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 02-SEP-2026, entry version 180. 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 GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; OZ408683; CAO7026736.1; -; 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; 25. DR FunCoup; P92948; 4646. DR IntAct; P92948; 7. DR STRING; 3702.P92948; -. DR GlyGen; P92948; 1 site. DR iPTMnet; P92948; -. DR PaxDb; 3702-P92948; -. DR ProteomicsDB; 222807; -. DR GeneID; 837506; -. DR KEGG; ath:AT1G09770; -. DR Araport; AT1G09770; -. DR TAIR; AT1G09770; CDC5. DR eggNOG; KOG0050; Eukaryota. DR HOGENOM; CLU_009082_1_0_1; -. DR InParanoid; P92948; -. DR OMA; CVAMGNE; -. DR PhylomeDB; P92948; -. DR CD-CODE; 4299E36E; Nucleolus. DR PRO; PR:P92948; -. DR Proteomes; UP000006548; Chromosome 1. DR GO; GO:0005576; C:extracellular region; HDA:TAIR. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central. DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR. 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:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:TAIR. DR CDD; cd00167; SANT; 1. DR CDD; cd11659; SANT_CDC5_II; 1. DR FunFam; 1.10.10.60:FF:000021; CDC5 cell division cycle 5-like; 1. DR FunFam; 1.10.10.60:FF:000091; CDC5 cell division cycle 5-like; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 2. DR InterPro; IPR047242; CDC5L/Cef1. DR InterPro; IPR021786; Cdc5p/Cef1_C. DR InterPro; IPR009057; Homeodomain-like_sf. DR InterPro; IPR017930; Myb_dom. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR047240; SANT_CDC5L_II. DR PANTHER; PTHR45885; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1. DR PANTHER; PTHR45885:SF1; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1. DR Pfam; PF11831; Myb_Cef; 1. DR Pfam; PF13921; Myb_DNA-bind_6; 1. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF46689; Homeodomain-like; 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 113..126 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 406..416 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 433..442 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 446..475 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 500..513 FT /note="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. 7; 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 //