DCAF1_ARATH
ID DCAF1_ARATH Reviewed; 1883 AA.
AC Q9M086; Q8GX50;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=DDB1- and CUL4-associated factor homolog 1;
DE AltName: Full=Protein DDB1-CUL4 ASSOCIATED FACTOR 1;
DE Short=Protein DCAF1;
GN Name=DCAF1; OrderedLocusNames=At4g31160; ORFNames=F6E21_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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1521-1883.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF
RP CUL4-RBX1-DDB1-DCAF1 COMPLEX, INTERACTION WITH DDB1A, AND MUTAGENESIS OF
RP ASP-1622; ARG-1624; ASP-1658 AND ARG-1660.
RX PubMed=18552200; DOI=10.1105/tpc.108.058891;
RA Zhang Y., Feng S., Chen F., Chen H., Wang J., McCall C., Xiong Y.,
RA Deng X.W.;
RT "Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 forms a nuclear E3 ubiquitin
RT ligase with DDB1 and CUL4 that is involved in multiple plant developmental
RT processes.";
RL Plant Cell 20:1437-1455(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Component of the CUL4-RBX1-DDB1-DCAF1 E3 ubiquitin-protein
CC ligase complex, DCAF1 may function as the substrate recognition module
CC within this complex. Appears to be required for plant embryogenesis and
CC to affect several other developmental processes including leaf, shoot,
CC and flower development. {ECO:0000269|PubMed:18552200}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the CUL4-RBX1-DDB1-DCAF1 E3 ubiquitin-protein
CC ligase complex. Interacts with DDB1A through its DWD motifs.
CC {ECO:0000269|PubMed:18552200}.
CC -!- INTERACTION:
CC Q9M086; Q8LGH4: CUL4; NbExp=2; IntAct=EBI-2429941, EBI-541750;
CC Q9M086; Q9M0V3: DDB1A; NbExp=6; IntAct=EBI-2429941, EBI-1632780;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18552200}.
CC -!- TISSUE SPECIFICITY: Ubiquitous but predominantly expressed in the
CC inflorescence and roots.
CC -!- DOMAIN: The DWD boxes are required for interaction with DDB1A.
CC -!- DISRUPTION PHENOTYPE: Embryonic development is arrested at the globular
CC stage. {ECO:0000269|PubMed:18552200}.
CC -!- SIMILARITY: Belongs to the VPRBP/DCAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB79834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161578; CAB79834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85867.1; -; Genomic_DNA.
DR EMBL; AK118434; BAC43043.1; ALT_INIT; mRNA.
DR PIR; T10670; T10670.
DR RefSeq; NP_194845.4; NM_119266.7.
DR AlphaFoldDB; Q9M086; -.
DR SMR; Q9M086; -.
DR BioGRID; 14531; 6.
DR IntAct; Q9M086; 2.
DR STRING; 3702.AT4G31160.1; -.
DR iPTMnet; Q9M086; -.
DR PaxDb; Q9M086; -.
DR PRIDE; Q9M086; -.
DR ProteomicsDB; 222758; -.
DR EnsemblPlants; AT4G31160.1; AT4G31160.1; AT4G31160.
DR GeneID; 829244; -.
DR Gramene; AT4G31160.1; AT4G31160.1; AT4G31160.
DR KEGG; ath:AT4G31160; -.
DR Araport; AT4G31160; -.
DR TAIR; locus:2126296; AT4G31160.
DR eggNOG; KOG1832; Eukaryota.
DR HOGENOM; CLU_237244_0_0_1; -.
DR InParanoid; Q9M086; -.
DR OMA; ECSQDQA; -.
DR OrthoDB; 105679at2759; -.
DR PhylomeDB; Q9M086; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M086; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M086; baseline and differential.
DR Genevisible; Q9M086; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0048827; P:phyllome development; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR033270; VPRBP/DCAF1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13129; PTHR13129; 3.
DR Pfam; PF08513; LisH; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..1883
FT /note="DDB1- and CUL4-associated factor homolog 1"
FT /id="PRO_0000391641"
FT DOMAIN 1087..1119
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 1464..1503
FT /note="WD 1"
FT REPEAT 1506..1546
FT /note="WD 2"
FT REPEAT 1548..1586
FT /note="WD 3"
FT REPEAT 1587..1626
FT /note="WD 4"
FT REPEAT 1633..1671
FT /note="WD 5"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1619..1626
FT /note="DWD box 1"
FT MOTIF 1655..1662
FT /note="DWD box 2"
FT COMPBIAS 310..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1798
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1869
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MUTAGEN 1622
FT /note="D->A: Abolishes the DDB1A interaction; when
FT associated with A-1624."
FT /evidence="ECO:0000269|PubMed:18552200"
FT MUTAGEN 1624
FT /note="R->A: Abolishes the DDB1A interaction. when
FT associated with A-1622."
FT /evidence="ECO:0000269|PubMed:18552200"
FT MUTAGEN 1658
FT /note="D->A: Abolishes the DDB1A interaction. when
FT associated with A-1660. when associated with ALA-1624."
FT /evidence="ECO:0000269|PubMed:18552200"
FT MUTAGEN 1660
FT /note="R->A: Abolishes the DDB1A interaction. when
FT associated with A-1658."
FT /evidence="ECO:0000269|PubMed:18552200"
SQ SEQUENCE 1883 AA; 205451 MW; 822ECA9FB6BA3CE1 CRC64;
MDGQEHAEVP NSMVEDDQSV VAAEAIAELA NSTGEPNPEE GEEQSVEDEL IAKAQKLMED
ITSVANNPNP NILHALSQLL ESQESLFLEE NGHFSNARGS HNSGKLCILI RENDEFFELI
SSTFLSENSY STAVKAASAR LLMNCSLTWM YPHVFDDAVT ENFKNWVMEE AVKFPGEDSA
KKEASDFEML KTYSTGLLAL SLASRGQIVE DVLTSGLSAK LMHYLRVRVL KEPSTSRIHT
TETKHVSLKT KEEGRSRVRK IVDTVEGDHV LETDSGREMG QTDVQPDGEF EIDGRDVFNV
SGVVDCKIKP GDDNSVRDDP SRHRLNRSKS RGRGRVHEGA PDTEVLLASP RLGRLLVRDR
DLSKISDGRN AEDVTVCLGK MKSGIMEIER EDNDECFQGC IIGTKNITDL VKRAVGAAET
EARAAHAPDD AAKAAGDAAA ELVKTAALEE FKSSGSEEAA VSAATRAAIT VIDAAEVSRN
PTCVTSDQTT DVSEVSLPDI ESLAQLQEKY CIQCLEILGE YVEVLGPVLH EKGVDVCIVL
LERTSQLDDR STVSPLLPDV MKLICALAAH RKFAAMFVER RGILKLLAVP RVSETFYGLS
SCLYTIGSLQ GIMERVCALP LVVIHQVVKL AIELLDCSQD QARKNSALFF AAAFVFRAIL
DAFDAQDSLQ KLLAILKDAA SVRTGANTDR SAPEVMTSSE KQMAFHTCFA LRQYFRAHLL
LLVDSIRPSR ISRGGVPSSM KPNIRAAYKP LDISNEAVDA IFLQLQKDRR LGPTFVKAQW
PAVNNFLASS GHVTMLELCQ TPPVDRYLHD LLQYAFGVLH IVTSIPDGRK AIAHATLSNN
RAGIAVILDA ANISNSIVDP EIIQPALNVL INLVCPPPSL SNKPPLAQNH QPVPGQATTR
PSTDVAVGTQ STGNAPQTPV APASSGLVGD RRIFLGAGTG SAGLAAKLEQ VYRQAREAVR
GNDGIKILLK LLQPRIYVNP PATPDCLRAL ACRVLLGLAR DDTIAQILTK LEVGKSLSEL
IRDSGGQSSG TDQGRWQAEL AQVALELIGI VTNSGHATTL TASDAATPTL RRIERAAIAA
ATPITYDSKE LLLLIHEHLQ ASGLGDTASA LLKEAQLTPL PSSASPSSIA YSTTQEMSTP
LAQEQWPSGR ANSGFFTSKP KVCAHDEDPN SRSNAALSAK KKHLASSTLE MPTPVAQQQW
PSGRANCGFC PSIPKINARD EDPSSRGNAA PSAKKKQLTF SPSFSSQSRK QSFSHDALPQ
STQRINCCSN SDPALADTSE TAAELVLKND LDADAQFKTP ISFPRKRKLS ELRDSSVPGK
RIDLGERRNS TFADGSGLQT PASALDANQS GSSRLGQMTP ASQLRLPSDP QPSNPERLSL
DSLVVQYLKH QHRQCLAPIT TLPPVSLLHP HVCPEPKRLL EAPLNMTGRL GTRELQSFYS
GVHGNRRDRQ FVFSRFKSWR SFRDETALFT CIALLGGTNH IAVGSHAGEI KIFEASSGSM
LESVSGHQAP VTLVQPYVSR DTQLLLSSSS SDVQLWDASS ITGGPRHSFD GCKAAKFSNS
GLQFAALSCE ASRKDVLLYD VQTCSPCQKL TDTVTSSRSN PYSLVHFSPC DTLILWNGVL
WDRRIPEKVR RFDQFTDYGG GGFHPSRNEV IINSEIWDMR TFKLLRSVPS LDQTAITFNS
RGDVIYAMLR RNIEDVMSAV HTRRVKHPLF AAFRTLDAIN YSDIATIPVD RCLLDFATEP
TDSFLGLITM EDQEDMFSSA RMYEIGRRRP TDDDSDPDDD DETEDEDEDD EEEDDLDRIL
GLAGDNSDSG DDDLSSEDNE DSVSDFDEEA DILIDGDFME ELIEGENEDD GNGEDEDDDD
DGEMQDFMSS GEEDDYRDNI RSS
