CUL4_ARATH
ID CUL4_ARATH Reviewed; 792 AA.
AC Q8LGH4; Q84LL5; Q8RWT9; Q9FGP0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Cullin-4;
DE Short=AtCUL4;
GN Name=CUL4; OrderedLocusNames=At5g46210; ORFNames=MDE13.3;
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].
RA Shen W.H.;
RT "Arabidopsis thaliana mRNA for cullin 4.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, COMPONENT OF CUL4-RBX1-COP10-DDB1A-DET1 COMPLEX, INTERACTION WITH
RP CSN3; CSN4; CSN5; CSN8; CAND1; COP10; DDB1A AND RBX1, SUBCELLULAR LOCATION,
RP NEDDYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16844902; DOI=10.1105/tpc.106.043224;
RA Chen H., Shen Y., Tang X., Yu L., Wang J., Guo L., Zhang Y., Zhang H.,
RA Feng S., Strickland E., Zheng N., Deng X.-W.;
RT "Arabidopsis CULLIN4 forms an E3 ubiquitin ligase with RBX1 and the CDD
RT complex in mediating light control of development.";
RL Plant Cell 18:1991-2004(2006).
RN [7]
RP FUNCTION, INTERACTION WITH DDB1A; DDB1B; DET1 AND RBX1, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16792691; DOI=10.1111/j.1365-313x.2006.02810.x;
RA Bernhardt A., Lechner E., Hano P., Schade V., Dieterle M., Anders M.,
RA Dubin M.J., Benvenuto G., Bowler C., Genschik P., Hellmann H.;
RT "CUL4 associates with DDB1 and DET1 and its downregulation affects diverse
RT aspects of development in Arabidopsis thaliana.";
RL Plant J. 47:591-603(2006).
RN [8]
RP FUNCTION, COMPONENT OF THE CUL4-RBX1-DDB1-PRL1 COMPLEX, INTERACTION WITH
RP DDB1A, AND DISRUPTION PHENOTYPE.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [9]
RP FUNCTION.
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 [10]
RP FUNCTION, COMPONENT OF CUL4-DDB1-COP1-SPA1 COMPLEX, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20061554; DOI=10.1105/tpc.109.065490;
RA Chen H., Huang X., Gusmaroli G., Terzaghi W., Lau O.S., Yanagawa Y.,
RA Zhang Y., Li J., Lee J.H., Zhu D., Deng X.W.;
RT "Arabidopsis CULLIN4-damaged DNA binding protein 1 interacts with
RT CONSTITUTIVELY PHOTOMORPHOGENIC1-SUPPRESSOR OF PHYA complexes to regulate
RT photomorphogenesis and flowering time.";
RL Plant Cell 22:108-123(2010).
RN [11]
RP FUNCTION, AND COMPONENT OF THE CUL4-RBX1-DDB1-DWA1/DWA2 COMPLEX.
RX PubMed=20525848; DOI=10.1105/tpc.109.073783;
RA Lee J.H., Yoon H.J., Terzaghi W., Martinez C., Dai M., Li J., Byun M.O.,
RA Deng X.W.;
RT "DWA1 and DWA2, two Arabidopsis DWD protein components of CUL4-based E3
RT ligases, act together as negative regulators in aba signal transduction.";
RL Plant Cell 22:1716-1732(2010).
CC -!- FUNCTION: Component of the CUL4-RBX1-CDD (COP10-DDB1a-DET1) E3
CC ubiquitin-protein ligase complex which mediates the ubiquitination and
CC subsequent proteasomal degradation of target proteins. Participates in
CC the CDD complex to light-mediated control of development. May repress
CC photomorphogenesis through enhancing COP1 E3 ubiquitin-protein ligase
CC activity. Acts together with the CUL4-DDB1-COP1-SPA E3 ubiquitin-
CC protein ligase complexes in the repression of photomorphogenesis and
CC flowering time. Component ot the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-
CC protein ligase complex which mediates ubiquitination and subsequent
CC degradation of AKIN10. Component of the CUL4-RBX1-DDB1-DWA1/DWA2 E3
CC ubiquitin-protein ligase complex that acts as negative regulator in
CC abscisic acid (ABA) signaling and may target ABI5 for degradation.
CC {ECO:0000269|PubMed:16792691, ECO:0000269|PubMed:16844902,
CC ECO:0000269|PubMed:18223036, ECO:0000269|PubMed:18552200,
CC ECO:0000269|PubMed:20061554, ECO:0000269|PubMed:20525848}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with COP10, CSN3, CSN4, CSN5, CSN8, DDB1A, DDB1B,
CC DDB2, DET1 and RBX1. {ECO:0000269|PubMed:16792691,
CC ECO:0000269|PubMed:16844902, ECO:0000269|PubMed:18223036}.
CC -!- INTERACTION:
CC Q8LGH4; Q8L5Y6: CAND1; NbExp=2; IntAct=EBI-541750, EBI-602912;
CC Q8LGH4; Q9LJD7: COP10; NbExp=4; IntAct=EBI-541750, EBI-2429853;
CC Q8LGH4; Q8W575: CSN3; NbExp=2; IntAct=EBI-541750, EBI-531055;
CC Q8LGH4; Q8L5U0: CSN4; NbExp=2; IntAct=EBI-541750, EBI-531074;
CC Q8LGH4; Q9M086: DCAF1; NbExp=2; IntAct=EBI-541750, EBI-2429941;
CC Q8LGH4; Q9M0V3: DDB1A; NbExp=11; IntAct=EBI-541750, EBI-1632780;
CC Q8LGH4; Q940X7: RBX1A; NbExp=3; IntAct=EBI-541750, EBI-532404;
CC Q8LGH4; Q9ZNU6: DET1; Xeno; NbExp=2; IntAct=EBI-541750, EBI-2029363;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16844902}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16792691}.
CC -!- PTM: Neddylated (rubylated). Deneddylated via its interaction with the
CC COP9 signalosome (CSN) complex. {ECO:0000269|PubMed:16844902}.
CC -!- DISRUPTION PHENOTYPE: Small plants with mishaped cotyledons and leaves.
CC Reduction of the number and the size of lateral roots. Increased
CC sensitivity to sugar, cytokinin and abscisic acid (ABA). Early
CC flowering under short day (SD) conditions.
CC {ECO:0000269|PubMed:16792691, ECO:0000269|PubMed:16844902,
CC ECO:0000269|PubMed:18223036, ECO:0000269|PubMed:20061554}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08502.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC85265.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ318018; CAC85265.1; ALT_INIT; mRNA.
DR EMBL; AB025620; BAB08502.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95353.1; -; Genomic_DNA.
DR EMBL; AY091113; AAM14063.1; -; mRNA.
DR EMBL; AY084267; AAM60859.1; -; mRNA.
DR RefSeq; NP_568658.1; NM_123990.3.
DR AlphaFoldDB; Q8LGH4; -.
DR SMR; Q8LGH4; -.
DR BioGRID; 19912; 19.
DR DIP; DIP-40462N; -.
DR IntAct; Q8LGH4; 16.
DR MINT; Q8LGH4; -.
DR STRING; 3702.AT5G46210.1; -.
DR iPTMnet; Q8LGH4; -.
DR PaxDb; Q8LGH4; -.
DR PRIDE; Q8LGH4; -.
DR ProteomicsDB; 220321; -.
DR EnsemblPlants; AT5G46210.1; AT5G46210.1; AT5G46210.
DR GeneID; 834663; -.
DR Gramene; AT5G46210.1; AT5G46210.1; AT5G46210.
DR KEGG; ath:AT5G46210; -.
DR Araport; AT5G46210; -.
DR TAIR; locus:2162060; AT5G46210.
DR eggNOG; KOG2167; Eukaryota.
DR HOGENOM; CLU_004747_7_2_1; -.
DR InParanoid; Q8LGH4; -.
DR OMA; WPTYPVM; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q8LGH4; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LGH4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LGH4; baseline and differential.
DR Genevisible; Q8LGH4; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000151; C:ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048825; P:cotyledon development; IMP:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR GO; GO:0048575; P:short-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..792
FT /note="Cullin-4"
FT /id="PRO_0000396851"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT CONFLICT 29
FT /note="A -> T (in Ref. 4; AAM14063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 91471 MW; 6C1E21BFCB9141DF CRC64;
MSLPTKRSTF SAASASDDSS YSSPPMKKAK NDLHHSPQHP NTADKVVGFH MEEDPTPAAA
NLSRKKATLP QPTKKFVIKL NKAKPTLPTN FEENTWEKLQ SAIRAIFLKK KISFDLESLY
QAVDNLCLHK LDGKLYDQIE KECEEHISAA LQSLVGQNTD LTVFLSRVEK CWQDFCDQML
MIRSIALTLD RKYVIQNPNV RSLWEMGLQL FRKHLSLAPE VEQRTVKGLL SMIEKERLAE
AVNRTLLSHL LKMFTALGIY MESFEKPFLE GTSEFYAAEG MKYMQQSDVP EYLKHVEGRL
HEENERCILY IDAVTRKPLI TTVERQLLER HILVVLEKGF TTLMDGRRTE DLQRMQTLFS
RVNALESLRQ ALSSYVRKTG QKIVMDEEKD KDMVQSLLDF KASLDIIWEE SFYKNESFGN
TIKDSFEHLI NLRQNRPAEL IAKFLDEKLR AGNKGTSEEE LESVLEKVLV LFRFIQGKDV
FEAFYKKDLA KRLLLGKSAS IDAEKSMISK LKTECGSQFT NKLEGMFKDI ELSKEINESF
KQSSQARTKL PSGIEMSVHV LTTGYWPTYP PMDVKLPHEL NVYQDIFKEF YLSKYSGRRL
MWQNSLGHCV LKADFSKGKK ELAVSLFQAV VLMLFNDAMK LSFEDIKDST SIEDKELRRT
LQSLACGKVR VLQKNPKGRD VEDGDEFEFN DEFAAPLYRI KVNAIQMKET VEENTSTTER
VFQDRQYQID AAIVRIMKTR KVLSHTLLIT ELFQQLKFPI KPADLKKRIE SLIDREYLER
EKSNPQIYNY LA
