CIP8_ARATH
ID CIP8_ARATH Reviewed; 334 AA.
AC Q9SPL2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=E3 ubiquitin-protein ligase CIP8;
DE EC=2.3.2.27 {ECO:0000269|PubMed:12028569};
DE AltName: Full=COP1-interacting protein 8;
DE AltName: Full=RING-type E3 ubiquitin transferase CIP8 {ECO:0000305};
GN Name=CIP8; OrderedLocusNames=At5g64920; ORFNames=MXK3.15;
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 COP1, AND MUTAGENESIS OF CYS-275; HIS-277;
RP HIS-280 AND CYS-283.
RC STRAIN=cv. Columbia; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
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 FUNCTION, CATALYTIC ACTIVITY, DOMAIN, INTERACTION WITH UBC8, AND
RP MUTAGENESIS OF CYS-275; HIS-277; HIS-280 AND CYS-283.
RX PubMed=12028569; DOI=10.1046/j.1365-313x.2002.01298.x;
RA Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W.;
RT "Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1
RT interacting protein 8 (CIP8).";
RL Plant J. 30:385-394(2002).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. Probably forms a
CC minimal ubiquitin ligase complex in cooperation with the E2 enzyme
CC UBC8. Its interaction with COP1 suggests that it may participate in
CC proteasome-mediated degradation of HY5 in vivo.
CC {ECO:0000269|PubMed:10488108, ECO:0000269|PubMed:12028569}.
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:12028569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the RING finger of COP1. Interacts with UBC8
CC through its N-terminal region. {ECO:0000269|PubMed:10488108,
CC ECO:0000269|PubMed:12028569}.
CC -!- INTERACTION:
CC Q9SPL2; P43254: COP1; NbExp=6; IntAct=EBI-301644, EBI-301649;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10488108}.
CC -!- TISSUE SPECIFICITY: Expressed in both light- and dark-grown seedlings.
CC {ECO:0000269|PubMed:10488108}.
CC -!- DOMAIN: The RING-type zinc finger domain is required but not sufficient
CC for ubiquitin ligase activity. It mediates the interaction with the
CC RING finger of COP1. {ECO:0000269|PubMed:12028569}.
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DR EMBL; AF162150; AAD56636.1; -; mRNA.
DR EMBL; AB019236; BAA97304.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97970.1; -; Genomic_DNA.
DR EMBL; AY081279; AAL91168.1; -; mRNA.
DR EMBL; BT008730; AAP42743.1; -; mRNA.
DR PIR; T51245; T51245.
DR RefSeq; NP_201297.1; NM_125891.3.
DR AlphaFoldDB; Q9SPL2; -.
DR SMR; Q9SPL2; -.
DR BioGRID; 21858; 4.
DR IntAct; Q9SPL2; 4.
DR STRING; 3702.AT5G64920.1; -.
DR PaxDb; Q9SPL2; -.
DR PRIDE; Q9SPL2; -.
DR ProteomicsDB; 246679; -.
DR EnsemblPlants; AT5G64920.1; AT5G64920.1; AT5G64920.
DR GeneID; 836616; -.
DR Gramene; AT5G64920.1; AT5G64920.1; AT5G64920.
DR KEGG; ath:AT5G64920; -.
DR Araport; AT5G64920; -.
DR TAIR; locus:2177684; AT5G64920.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_053614_0_0_1; -.
DR InParanoid; Q9SPL2; -.
DR OMA; DGWDNDE; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q9SPL2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SPL2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SPL2; baseline and differential.
DR Genevisible; Q9SPL2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..334
FT /note="E3 ubiquitin-protein ligase CIP8"
FT /id="PRO_0000055875"
FT ZN_FING 257..298
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 111..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 275
FT /note="C->A: Abolishes interaction with COP1 and
FT ubiquitination of HY5 in vitro; when associated with A-277;
FT A-280 and A-283."
FT /evidence="ECO:0000269|PubMed:10488108,
FT ECO:0000269|PubMed:12028569"
FT MUTAGEN 277
FT /note="H->A: Abolishes interaction with COP1 and
FT ubiquitination of HY5 in vitro; when associated with A-275;
FT A-280 and A-283."
FT /evidence="ECO:0000269|PubMed:10488108,
FT ECO:0000269|PubMed:12028569"
FT MUTAGEN 280
FT /note="H->A: Abolishes interaction with COP1 and
FT ubiquitination of HY5 in vitro; when associated with A-275;
FT A-277 and A-283."
FT /evidence="ECO:0000269|PubMed:10488108,
FT ECO:0000269|PubMed:12028569"
FT MUTAGEN 283
FT /note="C->A: Abolishes interaction with COP1 and
FT ubiquitination of HY5 in vitro; when associated with A-275;
FT A-277 and A-280."
FT /evidence="ECO:0000269|PubMed:10488108,
FT ECO:0000269|PubMed:12028569"
SQ SEQUENCE 334 AA; 36965 MW; 59EADBA18782E0B8 CRC64;
MSDAPSSSPD ATASHWCYHC NKRVVVETLD DFVVCCECNK GFVESIQPTP AAYSSPAPPQ
PLSPDLNVED SSIGSHFLQM LRLLAHAPSQ RSPPRHLDVL SYEDDFFRLE LNSRNEIDDD
EDEDEDDGDE EEEDEEENLT VNDEEDEEDD LRRRNRFPLT TTQSRTGRNR ILDWAEILMG
IEDNSIEFRM ESDRYAGNPA DYIDDAAGYE ALLQNLAEGD GGGGGGRRGA PPAAKSAIEA
LETFEVSSSE GEMVMVCAVC KDGMVMGETG KKLPCGHCYH GDCIVPWLGT RNSCPVCRFQ
LETDDAEYEE ERKKRTSTVS DSAAASSSSS TSRY
