CSN6B_ARATH
ID CSN6B_ARATH Reviewed; 317 AA.
AC Q8W1P0; O65591; Q8RXW5; Q8W205;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=COP9 signalosome complex subunit 6b {ECO:0000303|PubMed:11701877};
DE Short=AtCSN6b {ECO:0000303|PubMed:11701877};
DE Short=Signalosome subunit 6b {ECO:0000303|PubMed:11701877};
GN Name=CSN6B {ECO:0000303|PubMed:11701877};
GN OrderedLocusNames=At4g26430 {ECO:0000312|Araport:AT4G26430};
GN ORFNames=M3E9.140 {ECO:0000312|EMBL:CAA18227.1};
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].
RX PubMed=11701877; DOI=10.2307/3871583;
RA Peng Z., Serino G., Deng X.-W.;
RT "Molecular characterization of subunit 6 of the COP9 signalosome and its
RT role in multifaceted developmental processes in Arabidopsis.";
RL Plant Cell 13:2393-2407(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11742986; DOI=10.1093/emboj/20.24.7096;
RA Fu H., Reis N., Lee Y., Glickman M.H., Vierstra R.;
RT "Subunit interaction maps for the regulatory particle of the 26S proteasome
RT and the COP9 signalosome.";
RL EMBO J. 20:7096-7107(2001).
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].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP INTERACTION WITH CSN4; CSN5 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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17307927; DOI=10.1105/tpc.106.047571;
RA Gusmaroli G., Figueroa P., Serino G., Deng X.W.;
RT "Role of the MPN subunits in COP9 signalosome assembly and activity, and
RT their regulatory interaction with Arabidopsis Cullin3-based E3 ligases.";
RL Plant Cell 19:564-581(2007).
RN [10]
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 PSIAA6 by regulating the
CC activity of the Ubl ligase SCF-TIR complex. Essential for the
CC structural integrity of the CSN holocomplex (PubMed:17307927).
CC {ECO:0000269|PubMed:11337587, ECO:0000269|PubMed:17307927}.
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. Interacts with itself. In the complex, it probably interacts
CC directly with CSN4, CSN5A or CSN5B, and CSN7. Binds to the translation
CC initiation factors TIF3E1 (PubMed:19704582).
CC {ECO:0000269|PubMed:12615944, ECO:0000269|PubMed:19704582}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions, due to the redundancy with CSN6A. Csn6a and csn6b double
CC mutants are lethal at the seedling stage.
CC {ECO:0000269|PubMed:17307927}.
CC -!- MISCELLANEOUS: Although strongly related to metalloprotease proteins,
CC it lacks the JAMM motif that probably constitutes the catalytic center.
CC Its function as protease is therefore unsure.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18227.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79498.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF434762; AAL49561.1; -; mRNA.
DR EMBL; AF395064; AAL58107.1; -; mRNA.
DR EMBL; AL022223; CAA18227.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79498.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85198.1; -; Genomic_DNA.
DR EMBL; AY080638; AAL85984.1; -; mRNA.
DR EMBL; BT002345; AAN86178.1; -; mRNA.
DR EMBL; AY087556; AAM65098.1; -; mRNA.
DR PIR; T05061; T05061.
DR RefSeq; NP_567746.1; NM_118776.3.
DR AlphaFoldDB; Q8W1P0; -.
DR SMR; Q8W1P0; -.
DR BioGRID; 14036; 4.
DR IntAct; Q8W1P0; 4.
DR STRING; 3702.AT4G26430.1; -.
DR PaxDb; Q8W1P0; -.
DR PRIDE; Q8W1P0; -.
DR ProteomicsDB; 222702; -.
DR EnsemblPlants; AT4G26430.1; AT4G26430.1; AT4G26430.
DR GeneID; 828749; -.
DR Gramene; AT4G26430.1; AT4G26430.1; AT4G26430.
DR KEGG; ath:AT4G26430; -.
DR Araport; AT4G26430; -.
DR TAIR; locus:2131493; AT4G26430.
DR eggNOG; KOG3050; Eukaryota.
DR HOGENOM; CLU_027018_1_2_1; -.
DR InParanoid; Q8W1P0; -.
DR OMA; NTAYDKH; -.
DR OrthoDB; 1455324at2759; -.
DR PhylomeDB; Q8W1P0; -.
DR PRO; PR:Q8W1P0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W1P0; baseline and differential.
DR Genevisible; Q8W1P0; AT.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0010387; P:COP9 signalosome assembly; IMP:TAIR.
DR GO; GO:0000338; P:protein deneddylation; TAS:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR CDD; cd08063; MPN_CSN6; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033859; MPN_CSN6.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Nucleus; Phytochrome signaling pathway;
KW Reference proteome; Signalosome.
FT CHAIN 1..317
FT /note="COP9 signalosome complex subunit 6b"
FT /id="PRO_0000194867"
FT DOMAIN 11..164
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT CONFLICT 208
FT /note="L -> V (in Ref. 1; AAL49561)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="G -> GC (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35404 MW; 9629A50F9EDA2C0E CRC64;
MAPSSSSGLT FKLHPLVMLN ISDHFTRVKT QLNPPAASCA TGNGSNNADA MLLQNPRVYG
CVIGLQRGRT VEIFNSFELI FDPALDTLDR SFLEKKQELY KKVFPDFYVL GWYSTGSDAT
ESDMHIHKAL MDINESPVYV LLNPAINHAQ KDLPVTIYES EFHVIDGIPQ SIFVHTSYTI
ETVEAERISV DHVAHLKPSD GGSAATQLAA HLTGIHSAIK MLNSRIRVLY QHIVAMQKGD
KPCENSVLRQ VSSLLRSLPA AESEKFNENF LMEYNDKLLM SYLAMITNCT SNMNEVVDKF
NTAYDKHSRR GGRTAFM
