CIP7_ARATH
ID CIP7_ARATH Reviewed; 1058 AA.
AC O80386; M9P1T0; M9P1T2; M9P1T3; M9P1T5; M9P3Q3; M9P3Q9; M9P3R1; M9P3Z4;
AC M9P407; M9P412; M9P4F1; M9P4F6; M9P4G1; M9P4G6; M9P6Z0; M9P6Z1; M9P6Z2;
AC Q56WV4; Q7GDB1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=COP1-interacting protein 7 {ECO:0000303|PubMed:9668129};
GN Name=CIP7 {ECO:0000303|PubMed:9668129};
GN OrderedLocusNames=At4g27430 {ECO:0000312|Araport:AT4G27430};
GN ORFNames=F27G19.30 {ECO:0000312|EMBL:CAB43875.1};
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], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-235,
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP COP1, AND INDUCTION BY LIGHT.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 [GENOMIC DNA] OF 687-915.
RC STRAIN=cv. Ak-1, cv. C24, cv. Columbia, cv. Ct-1, cv. Ei-2, cv. Ei-6,
RC cv. Kb-0, cv. Kon, cv. Ler-1, cv. Mt-0, cv. Mz-0, cv. Nd-1, cv. Oy-0,
RC cv. Petergof, cv. Ra-0, cv. Se-0, and cv. Yo-0;
RX PubMed=23554957; DOI=10.1371/journal.pone.0058916;
RA Vigueira C.C., Rauh B., Mitchell-Olds T., Lawton-Rauh A.L.;
RT "Signatures of demography and recombination at coding genes in naturally-
RT distributed populations of Arabidopsis lyrata subsp. petraea.";
RL PLoS ONE 8:E58916-E58916(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 780-1058.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-915 AND SER-992, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Exhibits transcriptional activation activity. Positive
CC regulator of light-regulated genes, probably being a direct downstream
CC target of COP1 for mediating light control of gene expression.
CC {ECO:0000269|PubMed:9668129}.
CC -!- SUBUNIT: Interacts with COP1. {ECO:0000269|PubMed:9668129}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:9668129}.
CC -!- INDUCTION: Triggered by light. Repressed by COP1 in darkness.
CC {ECO:0000269|PubMed:9668129}.
CC -!- DISRUPTION PHENOTYPE: Defects in light-dependent anthocyanin and
CC chlorophyll accumulation, as well as defects in the light control
CC expression of light-inducible genes involved in anthocyanin
CC biosynthesis and photosynthesis. {ECO:0000269|PubMed:9668129}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB012912; BAA31738.1; -; mRNA.
DR EMBL; AL078467; CAB43875.1; -; Genomic_DNA.
DR EMBL; AL161571; CAB81393.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85339.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85340.1; -; Genomic_DNA.
DR EMBL; AB012913; BAA31739.1; -; Genomic_DNA.
DR EMBL; JX858616; AFX87054.1; -; Genomic_DNA.
DR EMBL; JX858617; AFX87055.1; -; Genomic_DNA.
DR EMBL; JX858618; AFX87056.1; -; Genomic_DNA.
DR EMBL; JX858619; AFX87057.1; -; Genomic_DNA.
DR EMBL; JX858621; AFX87059.1; -; Genomic_DNA.
DR EMBL; JX858622; AFX87060.1; -; Genomic_DNA.
DR EMBL; JX858625; AFX87063.1; -; Genomic_DNA.
DR EMBL; JX858626; AFX87064.1; -; Genomic_DNA.
DR EMBL; JX858627; AFX87065.1; -; Genomic_DNA.
DR EMBL; JX858628; AFX87066.1; -; Genomic_DNA.
DR EMBL; JX858629; AFX87067.1; -; Genomic_DNA.
DR EMBL; JX858630; AFX87068.1; -; Genomic_DNA.
DR EMBL; JX858632; AFX87069.1; -; Genomic_DNA.
DR EMBL; JX858633; AFX87070.1; -; Genomic_DNA.
DR EMBL; JX858634; AFX87071.1; -; Genomic_DNA.
DR EMBL; JX858635; AFX87072.1; -; Genomic_DNA.
DR EMBL; JX858636; AFX87073.1; -; Genomic_DNA.
DR EMBL; AK221927; BAD94351.1; -; mRNA.
DR PIR; T08935; T08935.
DR RefSeq; NP_001119068.1; NM_001125596.2.
DR RefSeq; NP_194473.1; NM_118877.4.
DR AlphaFoldDB; O80386; -.
DR STRING; 3702.AT4G27430.2; -.
DR iPTMnet; O80386; -.
DR PaxDb; O80386; -.
DR PRIDE; O80386; -.
DR ProteomicsDB; 246499; -.
DR EnsemblPlants; AT4G27430.1; AT4G27430.1; AT4G27430.
DR EnsemblPlants; AT4G27430.2; AT4G27430.2; AT4G27430.
DR GeneID; 828851; -.
DR Gramene; AT4G27430.1; AT4G27430.1; AT4G27430.
DR Gramene; AT4G27430.2; AT4G27430.2; AT4G27430.
DR KEGG; ath:AT4G27430; -.
DR Araport; AT4G27430; -.
DR TAIR; locus:2124039; AT4G27430.
DR eggNOG; ENOG502QTSA; Eukaryota.
DR HOGENOM; CLU_008836_1_0_1; -.
DR InParanoid; O80386; -.
DR OMA; YMQNFQG; -.
DR OrthoDB; 170880at2759; -.
DR PhylomeDB; O80386; -.
DR PRO; PR:O80386; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O80386; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:TAIR.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IDA:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1058
FT /note="COP1-interacting protein 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441273"
FT REGION 123..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 340..347
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 431..438
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 764..771
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 123..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 1058 AA; 118425 MW; CF6C3693F5F02D73 CRC64;
MDPRTRLDYA LFQLTPTRTR CDLVIFSGGE NEKLASGIFQ PFVTHLKSVS DQISKGGYSV
TLRPSSVGVP WFTKVTLQRF VRFVTTPEVL ERSVTLEKEI EQIEDSIQAN AAAIAGEAEG
NELGGTWTSQ KSTALSKTKG ETDGDTVEEN SKVGLQRVLE NRKAALCKEQ AMAYARALVV
GFELDYMDDL FSFADAFGAS RLREACVNFV DLCKRKNEDR MWVDQITAMQ AFPRPELTFM
GDSGIVLAGE ENDLLNATNV KHGNSMDASS QGSFETGQEG RAQMAMPWPN QFPQYMQNFQ
GHGYPPPYMF PGMQGQSPYF HGNMQWPVNM GDVESNEKSS KKKKKKKKNK KKSKQDESAE
PSDNSSTETE SEDGNEGKKQ SRKVVIRNIN YITSKRNGAK ESDSDESGEE EGFVDGDSIK
QQVEEAIGSV ERRHKSTSHR QRKHKSHNGD DDSSNKETKG NDNWDAFQNL LLKDNDSEPE
ELLRISSTAL NMASEVVRKR EPPSDDSFLV AIGNEDWGRE TSIEKFNAGE NVRIIRKGNN
YDEEMLNPGR SDESRSYSQA EMSVHDGKLR TRNEAEEDWF IRNQAGPETD PSLVKTFVGD
HFHLNKSSER DVLTDDSFMI HSRVENQVED SRLRTEIMDL DVYGTTQQEN SAPENTPHEP
DDLYMVLGRE QDVKPTLLPW TPEIDFETNT LAQRTSRIDL ITATKASAGE QTLDGKEKKS
RGISKGKDAK SRASSRPDPA SKAKRPAWGS RAAVSKSKSE MEEERKKRME ELLIQRQKRI
AEKSSGGSVS SSLASKKTPT VTKSVKSSIK NEKTPEAAQS KAKPVLRSST IERLAVARTA
PKEPQQKPVI KRTSKPSGYK TEKAQEKKSS KIGQSDAKSV ELSRDPSLEI KETVVEDSHS
YLSEKQVDAL PAVASVDDFK DIKELHSLPS EETARVKNRP NEIIAEKVQD QTKIDDQETV
KNTSVSEDKQ ITTKHYSEDV GEVQASQEKP VSPKKSVTFS ETNMEEKYYF SPAVSEIDIS
TPPATEADHS RKKWNSEETS PKATAKVFRK LLMFGRKK