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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}.
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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
 
 
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