COP10_ARATH
ID COP10_ARATH Reviewed; 182 AA.
AC Q9LJD7; A0A178VI85; Q0WNL1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Constitutive photomorphogenesis protein 10;
GN Name=COP10; OrderedLocusNames=At3g13550; ORFNames=MRP15.21;
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH CSN3; CSN4 AND CSN8, AND MUTAGENESIS OF
RP THR-78.
RX PubMed=11877375; DOI=10.1101/gad.964602;
RA Suzuki G., Yanagawa Y., Kwok S.F., Matsui M., Deng X.-W.;
RT "Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts
RT together with COP1 and the COP9 signalosome in repressing
RT photomorphogenesis.";
RL Genes Dev. 16:554-559(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, IDENTIFICATION IN CDD COMPLEX WITH DDB1A AND DET1, AND
RP INTERACTION WITH COP1 AND UBC5.
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 [6]
RP IDENTIFICATION IN CDD COMPLEX WITH DET1 AND DDB1A.
RX PubMed=24563205; DOI=10.1105/tpc.113.122234;
RA Irigoyen M.L., Iniesto E., Rodriguez L., Puga M.I., Yanagawa Y., Pick E.,
RA Strickland E., Paz-Ares J., Wei N., De Jaeger G., Rodriguez P.L.,
RA Deng X.W., Rubio V.;
RT "Targeted degradation of abscisic acid receptors is mediated by the
RT ubiquitin ligase substrate adaptor DDA1 in Arabidopsis.";
RL Plant Cell 26:712-728(2014).
CC -!- FUNCTION: Component of light signal transduction machinery. Involved in
CC repression of photomorphogenesis in darkness by participating in the
CC CDD complex, a complex probably required to regulate the activity of
CC ubiquitin conjugating enzymes (E2s). Repression of photomorphogenesis
CC is probably mediated by ubiquitination and subsequent degradation of
CC photomorphogenesis-promoting factors such as HY5, HYH and LAF1.
CC Although strongly related to ubiquitin-conjugating enzyme, it has no
CC catalytic activity by itself due to the absence of the conserved Cys
CC active site at position 120. It can however enhance the activity of E2
CC conjugating enzymes. {ECO:0000269|PubMed:11877375,
CC ECO:0000269|PubMed:15342494}.
CC -!- SUBUNIT: Component of the CDD complex, at least composed of COP10, DET1
CC and DDB1A (PubMed:15342494, PubMed:24563205). Interacts with E3
CC ubiquitin ligase COP1. Interacts with E2 ubiquitin conjugating UBC5.
CC Interacts with CSN3, CSN4 and CSN8 subunits of the COP9 complex.
CC {ECO:0000269|PubMed:11877375, ECO:0000269|PubMed:15342494,
CC ECO:0000269|PubMed:24563205}.
CC -!- INTERACTION:
CC Q9LJD7; P43254: COP1; NbExp=3; IntAct=EBI-2429853, EBI-301649;
CC Q9LJD7; Q8LGH4: CUL4; NbExp=4; IntAct=EBI-2429853, EBI-541750;
CC Q9LJD7; Q9M0V3: DDB1A; NbExp=5; IntAct=EBI-2429853, EBI-1632780;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11877375}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LJD7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flower, leaf, stem and seedling.
CC Expressed at lower level in root. {ECO:0000269|PubMed:11877375}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AY034618; AAK57749.1; -; mRNA.
DR EMBL; AP000603; BAB01762.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75370.1; -; Genomic_DNA.
DR EMBL; AK229428; BAF01288.1; -; mRNA.
DR RefSeq; NP_566459.2; NM_112201.5. [Q9LJD7-1]
DR AlphaFoldDB; Q9LJD7; -.
DR SMR; Q9LJD7; -.
DR BioGRID; 5891; 15.
DR IntAct; Q9LJD7; 8.
DR STRING; 3702.AT3G13550.1; -.
DR PaxDb; Q9LJD7; -.
DR PRIDE; Q9LJD7; -.
DR ProteomicsDB; 242288; -. [Q9LJD7-1]
DR EnsemblPlants; AT3G13550.1; AT3G13550.1; AT3G13550. [Q9LJD7-1]
DR GeneID; 820557; -.
DR Gramene; AT3G13550.1; AT3G13550.1; AT3G13550. [Q9LJD7-1]
DR KEGG; ath:AT3G13550; -.
DR Araport; AT3G13550; -.
DR TAIR; locus:2092830; AT3G13550.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_14_3_1; -.
DR InParanoid; Q9LJD7; -.
DR OMA; GDRAKHD; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; Q9LJD7; -.
DR PRO; PR:Q9LJD7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJD7; baseline and differential.
DR Genevisible; Q9LJD7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0010099; P:regulation of photomorphogenesis; IMP:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phytochrome signaling pathway;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..182
FT /note="Constitutive photomorphogenesis protein 10"
FT /id="PRO_0000082611"
FT DOMAIN 36..182
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MUTAGEN 78
FT /note="T->I: In COP10-4; induces an open cotyledon
FT phenotype due to defects in photomorphogenic repression."
FT /evidence="ECO:0000269|PubMed:11877375"
SQ SEQUENCE 182 AA; 20130 MW; 6F255A398ECE901E CRC64;
MMTPGGSGRL RPLPTAMYAG YSGTASSWVA KTSVSASGKR IQREMAELNI DPPPDCSAGP
KGDNLYHWIA TIIGPSGTPY EGGIFFLDII FPSDYPFKPP KLVFKTRIYH CNVDTAGDLS
VNILRDSWSP ALTITKVLQA IRSIFLKPEP YSPALPVIAR LYLTDREKHD EVAKEWTLRF
AK
