
AccessioniPrimary (citable) accession number: P42753
Secondary accession number(s): O49489, Q56XG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 15, 2005
Last modified: May 11, 2016
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants overexpressing CYCD3-1 show extensive leaf curling, disorganized meristems, increased leaf number, late flowering and delayed senescence. CYCD3-1 is a highly unstable protein whose proteolysis is mediated by a proteasome-dependent pathway, and whose levels are highly dependent on the rate of protein synthesis.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.