CDT1A_ARATH
ID CDT1A_ARATH Reviewed; 571 AA.
AC Q9SJW9; Q710F0; Q8L7I6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=CDT1-like protein a, chloroplastic;
DE Short=AtCDT1a;
DE Flags: Precursor;
GN Name=CDT1A; OrderedLocusNames=At2g31270; ORFNames=F16D14.11;
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], FUNCTION, INTERACTION WITH CDC6 AND CDKA-1,
RP TISSUE SPECIFICITY, INDUCTION BY ABSCISIC ACID, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=15316110; DOI=10.1105/tpc.104.022400;
RA del Mar Castellano M., Boniotti M.B., Caro E., Schnittger A., Gutierrez C.;
RT "DNA replication licensing affects cell proliferation or endoreplication in
RT a cell type-specific manner.";
RL Plant Cell 16:2380-2393(2004).
RN [2]
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 [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;
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [5]
RP FUNCTION, INTERACTION WITH ARC6, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15928083; DOI=10.1073/pnas.0502564102;
RA Raynaud C., Perennes C., Reuzeau C., Catrice O., Brown S., Bergounioux C.;
RT "Cell and plastid division are coordinated through the prereplication
RT factor AtCDT1.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8216-8221(2005).
RN [6]
RP INDUCTION BY ABAP1.
RX PubMed=18818695; DOI=10.1038/emboj.2008.191;
RA Masuda H.P., Cabral L.M., De Veylder L., Tanurdzic M.,
RA de Almeida Engler J., Geelen D., Inze D., Martienssen R.A., Ferreira P.C.,
RA Hemerly A.S.;
RT "ABAP1 is a novel plant Armadillo BTB protein involved in DNA replication
RT and transcription.";
RL EMBO J. 27:2746-2756(2008).
CC -!- FUNCTION: Member of the pre-replication complex. Component of the
CC plastid division machinery. Promotes polyloidization and regulates
CC endoreduplication. Involved in the coordination of cell and plastid
CC division. {ECO:0000269|PubMed:15316110, ECO:0000269|PubMed:15928083}.
CC -!- SUBUNIT: Binds to ARC6.
CC -!- INTERACTION:
CC Q9SJW9; B7U179: ABAP1; NbExp=3; IntAct=EBI-8079732, EBI-541722;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15928083}.
CC -!- TISSUE SPECIFICITY: Expressed in proliferating (e.g. shoot and root
CC apical meristems, organ primordia) and endoreplicating cells (e.g.
CC guard cells and stomatal lineage, developing trichomes).
CC {ECO:0000269|PubMed:15316110}.
CC -!- INDUCTION: Repressed by abscisic acid (ABA) and ABAP1. Degraded by the
CC proteasome. {ECO:0000269|PubMed:15316110, ECO:0000269|PubMed:18818695}.
CC -!- PTM: Phosphorylated by cyclin D- and cyclin A-containing CDKA-1, and
CC thus targeted to proteasome-mediated proteolysis.
CC {ECO:0000269|PubMed:15316110}.
CC -!- SIMILARITY: Belongs to the Cdt1 family. {ECO:0000305}.
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DR EMBL; AJ421408; CAD13172.2; -; mRNA.
DR EMBL; AC006593; AAD20672.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08516.1; -; Genomic_DNA.
DR EMBL; AY131998; AAM96888.1; -; mRNA.
DR PIR; F84718; F84718.
DR RefSeq; NP_180685.1; NM_128683.4.
DR AlphaFoldDB; Q9SJW9; -.
DR SMR; Q9SJW9; -.
DR BioGRID; 3032; 3.
DR IntAct; Q9SJW9; 1.
DR MINT; Q9SJW9; -.
DR STRING; 3702.AT2G31270.1; -.
DR iPTMnet; Q9SJW9; -.
DR MetOSite; Q9SJW9; -.
DR PaxDb; Q9SJW9; -.
DR PRIDE; Q9SJW9; -.
DR ProteomicsDB; 224470; -.
DR EnsemblPlants; AT2G31270.1; AT2G31270.1; AT2G31270.
DR GeneID; 817684; -.
DR Gramene; AT2G31270.1; AT2G31270.1; AT2G31270.
DR KEGG; ath:AT2G31270; -.
DR Araport; AT2G31270; -.
DR TAIR; locus:2042541; AT2G31270.
DR eggNOG; KOG4762; Eukaryota.
DR HOGENOM; CLU_019037_1_0_1; -.
DR InParanoid; Q9SJW9; -.
DR OMA; IMPESIV; -.
DR OrthoDB; 648388at2759; -.
DR PhylomeDB; Q9SJW9; -.
DR PRO; PR:Q9SJW9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJW9; baseline and differential.
DR Genevisible; Q9SJW9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0051276; P:chromosome organization; IMP:TAIR.
DR GO; GO:0006260; P:DNA replication; IMP:TAIR.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0071163; P:DNA replication preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0048229; P:gametophyte development; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IBA:GO_Central.
DR CDD; cd08767; Cdt1_c; 1.
DR CDD; cd08674; Cdt1_m; 1.
DR Gene3D; 1.10.10.1420; -; 1.
DR InterPro; IPR045173; Cdt1.
DR InterPro; IPR032054; Cdt1_C.
DR InterPro; IPR038090; Cdt1_C_WH_dom_sf.
DR InterPro; IPR014939; CDT1_Gemini-bd-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR28637; PTHR28637; 1.
DR Pfam; PF08839; CDT1; 1.
DR Pfam; PF16679; CDT1_C; 1.
DR SMART; SM01075; CDT1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chloroplast; DNA replication; Phosphoprotein; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..571
FT /note="CDT1-like protein a, chloroplastic"
FT /id="PRO_0000406938"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 114
FT /note="K -> R (in Ref. 1; CAD13172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 63740 MW; 33455EBE4874E517 CRC64;
MSTPGSSRSI PFKSKKRLVM DSPSSKSQTG NPNPSSVALP TPEKPLENML SRSRNRSVAL
SVKEIRQAAG SRRRSEDPVA SSAKSRLFFD SSSSSPSKRK SSNKNAEKEK LPEKYENLGK
FFEALDNSML LSKLRGSKPT FSNISKQIEH LTERRFCYSH LAQIKHILPE AIEIKRVLIH
DETTCCMKPD LHVTLNADAV EYNDKSKSES KKIALRKVFR ARLADFVKAH PQGDEVPEEP
LPEPFNRRKP VENSNVEVKR VSSLMEEMAS IPASKLFSSP ITSTPVKTTS SLAKPTSSQI
NIAPTPTKPT STPAKQTLSE INILPTPVKP VSTLAKFPST PAIIDSTPVI TATPPEFAST
PARLMSTSLA ARPLKRSNGH TNPDDISADP PTKLVRRSLS LNFDSYPEDE RTMDFTDDIP
IDQVPEEDVS SDDEILSILP DKLRHAIKEQ ERKAIEDQNP AISLAKRRRK MIACLPKLFN
VIHYLIQSIR RWVITKEELV HKIIAGHSDI TDRKEVEEQL ILLQEIVPEW MSEKKSSSGD
VLVCINKLAS PLTIRSRLEE ENKQEMAPLL S
