CDC5L_ARATH
ID CDC5L_ARATH Reviewed; 844 AA.
AC P92948; B9DFT0; O04498; Q6R0C5;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cell division cycle 5-like protein;
DE Short=Cdc5-like protein;
DE AltName: Full=Atypical R2R3-MYB transcription factor CDC5;
DE AltName: Full=MOS4-associated complex protein 1;
DE Short=MAC protein 1;
DE AltName: Full=Protein MYB DOMAIN CELL DIVISION CYCLE 5;
DE Short=AtMYBCD5;
GN Name=CDC5; Synonyms=MAC1, MYBCD5; OrderedLocusNames=At1g09770;
GN ORFNames=F21M12.15;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8917598; DOI=10.1073/pnas.93.23.13371;
RA Hirayama T., Shinozaki K.;
RT "A cdc5+ homolog of a higher plant, Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13371-13376(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [3]
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 [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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-504.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP GENE FAMILY.
RX PubMed=11597504; DOI=10.1016/s1369-5266(00)00199-0;
RA Stracke R., Werber M., Weisshaar B.;
RT "The R2R3-MYB gene family in Arabidopsis thaliana.";
RL Curr. Opin. Plant Biol. 4:447-456(2001).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, COMPONENT OF THE MAC COMPLEX, AND
RP INTERACTION WITH PRL1 AND MOS4.
RX PubMed=17575050; DOI=10.1101/gad.1559607;
RA Palma K., Zhao Q., Cheng Y.T., Bi D., Monaghan J., Cheng W., Zhang Y.,
RA Li X.;
RT "Regulation of plant innate immunity by three proteins in a complex
RT conserved across the plant and animal kingdoms.";
RL Genes Dev. 21:1484-1493(2007).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17298883; DOI=10.1016/j.plaphy.2006.12.003;
RA Lin Z., Yin K., Wang X., Liu M., Chen Z., Gu H., Qu L.J.;
RT "Virus induced gene silencing of AtCDC5 results in accelerated cell death
RT in Arabidopsis leaves.";
RL Plant Physiol. Biochem. 45:87-94(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE MAC COMPLEX, AND
RP INTERACTION WITH PRP19A.
RX PubMed=19629177; DOI=10.1371/journal.ppat.1000526;
RA Monaghan J., Xu F., Gao M., Zhao Q., Palma K., Long C., Chen S., Zhang Y.,
RA Li X.;
RT "Two Prp19-like U-box proteins in the MOS4-associated complex play
RT redundant roles in plant innate immunity.";
RL PLoS Pathog. 5:E1000526-E1000526(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Component of the MAC complex that probably regulates defense
CC responses through transcriptional control and thereby is essential for
CC plant innate immunity. Possesses a sequence specific DNA sequence
CC 'CTCAGCG' binding activity. Involved in mRNA splicing and cell cycle
CC control. May also play a role in the response to DNA damage.
CC {ECO:0000250|UniProtKB:Q99459, ECO:0000269|PubMed:17298883,
CC ECO:0000269|PubMed:17575050, ECO:0000269|PubMed:8917598}.
CC -!- SUBUNIT: Component of the multiprotein assembly MOS4-associated complex
CC (MAC) at least composed of MOS4, CDC5, PRL1 and PRP19. Interacts with
CC PRL1, MOS4 and PRP19A. Associated with the spliceosome.
CC {ECO:0000269|PubMed:17575050, ECO:0000269|PubMed:19629177}.
CC -!- INTERACTION:
CC P92948; Q949S9: MOS4; NbExp=3; IntAct=EBI-1382948, EBI-1382943;
CC P92948; Q42384: PRL1; NbExp=2; IntAct=EBI-1382948, EBI-1382964;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:17298883}.
CC -!- TISSUE SPECIFICITY: Expressed extensively in shoot and root meristems.
CC {ECO:0000269|PubMed:8917598}.
CC -!- DISRUPTION PHENOTYPE: Accelerated cell death. Enhanced susceptibility
CC to virulent and avirulent pathogens. {ECO:0000269|PubMed:17298883,
CC ECO:0000269|PubMed:17575050}.
CC -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
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DR EMBL; D58424; BAA09598.1; -; mRNA.
DR EMBL; AY519553; AAS10023.1; -; mRNA.
DR EMBL; AC000132; AAB60730.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28490.1; -; Genomic_DNA.
DR EMBL; AY093057; AAM13056.1; -; mRNA.
DR EMBL; BT008801; AAP68240.1; -; mRNA.
DR EMBL; AK316890; BAH19597.1; -; mRNA.
DR PIR; F86231; F86231.
DR RefSeq; NP_172448.1; NM_100849.3.
DR AlphaFoldDB; P92948; -.
DR SMR; P92948; -.
DR BioGRID; 22747; 23.
DR IntAct; P92948; 7.
DR STRING; 3702.AT1G09770.1; -.
DR iPTMnet; P92948; -.
DR PaxDb; P92948; -.
DR PRIDE; P92948; -.
DR ProteomicsDB; 222807; -.
DR EnsemblPlants; AT1G09770.1; AT1G09770.1; AT1G09770.
DR GeneID; 837506; -.
DR Gramene; AT1G09770.1; AT1G09770.1; AT1G09770.
DR KEGG; ath:AT1G09770; -.
DR Araport; AT1G09770; -.
DR TAIR; locus:2024336; AT1G09770.
DR eggNOG; KOG0050; Eukaryota.
DR HOGENOM; CLU_009082_1_0_1; -.
DR InParanoid; P92948; -.
DR OMA; PFRTQRE; -.
DR OrthoDB; 975557at2759; -.
DR PhylomeDB; P92948; -.
DR PRO; PR:P92948; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92948; baseline and differential.
DR Genevisible; P92948; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR021786; Cdc5p/Cef1_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF11831; Myb_Cef; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Coiled coil; DNA damage; DNA repair; DNA-binding;
KW Immunity; Innate immunity; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Plant defense; Reference proteome; Repeat; Spliceosome;
KW Transcription; Transcription regulation.
FT CHAIN 1..844
FT /note="Cell division cycle 5-like protein"
FT /id="PRO_0000391630"
FT DOMAIN 2..57
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 58..107
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 30..53
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 81..103
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 113..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 145..189
FT /evidence="ECO:0000255"
FT COILED 685..723
FT /evidence="ECO:0000255"
FT COMPBIAS 400..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 177
FT /note="E -> K (in Ref. 2; AAS10023)"
FT /evidence="ECO:0000305"
FT CONFLICT 460..461
FT /note="HE -> QQ (in Ref. 1; BAA09598)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="S -> G (in Ref. 6; BAH19597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 844 AA; 95767 MW; B640967BB8AB4614 CRC64;
MRIMIKGGVW KNTEDEILKA AVMKYGKNQW ARISSLLVRK SAKQCKARWY EWLDPSIKKT
EWTREEDEKL LHLAKLLPTQ WRTIAPIVGR TPSQCLERYE KLLDAACTKD ENYDAADDPR
KLRPGEIDPN PEAKPARPDP VDMDEDEKEM LSEARARLAN TRGKKAKRKA REKQLEEARR
LASLQKRREL KAAGIDGRHR KRKRKGIDYN AEIPFEKRAP AGFYDTADED RPADQVKFPT
TIEELEGKRR ADVEAHLRKQ DVARNKIAQR QDAPAAILQA NKLNDPEVVR KRSKLMLPPP
QISDHELEEI AKMGYASDLL AENEELTEGS AATRALLANY SQTPRQGMTP MRTPQRTPAG
KGDAIMMEAE NLARLRDSQT PLLGGENPEL HPSDFTGVTP RKKEIQTPNP MLTPSMTPGG
AGLTPRIGLT PSRDGSSFSM TPKGTPFRDE LHINEDMDMH ESAKLERQRR EEARRSLRSG
LTGLPQPKNE YQIVAQPPPE ESEEPEEKIE EDMSDRIARE KAEEEARQQA LLKKRSKVLQ
RDLPRPPAAS LAVIRNSLLS ADGDKSSVVP PTPIEVADKM VREELLQLLE HDNAKYPLDD
KAEKKKGAKN RTNRSASQVL AIDDFDENEL QEADKMIKEE GKFLCVSMGH ENKTLDDFVE
AHNTCVNDLM YFPTRSAYEL SSVAGNADKV AAFQEEMENV RKKMEEDEKK AEHMKAKYKT
YTKGHERRAE TVWTQIEATL KQAEIGGTEV ECFKALKRQE EMAASFRKKN LQEEVIKQKE
TESKLQTRYG NMLAMVEKAE EIMVGFRAQA LKKQEDVEDS HKLKEAKLAT GEEEDIAIAM
EASA
