COP1_ARATH
ID COP1_ARATH Reviewed; 675 AA.
AC P43254; O23974; O23975; O48770; Q1JPL6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=E3 ubiquitin-protein ligase COP1 {ECO:0000303|PubMed:1423630};
DE EC=2.3.2.27 {ECO:0000269|PubMed:14597662};
DE AltName: Full=Constitutive photomorphogenesis protein 1 {ECO:0000303|PubMed:1423630};
DE AltName: Full=RING-type E3 ubiquitin transferase COP1 {ECO:0000303|PubMed:1423630};
GN Name=COP1 {ECO:0000303|PubMed:1423630};
GN OrderedLocusNames=At2g32950 {ECO:0000312|Araport:AT2G32950};
GN ORFNames=T21L14.11 {ECO:0000312|EMBL:AAB91983.1};
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].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=1423630; DOI=10.1016/0092-8674(92)90555-q;
RA Deng X.-W., Matsui M., Wei N., Wagner D., Chu A.M., Feldmann K.A.,
RA Quail P.H.;
RT "COP1, an Arabidopsis regulatory gene, encodes a protein with both a zinc-
RT binding motif and a G beta homologous domain.";
RL Cell 71:791-801(1992).
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;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-387 AND 506-594.
RX PubMed=9744100; DOI=10.1046/j.1365-313x.1998.00184.x;
RA Simpson C.G., Mcquade C., Lyon J., Brown J.W.S.;
RT "Characterisation of exon skipping mutants of the COP1 gene from
RT Arabidopsis.";
RL Plant J. 15:125-131(1998).
RN [6]
RP CHARACTERIZATION, AND MUTANTS COP1-8 AND COP1-9.
RX PubMed=8205001; DOI=10.2307/3869929;
RA McNellis T.W., von Arnim A.G., Araki T., Komeda Y., Misera S., Deng X.-W.;
RT "Genetic and molecular analysis of an allelic series of cop1 mutants
RT suggests functional roles for the multiple protein domains.";
RL Plant Cell 6:487-500(1994).
RN [7]
RP INTERACTION WITH CIP1.
RC STRAIN=cv. Columbia;
RX PubMed=7753789; DOI=10.1073/pnas.92.10.4239;
RA Matsui M., Stoop C.D., von Arnim A.G., Wei N., Deng X.-W.;
RT "Arabidopsis COP1 protein specifically interacts in vitro with a
RT cytoskeleton-associated protein, CIP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4239-4243(1995).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=10480941; DOI=10.1074/jbc.274.38.27231;
RA Stacey M.G., von Arnim A.G.;
RT "A novel motif mediates the targeting of the Arabidopsis COP1 protein to
RT subnuclear foci.";
RL J. Biol. Chem. 274:27231-27236(1999).
RN [9]
RP INTERACTION.
RX PubMed=9755158; DOI=10.1093/emboj/17.19.5577;
RA Torii K.U., McNellis T.W., Deng X.-W.;
RT "Functional dissection of Arabidopsis COP1 reveals specific roles of its
RT three structural modules in light control of seedling development.";
RL EMBO J. 17:5577-5587(1998).
RN [10]
RP FUNCTION, AND INTERACTION WITH CIP7.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Etiolated seedling;
RX PubMed=9668129; DOI=10.2307/3870713;
RA Yamamoto Y.Y., Matsui M., Ang L.-H., Deng X.-W.;
RT "Role of a COP1 interactive protein in mediating light-regulated gene
RT expression in arabidopsis.";
RL Plant Cell 10:1083-1094(1998).
RN [11]
RP INTERACTION WITH CIP8.
RC TISSUE=Seedling;
RX PubMed=10488108; DOI=10.1074/jbc.274.39.27674;
RA Torii K.U., Stoop-Myer C.D., Okamoto H., Coleman J.E., Matsui M.,
RA Deng X.-W.;
RT "The RING finger motif of photomorphogenic repressor COP1 specifically
RT interacts with the RING-H2 motif of a novel Arabidopsis protein.";
RL J. Biol. Chem. 274:27674-27681(1999).
RN [12]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 294-ARG--LYS-296 AND
RP 312-LYS--ARG-314.
RX PubMed=10072396; DOI=10.2307/3870865;
RA Stacey M.G., Hicks S.N., von Arnim A.G.;
RT "Discrete domains mediate the light-responsive nuclear and cytoplasmic
RT localization of Arabidopsis COP1.";
RL Plant Cell 11:349-364(1999).
RN [13]
RP CHARACTERIZATION, AND INTERACTION WITH SPA1.
RX PubMed=11461903; DOI=10.1074/jbc.m103140200;
RA Hoecker U., Quail P.H.;
RT "The phytochrome A-specific signaling intermediate SPA1 interacts directly
RT with COP1, a constitutive repressor of light signaling in Arabidopsis.";
RL J. Biol. Chem. 276:38173-38178(2001).
RN [14]
RP INTERACTION WITH BBX24/STO AND BBX25/STH, MUTANTS COP1-4; COP1-8 AND
RP COP1-9, AND MUTAGENESIS OF LYS-422; ARG-465; TRP-467; LYS-550 AND GLU-592.
RC TISSUE=Etiolated seedling;
RX PubMed=11226162; DOI=10.1093/emboj/20.1.118;
RA Holm M., Hardtke C.S., Gaudet R., Deng X.-W.;
RT "Identification of a structural motif that confers specific interaction
RT with the WD40 repeat domain of Arabidopsis COP1.";
RL EMBO J. 20:118-127(2001).
RN [15]
RP UBIQUITINATION OF HY5.
RX PubMed=10839542; DOI=10.1038/35013076;
RA Osterlund M.T., Hardtke C.S., Wei N., Deng X.-W.;
RT "Targeted destabilization of HY5 during light-regulated development of
RT Arabidopsis.";
RL Nature 405:462-466(2000).
RN [16]
RP FUNCTION IN DEGRADATION OF HYH.
RX PubMed=12023303; DOI=10.1101/gad.969702;
RA Holm M., Ma L.-G., Qu L.-J., Deng X.-W.;
RT "Two interacting bZIP proteins are direct targets of COP1-mediated control
RT of light-dependent gene expression in Arabidopsis.";
RL Genes Dev. 16:1247-1259(2002).
RN [17]
RP FUNCTION.
RX PubMed=11967090; DOI=10.1046/j.1365-313x.2002.01264.x;
RA Shin B., Choi G., Yi H., Yang S., Cho I., Kim J., Lee S., Paek N.-C.,
RA Kim J.-H., Song P.S., Choi G.;
RT "AtMYB21, a gene encoding a flower-specific transcription factor, is
RT regulated by COP1.";
RL Plant J. 30:23-32(2002).
RN [18]
RP INTERACTION WITH SPA1, CATALYTIC ACTIVITY, AND UBIQUITINATION.
RX PubMed=14597662; DOI=10.1101/gad.1122903;
RA Saijo Y., Sullivan J.A., Wang H., Yang J., Shen Y., Rubio V., Ma L.,
RA Hoecker U., Deng X.W.;
RT "The COP1-SPA1 interaction defines a critical step in phytochrome A-
RT mediated regulation of HY5 activity.";
RL Genes Dev. 17:2642-2647(2003).
RN [19]
RP INTERACTION WITH SPA3 AND SPA4.
RX PubMed=12887588; DOI=10.1046/j.1365-313x.2003.01813.x;
RA Laubinger S., Hoecker U.;
RT "The SPA1-like proteins SPA3 and SPA4 repress photomorphogenesis in the
RT light.";
RL Plant J. 35:373-385(2003).
RN [20]
RP UBIQUITINATION, UBIQUITINATION OF LAF1, AND MUTAGENESIS OF CYS-52 AND
RP CYS-55.
RX PubMed=12827204; DOI=10.1038/nature01696;
RA Seo H.S., Yang J.-Y., Ishikawa M., Bolle C., Ballesteros M.L., Chua N.-H.;
RT "LAF1 ubiquitination by COP1 controls photomorphogenesis and is stimulated
RT by SPA1.";
RL Nature 423:995-999(2003).
RN [21]
RP INTERACTION WITH SPA2.
RX PubMed=15308756; DOI=10.1105/tpc.104.024216;
RA Laubinger S., Fittinghoff K., Hoecker U.;
RT "The SPA quartet: a family of WD-repeat proteins with a central role in
RT suppression of photomorphogenesis in Arabidopsis.";
RL Plant Cell 16:2293-2306(2004).
RN [22]
RP INTERACTION WITH COP10.
RX PubMed=15342494; DOI=10.1101/gad.1229504;
RA Yanagawa Y., Sullivan J.A., Komatsu S., Gusmaroli G., Suzuki G., Yin J.,
RA Ishibashi T., Saijo Y., Rubio V., Kimura S., Wang J., Deng X.-W.;
RT "Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances
RT the activity of ubiquitin conjugating enzymes.";
RL Genes Dev. 18:2172-2181(2004).
RN [23]
RP INTERACTION WITH SPA1 AND PHYA, AND UBIQUITINATION OF PHYA.
RX PubMed=18722184; DOI=10.1016/j.molcel.2008.08.003;
RA Saijo Y., Zhu D., Li J., Rubio V., Zhou Z., Shen Y., Hoecker U., Wang H.,
RA Deng X.W.;
RT "Arabidopsis COP1/SPA1 complex and FHY1/FHY3 associate with distinct
RT phosphorylated forms of phytochrome A in balancing light signaling.";
RL Mol. Cell 31:607-613(2008).
RN [24]
RP DWD MOTIF.
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 [25]
RP INTERACTION WITH UVR8.
RC STRAIN=cv. Wassilewskija;
RX PubMed=19165148; DOI=10.1038/emboj.2009.4;
RA Favory J.J., Stec A., Gruber H., Rizzini L., Oravecz A., Funk M.,
RA Albert A., Cloix C., Jenkins G.I., Oakeley E.J., Seidlitz H.K., Nagy F.,
RA Ulm R.;
RT "Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and
RT stress acclimation in Arabidopsis.";
RL EMBO J. 28:591-601(2009).
RN [26]
RP INTERACTION WITH HRT/RPP8 AND CRY2.
RX PubMed=20624951; DOI=10.1073/pnas.1004529107;
RA Jeong R.-D., Chandra-Shekara A.C., Barman S.R., Navarre D., Klessig D.F.,
RA Kachroo A., Kachroo P.;
RT "Cryptochrome 2 and phototropin 2 regulate resistance protein-mediated
RT viral defense by negatively regulating an E3 ubiquitin ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13538-13543(2010).
RN [27]
RP INTERACTION WITH UVR8.
RX PubMed=21454788; DOI=10.1126/science.1200660;
RA Rizzini L., Favory J.J., Cloix C., Faggionato D., O'Hara A., Kaiserli E.,
RA Baumeister R., Schaefer E., Nagy F., Jenkins G.I., Ulm R.;
RT "Perception of UV-B by the Arabidopsis UVR8 protein.";
RL Science 332:103-106(2011).
RN [28]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SHW1, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26474641; DOI=10.1104/pp.15.01184;
RA Srivastava A.K., Senapati D., Srivastava A., Chakraborty M., Gangappa S.N.,
RA Chattopadhyay S.;
RT "SHORT HYPOCOTYL IN WHITE LIGHT1 interacts with ELONGATED HYPOCOTYL5 (HY5)
RT and CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1) and promotes COP1-mediated
RT degradation of HY5 during Arabidopsis seedling development.";
RL Plant Physiol. 169:2922-2934(2015).
RN [29]
RP INTERACTION WITH CSU2.
RX PubMed=26714275; DOI=10.1371/journal.pgen.1005747;
RA Xu D., Lin F., Jiang Y., Ling J., Hettiarachchi C., Tellgren-Roth C.,
RA Holm M., Wei N., Deng X.W.;
RT "Arabidopsis COP1 SUPPRESSOR 2 represses COP1 E3 ubiquitin ligase activity
RT through their coiled-coil domains association.";
RL PLoS Genet. 11:E1005747-E1005747(2015).
RN [30]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH DHU1.
RC STRAIN=cv. Columbia;
RX PubMed=28735869; DOI=10.1016/j.bbrc.2017.07.110;
RA Kim S.-H., Kim H., Chung S., Lee J.-H.;
RT "DHU1 negatively regulates UV-B signaling via its direct interaction with
RT COP1 and RUP1.";
RL Biochem. Biophys. Res. Commun. 491:285-290(2017).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 349-675 IN COMPLEX WITH A HUMAN
RP TRIB1 PEPTIDE.
RX PubMed=27041596; DOI=10.1016/j.str.2016.03.002;
RA Uljon S., Xu X., Durzynska I., Stein S., Adelmant G., Marto J.A.,
RA Pear W.S., Blacklow S.C.;
RT "Structural basis for substrate selectivity of the E3 ligase COP1.";
RL Structure 24:687-696(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a repressor of
CC photomorphogenesis and as an activator of etiolation in darkness. E3
CC ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating
CC enzyme in the form of a thioester and then directly transfers the
CC ubiquitin to targeted substrates. Represses photomorphogenesis in
CC darkness by mediating ubiquitination and subsequent proteasomal
CC degradation of light-induced transcription factors such as HY5, HYH and
CC LAF1. Down-regulates MYB21, probably via ubiquitination process. Light
CC stimuli abrogate the repression of photomorphogenesis, possibly due to
CC its localization to the cytoplasm. Could play a role in switching
CC between skotomorphogenetic and photomorphogenetic pathways. Mediates
CC the ubiquitination-dependent degradation of HY5 in the darkness during
CC seedling development (e.g. hypocotyl growth) (PubMed:26474641).
CC Represses CIP7 in darkness (PubMed:9668129).
CC {ECO:0000269|PubMed:11967090, ECO:0000269|PubMed:12023303,
CC ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:9668129}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:14597662};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:14597662}.
CC -!- SUBUNIT: Homodimer. Interacts with HY5, HYH, BBX24/STO, BBX25/STH,
CC CIP8, COP10, SPA1, SPA2, SPA3, SPA4 and UVR8 and phosphorylated PHYA.
CC Light induces dissociation of the SPA1/COP1 complex. Interacts with
CC HRT/RPP8 and triggers it to the 26s proteasome. Binds to CRY2; this
CC competitive interaction prevents triggering to proteasome of other
CC binding proteins (PubMed:20624951). Binds to SHW1 in the nucleus
CC (PubMed:26474641). Bonds to CIP7 (PubMed:9668129). Interacts with CSU2
CC (PubMed:26714275). Binds to CIP1 (PubMed:7753789). Interacts directly
CC with DHU1 (PubMed:28735869). {ECO:0000269|PubMed:10488108,
CC ECO:0000269|PubMed:11226162, ECO:0000269|PubMed:11461903,
CC ECO:0000269|PubMed:12887588, ECO:0000269|PubMed:14597662,
CC ECO:0000269|PubMed:15308756, ECO:0000269|PubMed:15342494,
CC ECO:0000269|PubMed:18722184, ECO:0000269|PubMed:19165148,
CC ECO:0000269|PubMed:20624951, ECO:0000269|PubMed:21454788,
CC ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:26714275,
CC ECO:0000269|PubMed:28735869, ECO:0000269|PubMed:7753789,
CC ECO:0000269|PubMed:9668129, ECO:0000269|PubMed:9755158}.
CC -!- INTERACTION:
CC P43254; Q9SID1: BBX25; NbExp=3; IntAct=EBI-301649, EBI-631960;
CC P43254; F4JZY1: CIP1; NbExp=3; IntAct=EBI-301649, EBI-2119970;
CC P43254; Q9SPL2: CIP8; NbExp=6; IntAct=EBI-301649, EBI-301644;
CC P43254; Q39057: CO; NbExp=8; IntAct=EBI-301649, EBI-1639724;
CC P43254; Q9SK53: COL3; NbExp=3; IntAct=EBI-301649, EBI-1995108;
CC P43254; P43254: COP1; NbExp=7; IntAct=EBI-301649, EBI-301649;
CC P43254; Q9LJD7: COP10; NbExp=3; IntAct=EBI-301649, EBI-2429853;
CC P43254; Q43125: CRY1; NbExp=4; IntAct=EBI-301649, EBI-300703;
CC P43254; Q96524: CRY2; NbExp=3; IntAct=EBI-301649, EBI-531555;
CC P43254; Q9FE22: HFR1; NbExp=6; IntAct=EBI-301649, EBI-626001;
CC P43254; O24646: HY5; NbExp=8; IntAct=EBI-301649, EBI-301660;
CC P43254; Q8W191-1: HYH; NbExp=3; IntAct=EBI-301649, EBI-11463635;
CC P43254; Q9M0K4: LAF1; NbExp=3; IntAct=EBI-301649, EBI-1543309;
CC P43254; P93025: PHOT2; NbExp=2; IntAct=EBI-301649, EBI-2270423;
CC P43254; Q9SJL7: RAX2; NbExp=3; IntAct=EBI-301649, EBI-2292310;
CC P43254; Q8W4J9: RPP8; NbExp=2; IntAct=EBI-301649, EBI-15865035;
CC P43254; Q9SYX2: SPA1; NbExp=17; IntAct=EBI-301649, EBI-626992;
CC P43254; Q9LJR3: SPA3; NbExp=7; IntAct=EBI-301649, EBI-626921;
CC P43254; Q94BM7: SPA4; NbExp=14; IntAct=EBI-301649, EBI-626943;
CC P43254; Q9FN03: UVR8; NbExp=4; IntAct=EBI-301649, EBI-2407499;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10072396,
CC ECO:0000269|PubMed:10480941, ECO:0000269|PubMed:26474641}. Cytoplasm
CC {ECO:0000269|PubMed:10072396, ECO:0000269|PubMed:10480941}.
CC Note=Localizes to the nucleus in darkness but is gradually relocated to
CC the cytoplasm upon illumination. Localizes to subnuclear foci (speckle)
CC and in dispersed nuclear localization in the dark.
CC {ECO:0000269|PubMed:10072396, ECO:0000269|PubMed:10480941}.
CC -!- DOMAIN: The coiled-coil domain (134-201) is necessary for SPA1, SPA3 or
CC SPA4 binding. The DWD box is required for interaction with DDB1A.
CC {ECO:0000250|UniProtKB:P29590}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:10839542,
CC ECO:0000269|PubMed:12827204, ECO:0000269|PubMed:14597662,
CC ECO:0000269|PubMed:18722184}.
CC -!- DISRUPTION PHENOTYPE: Abrogated induction of DHU1 in response to UV-B
CC (PubMed:28735869). The double mutant shw1 cop1 displays an enhanced
CC photomorphogenic growth in the darkness as well as abnormal
CC accumulation of HY5 (PubMed:26474641). The double mutant dhu1-1 cop1-6
CC phenotype resemble that of the single mutant cop1-6 (PubMed:28735869).
CC {ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:28735869}.
CC -!- MISCELLANEOUS: Plants lacking COP1 are not viable.
CC -!- MISCELLANEOUS: Although plants lack TRIB proteins, a human TRIB1
CC peptide binds to a highly conserved surface on the top face of the beta
CC propeller, indicating a general mode for recognition of peptide motifs
CC by COP1. {ECO:0000269|PubMed:27041596}.
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DR EMBL; L24437; AAA32772.1; -; mRNA.
DR EMBL; AC003033; AAB91983.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08766.1; -; Genomic_DNA.
DR EMBL; BT025337; ABF57293.1; -; mRNA.
DR EMBL; AJ000535; CAA04168.1; -; Genomic_DNA.
DR EMBL; AJ000536; CAA04169.1; -; Genomic_DNA.
DR PIR; T01112; T01112.
DR RefSeq; NP_180854.1; NM_128855.4.
DR PDB; 5IGO; X-ray; 1.60 A; A/B/C/D=349-675.
DR PDB; 5KWN; X-ray; 1.42 A; A=349-675.
DR PDB; 6QTO; X-ray; 1.27 A; A=349-675.
DR PDB; 6QTQ; X-ray; 1.30 A; A=349-675.
DR PDB; 6QTR; X-ray; 1.37 A; A=349-675.
DR PDB; 6QTS; X-ray; 1.11 A; A=349-675.
DR PDB; 6QTT; X-ray; 1.51 A; A=349-675.
DR PDB; 6QTU; X-ray; 1.30 A; A=349-675.
DR PDB; 6QTV; X-ray; 1.31 A; A=349-675.
DR PDB; 6QTW; X-ray; 1.39 A; A=349-675.
DR PDB; 6QTX; X-ray; 1.95 A; A=349-675.
DR PDBsum; 5IGO; -.
DR PDBsum; 5KWN; -.
DR PDBsum; 6QTO; -.
DR PDBsum; 6QTQ; -.
DR PDBsum; 6QTR; -.
DR PDBsum; 6QTS; -.
DR PDBsum; 6QTT; -.
DR PDBsum; 6QTU; -.
DR PDBsum; 6QTV; -.
DR PDBsum; 6QTW; -.
DR PDBsum; 6QTX; -.
DR AlphaFoldDB; P43254; -.
DR SMR; P43254; -.
DR BioGRID; 3204; 59.
DR DIP; DIP-32850N; -.
DR ELM; P43254; -.
DR IntAct; P43254; 30.
DR MINT; P43254; -.
DR STRING; 3702.AT2G32950.1; -.
DR iPTMnet; P43254; -.
DR PaxDb; P43254; -.
DR PRIDE; P43254; -.
DR ProteomicsDB; 220616; -.
DR EnsemblPlants; AT2G32950.1; AT2G32950.1; AT2G32950.
DR GeneID; 817857; -.
DR Gramene; AT2G32950.1; AT2G32950.1; AT2G32950.
DR KEGG; ath:AT2G32950; -.
DR Araport; AT2G32950; -.
DR TAIR; locus:2059359; AT2G32950.
DR eggNOG; KOG0297; Eukaryota.
DR HOGENOM; CLU_006994_2_1_1; -.
DR InParanoid; P43254; -.
DR OMA; RMHAHFD; -.
DR OrthoDB; 857220at2759; -.
DR PhylomeDB; P43254; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P43254; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P43254; baseline and differential.
DR Genevisible; P43254; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:TAIR.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; TAS:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0046283; P:anthocyanin-containing compound metabolic process; IMP:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IGI:TAIR.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009963; P:positive regulation of flavonoid biosynthetic process; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0009641; P:shade avoidance; IMP:TAIR.
DR GO; GO:0009647; P:skotomorphogenesis; TAS:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042755; COP1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR44080; PTHR44080; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Phytochrome signaling pathway; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger.
FT CHAIN 1..675
FT /note="E3 ubiquitin-protein ligase COP1"
FT /id="PRO_0000055881"
FT REPEAT 369..408
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 418..458
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 461..501
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 503..543
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 547..585
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 588..627
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 642..675
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT ZN_FING 52..90
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..177
FT /note="CLS (cytoplasmic localization signal)"
FT /evidence="ECO:0000303|PubMed:10072396,
FT ECO:0000303|PubMed:10480941"
FT REGION 120..177
FT /note="SNLS (subnuclear localization signal)"
FT /evidence="ECO:0000303|PubMed:10480941"
FT REGION 261..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..595
FT /note="Binding of human TRIB1 COP1-binding-motif"
FT /evidence="ECO:0000269|PubMed:27041596"
FT COILED 134..201
FT /evidence="ECO:0000255"
FT MOTIF 294..317
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29590"
FT SITE 422
FT /note="Human TRIB1 COP1-binding motif"
FT /evidence="ECO:0000269|PubMed:27041596"
FT SITE 441
FT /note="Human TRIB1 COP1-binding motif"
FT /evidence="ECO:0000269|PubMed:27041596"
FT MUTAGEN 52
FT /note="C->S: Abolishes LAF1 ubiquitination and degradation;
FT when associated with S-55."
FT /evidence="ECO:0000269|PubMed:12827204"
FT MUTAGEN 55
FT /note="C->S: Abolishes LAF1 ubiquitination and degradation;
FT when associated with S-52."
FT /evidence="ECO:0000269|PubMed:12827204"
FT MUTAGEN 294..296
FT /note="RKK->SKT: Abolishes localization to the nucleus."
FT /evidence="ECO:0000269|PubMed:10072396"
FT MUTAGEN 312..314
FT /note="KRR->TRS: Abolishes localization to the nucleus."
FT /evidence="ECO:0000269|PubMed:10072396"
FT MUTAGEN 422
FT /note="K->E: 5-fold increase in interaction with HY5, weak
FT interaction with BBX24/STO and BBX25/STH, and at low light
FT intensity shorter hypocotyl."
FT /evidence="ECO:0000269|PubMed:11226162"
FT MUTAGEN 465
FT /note="R->E: No interaction with BBX24/STO and BBX25/STH,
FT and at low light intensity shorter hypocotyl."
FT /evidence="ECO:0000269|PubMed:11226162"
FT MUTAGEN 467
FT /note="W->A: No interaction with HY5, BBX24/STO and
FT BBX25/STH and at low light intensity shorter hypocotyl."
FT /evidence="ECO:0000269|PubMed:11226162"
FT MUTAGEN 523..584
FT /note="Missing: In COP1-8; no interaction with SPA1 and
FT lethal."
FT MUTAGEN 524
FT /note="G->E: In COP1-9; no interaction with HY5, SPA1,
FT BBX25/STH or BBX24/STO and lethal."
FT MUTAGEN 550
FT /note="K->E: No interaction with HY5, BBX24/STO and
FT BBX25/STH and at low light intensity shorter hypocotyl."
FT /evidence="ECO:0000269|PubMed:11226162"
FT MUTAGEN 592
FT /note="E->R: Better interaction with HY5, BBX24/STO and
FT BBX25/STH and slightly longer hypocotyls."
FT /evidence="ECO:0000269|PubMed:11226162"
FT CONFLICT 292
FT /note="M -> I (in Ref. 1; AAA32772)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="E -> Q (in Ref. 5; CAA04168)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="R -> P (in Ref. 5; CAA04168)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="V -> F (in Ref. 1; AAA32772)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="L -> R (in Ref. 1; AAA32772)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="P -> R (in Ref. 5; CAA04169)"
FT /evidence="ECO:0000305"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6QTO"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:6QTS"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:5IGO"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:6QTS"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:6QTS"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:5KWN"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:6QTS"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 552..567
FT /evidence="ECO:0007829|PDB:6QTS"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:6QTS"
FT TURN 577..580
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 581..586
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 612..618
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:6QTS"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:5IGO"
FT TURN 637..639
FT /evidence="ECO:0007829|PDB:5IGO"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:6QTO"
FT STRAND 647..652
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 656..663
FT /evidence="ECO:0007829|PDB:6QTS"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:6QTS"
SQ SEQUENCE 675 AA; 76188 MW; E6D9A1B702EAE8F0 CRC64;
MEEISTDPVV PAVKPDPRTS SVGEGANRHE NDDGGSGGSE IGAPDLDKDL LCPICMQIIK
DAFLTACGHS FCYMCIITHL RNKSDCPCCS QHLTNNQLYP NFLLDKLLKK TSARHVSKTA
SPLDQFREAL QRGCDVSIKE VDNLLTLLAE RKRKMEQEEA ERNMQILLDF LHCLRKQKVD
ELNEVQTDLQ YIKEDINAVE RHRIDLYRAR DRYSVKLRML GDDPSTRNAW PHEKNQIGFN
SNSLSIRGGN FVGNYQNKKV EGKAQGSSHG LPKKDALSGS DSQSLNQSTV SMARKKRIHA
QFNDLQECYL QKRRQLADQP NSKQENDKSV VRREGYSNGL ADFQSVLTTF TRYSRLRVIA
EIRHGDIFHS ANIVSSIEFD RDDELFATAG VSRCIKVFDF SSVVNEPADM QCPIVEMSTR
SKLSCLSWNK HEKNHIASSD YEGIVTVWDV TTRQSLMEYE EHEKRAWSVD FSRTEPSMLV
SGSDDCKVKV WCTRQEASVI NIDMKANICC VKYNPGSSNY IAVGSADHHI HYYDLRNISQ
PLHVFSGHKK AVSYVKFLSN NELASASTDS TLRLWDVKDN LPVRTFRGHT NEKNFVGLTV
NSEYLACGSE TNEVYVYHKE ITRPVTSHRF GSPDMDDAEE EAGSYFISAV CWKSDSPTML
TANSQGTIKV LVLAA
