COP1_PEA
ID COP1_PEA Reviewed; 672 AA.
AC P93471;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=E3 ubiquitin-protein ligase COP1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P43254};
DE AltName: Full=Constitutive photomorphogenesis protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase COP1 {ECO:0000305};
GN Name=COP1;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9512668; DOI=10.1016/s0167-4781(97)00200-5;
RA Zhao L., Zhu Y., Wu X., Zhao J.;
RT "Molecular cloning and sequencing of the cDNA of cop1 gene from Pisum
RT sativum.";
RL Biochim. Biophys. Acta 1395:326-328(1998).
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. Light stimuli
CC abrogate the repression of photomorphogenesis, possibly due to its
CC localization to the cytoplasm. Could play a role in switching between
CC skotomorphogenetic and photomorphogenetic pathways.
CC {ECO:0000250|UniProtKB:P43254}.
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:0000250|UniProtKB:P43254};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COP1 family. {ECO:0000305}.
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DR EMBL; Y09579; CAA70768.1; -; mRNA.
DR PIR; T06560; T06560.
DR AlphaFoldDB; P93471; -.
DR SMR; P93471; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Phytochrome signaling pathway; Repeat; Transferase;
KW Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger.
FT CHAIN 1..672
FT /note="E3 ubiquitin-protein ligase COP1"
FT /id="PRO_0000055882"
FT REPEAT 366..405
FT /note="WD 1"
FT REPEAT 415..455
FT /note="WD 2"
FT REPEAT 458..498
FT /note="WD 3"
FT REPEAT 500..540
FT /note="WD 4"
FT REPEAT 544..582
FT /note="WD 5"
FT REPEAT 585..624
FT /note="WD 6"
FT REPEAT 639..671
FT /note="WD 7"
FT ZN_FING 47..85
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 62..172
FT /note="CLS (cytoplasmic localization signal)"
FT /evidence="ECO:0000250"
FT REGION 115..172
FT /note="SNLS (subnuclear localization signal)"
FT /evidence="ECO:0000250"
FT REGION 216..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 129..196
FT /evidence="ECO:0000255"
FT MOTIF 291..314
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 225..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 76033 MW; 64DFFDF2C3E68807 CRC64;
MEEHSVGPLV PAVVKPEPSK NFSTDTTAAG TFLLVPTMSD LDKDFLCPIC MQIIKDAFLT
ACGHSFCYMC IITHLRNKSD CPCCGHYLTN SNLFPNFLLD KLLKKTSDRQ ISKTASPVEH
FRQAVQKGCE VTMKELDTLL LLLTEKKRKM EQEEAERNMQ ILLDFLHCLR KQKVDELKEV
QTDLQFIKED IGAVEKHRMD LYRARDRYSV KLRMLDDSGG RKSRHSSMDL NSSGLASSPL
NLRGGLSSGS HTKKNDGKSQ ISSHGHGIQR RDPITGSDSQ YINQSGLALV RKKRVHTQFN
DLQECYLQKR RQAADKPHGQ QERDTNFISR EGYSCGLDDF QSVLTTFTRY SRLRVIAEIR
HGDIFHSANI VSSIEFDRDD DLFATAGVSR RIKVFDFSAV VNEPTDAHCP VVEMTTRSKL
SCLSWNKYAK NQIASSDYEG IVTVWTMTTR KSLMEYEEHE KRAWSVDFSR TDPSMLVSGS
DDCKVKVWCT NQEASVLNID MKANICCVKY NPGSGNYIAV GSADHHIHYY DLRNISRPVH
VFTGHKKAVS YVKFLSNDEL ASASTDSTLR LWDVKQNLPV RTFRGHANEK NFVGLTVRSE
YIACGSETNE VFVYHKEISK PLTWHRFGTL DMEDAEDEAG SYFISAVCWK SDRPTILTAN
SQGTIKVLVL AA
