CSN8_ARATH
ID CSN8_ARATH Reviewed; 197 AA.
AC P43255; Q8GWZ4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=COP9 signalosome complex subunit 8;
DE Short=CSN complex subunit 8;
DE AltName: Full=Constitutive photomorphogenesis protein 9;
DE AltName: Full=Protein FUSCA 7;
GN Name=CSN8; Synonyms=COP9, FUS7; OrderedLocusNames=At4g14110;
GN ORFNames=dl3095c;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8033203; DOI=10.1016/0092-8674(94)90578-9;
RA Wei N., Chamovitz D.A., Deng X.-W.;
RT "Arabidopsis COP9 is a component of a novel signaling complex mediating
RT light control of development.";
RL Cell 78:117-124(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-197.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-197.
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 [7]
RP COMPONENT OF THE COP9 COMPLEX WITH CSN1.
RX PubMed=8689678; DOI=10.1016/s0092-8674(00)80082-3;
RA Chamovitz D.A., Wei N., Osterlund M.T., von Arnim A.G., Staub J.M.,
RA Matsui M., Deng X.-W.;
RT "The COP9 complex, a novel multisubunit nuclear regulator involved in light
RT control of a plant developmental switch.";
RL Cell 86:115-121(1996).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8953769; DOI=10.2307/3870411;
RA Staub J.M., Wei N., Deng X.-W.;
RT "Evidence for FUS6 as a component of the nuclear-localized COP9 complex in
RT Arabidopsis.";
RL Plant Cell 8:2047-2056(1996).
RN [9]
RP FUNCTION.
RX PubMed=11337587; DOI=10.1126/science.1059776;
RA Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
RA Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
RT "Interactions of the COP9 signalosome with the E3 ubiquitin ligase
RT SCF(TIR1) in mediating auxin response.";
RL Science 292:1379-1382(2001).
RN [10]
RP INTERACTION WITH COP10.
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 [11]
RP INTERACTION WITH CSN4 AND CSN7.
RX PubMed=12615944; DOI=10.1105/tpc.009092;
RA Serino G., Su H., Peng Z., Tsuge T., Wei N., Gu H., Deng X.-W.;
RT "Characterization of the last subunit of the Arabidopsis COP9 signalosome:
RT implications for the overall structure and origin of the complex.";
RL Plant Cell 15:719-731(2003).
RN [12]
RP INTERACTION WITH TIF3H1.
RX PubMed=15548739; DOI=10.1105/tpc.104.026880;
RA Kim T.-H., Kim B.-H., Yahalom A., Chamovitz D.A., von Arnim A.G.;
RT "Translational regulation via 5' mRNA leader sequences revealed by
RT mutational analysis of the Arabidopsis translation initiation factor
RT subunit eIF3h.";
RL Plant Cell 16:3341-3356(2004).
RN [13]
RP INTERACTION WITH CSN7.
RX PubMed=18854373; DOI=10.1105/tpc.107.053801;
RA Dessau M., Halimi Y., Erez T., Chomsky-Hecht O., Chamovitz D.A.,
RA Hirsch J.A.;
RT "The Arabidopsis COP9 signalosome subunit 7 is a model PCI domain protein
RT with subdomains involved in COP9 signalosome assembly.";
RL Plant Cell 20:2815-2834(2008).
RN [14]
RP INTERACTION WITH TIF3E1.
RX PubMed=19704582; DOI=10.4161/psb.3.6.5434;
RA Paz-Aviram T., Yahalom A., Chamovitz D.A.;
RT "Arabidopsis eIF3e interacts with subunits of the ribosome, Cop9
RT signalosome and proteasome.";
RL Plant Signal. Behav. 3:409-411(2008).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes such as
CC photomorphogenesis and auxin and jasmonate responses. The CSN complex
CC is an essential regulator of the ubiquitin (Ubl) conjugation pathway by
CC mediating the deneddylation of the cullin subunits of SCF-type E3
CC ligase complexes, leading to decrease the Ubl ligase activity of SCF.
CC It is involved in repression of photomorphogenesis in darkness by
CC regulating the activity of COP1-containing Ubl ligase complexes. The
CC complex is also required for degradation of IAA6 by regulating the
CC activity of the Ubl ligase SCF-TIR complex.
CC {ECO:0000269|PubMed:11337587}.
CC -!- SUBUNIT: Component of the CSN complex, probably composed of CSN1, CSN2,
CC CSN3, CSN4, CSN5 (CSN5A or CSN5B), CSN6 (CSN6A or CSN6B), CSN7 and
CC CSN8. In the complex, it probably interacts directly with CSN4.
CC Interacts with itself and (via PCI domain) with CSN7 (via PCI domain).
CC Interacts with COP10. Binds to the translation initiation factors
CC TIF3E1 and TIF3H1 (PubMed:19704582, PubMed:15548739).
CC {ECO:0000269|PubMed:11877375, ECO:0000269|PubMed:12615944,
CC ECO:0000269|PubMed:15548739, ECO:0000269|PubMed:18854373,
CC ECO:0000269|PubMed:19704582}.
CC -!- INTERACTION:
CC P43255; P45432: CSN1; NbExp=4; IntAct=EBI-530981, EBI-530996;
CC P43255; Q8W575: CSN3; NbExp=6; IntAct=EBI-530981, EBI-531055;
CC P43255; Q8L5U0: CSN4; NbExp=3; IntAct=EBI-530981, EBI-531074;
CC P43255; Q94JU3: CSN7; NbExp=3; IntAct=EBI-530981, EBI-531152;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8953769}. Nucleus
CC {ECO:0000305|PubMed:8953769}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8953769}.
CC -!- SIMILARITY: Belongs to the CSN8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43138.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L32874; AAA32773.1; -; mRNA.
DR EMBL; Z97335; CAB10190.1; -; Genomic_DNA.
DR EMBL; AL161538; CAB78453.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83376.1; -; Genomic_DNA.
DR EMBL; AK118535; BAC43138.1; ALT_INIT; mRNA.
DR EMBL; BT006489; AAP21297.1; -; mRNA.
DR PIR; A54842; A54842.
DR RefSeq; NP_193147.1; NM_117488.4.
DR AlphaFoldDB; P43255; -.
DR SMR; P43255; -.
DR BioGRID; 12346; 17.
DR IntAct; P43255; 12.
DR STRING; 3702.AT4G14110.1; -.
DR PaxDb; P43255; -.
DR PRIDE; P43255; -.
DR ProteomicsDB; 220370; -.
DR DNASU; 827049; -.
DR EnsemblPlants; AT4G14110.1; AT4G14110.1; AT4G14110.
DR GeneID; 827049; -.
DR Gramene; AT4G14110.1; AT4G14110.1; AT4G14110.
DR KEGG; ath:AT4G14110; -.
DR Araport; AT4G14110; -.
DR TAIR; locus:2129435; AT4G14110.
DR eggNOG; KOG4414; Eukaryota.
DR HOGENOM; CLU_098091_0_0_1; -.
DR InParanoid; P43255; -.
DR OMA; DFSTRMV; -.
DR OrthoDB; 1577916at2759; -.
DR PhylomeDB; P43255; -.
DR PRO; PR:P43255; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P43255; baseline and differential.
DR Genevisible; P43255; AT.
DR GO; GO:0008180; C:COP9 signalosome; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004222; F:metalloendopeptidase activity; TAS:TAIR.
DR GO; GO:0010387; P:COP9 signalosome assembly; IMP:TAIR.
DR GO; GO:0000338; P:protein deneddylation; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR InterPro; IPR033205; COP9_CSN8.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR13339; PTHR13339; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Nucleus; Phytochrome signaling pathway;
KW Reference proteome; Signalosome.
FT CHAIN 1..197
FT /note="COP9 signalosome complex subunit 8"
FT /id="PRO_0000121015"
FT DOMAIN 20..190
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 197 AA; 22547 MW; D182ABACE4238759 CRC64;
MDLSPVKEAL AAKSFDKIAD ICDTLMLQVA SEGIEYHDDW PYAIHLLGYF YVDDCDSARF
LWKRIPTAIK ERKPEVVAAW GIGQKLWTHD YAGVYEAIRG YDWSQEAKDM VAAFSDLYTK
RMFQLLLSAY STITIHDLAL FLGMTEDDAT TYVVENGWTV DAASQMASVK KQAVKREQKV
DSSKLQRLTE YVFHLEH
