CSN5B_ARATH
ID CSN5B_ARATH Reviewed; 358 AA.
AC Q9FVU9; O82523;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=COP9 signalosome complex subunit 5b;
DE Short=Signalosome subunit 5b;
DE EC=3.4.-.-;
DE AltName: Full=Jun activation domain-binding homolog 2;
GN Name=CSN5B {ECO:0000303|PubMed:23424245};
GN Synonyms=AJH2 {ECO:0000303|PubMed:9811788},
GN CSN5A {ECO:0000303|PubMed:11742986};
GN OrderedLocusNames=At1g71230 {ECO:0000312|Araport:AT1G71230};
GN ORFNames=F3I17.12 {ECO:0000312|EMBL:AAG51882.1};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND SUBUNIT.
RC TISSUE=Seedling;
RX PubMed=9811788; DOI=10.2307/3870903;
RA Kwok S.F., Solano R., Tsuge T., Chamovitz D.A., Ecker J.R., Matsui M.,
RA Deng X.-W.;
RT "Arabidopsis homologs of a c-Jun coactivator are present both in monomeric
RT form and in the COP9 complex, and their abundance is differentially
RT affected by the pleiotropic cop/det/fus mutations.";
RL Plant Cell 10:1779-1790(1998).
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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 [7]
RP INTERACTION WITH CSN4 AND CSN6.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND MUTAGENESIS OF HIS-142;
RP HIS-144; CYS-149; ASP-155 AND ASP-175.
RX PubMed=15486099; DOI=10.1105/tpc.104.025999;
RA Gusmaroli G., Feng S., Deng X.W.;
RT "The Arabidopsis CSN5A and CSN5B subunits are present in distinct COP9
RT signalosome complexes, and mutations in their JAMM domains exhibit
RT differential dominant negative effects on development.";
RL Plant Cell 16:2984-3001(2004).
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 CYT1.
RX PubMed=23424245; DOI=10.1105/tpc.112.106880;
RA Wang J., Yu Y., Zhang Z., Quan R., Zhang H., Ma L., Deng X.W., Huang R.;
RT "Arabidopsis CSN5B interacts with VTC1 and modulates ascorbic acid
RT synthesis.";
RL Plant Cell 25:625-636(2013).
RN [11]
RP INTERACTION WITH FLZ3.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
CC -!- FUNCTION: Probable protease subunit of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes such as photomorphogenesis and auxin and jasmonate responses.
CC The CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of the SCF-type E3 ligase complexes, leading to decrease the
CC Ubl ligase activity of SCF. In the complex, it probably acts as the
CC catalytic center that mediates the cleavage of Nedd8 from cullins. It
CC however has no metalloprotease activity by itself and requires the
CC other subunits of the CSN complex (By similarity). The CSN complex is
CC involved in repression of photomorphogenesis in darkness by regulating
CC the activity of COP1-containing Ubl ligase complexes. The complex is
CC also required for degradation of PSIAA6 by regulating the activity of
CC the Ubl ligase SCF-TIR complex. Not involved in CSN's
CC deneddylation/derubylation activity (PubMed:15486099, PubMed:17307927).
CC Essential for the structural integrity of the CSN holocomplex
CC (PubMed:17307927). {ECO:0000250, ECO:0000269|PubMed:11337587,
CC ECO:0000269|PubMed:15486099, ECO:0000269|PubMed:17307927,
CC ECO:0000269|PubMed:9811788}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
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 CSN8
CC (PubMed:9811788, PubMed:12615944, PubMed:15486099). CSN5A or CSN5B are
CC present within distinct CSN complexes each containing only one copy of
CC CSN5 (PubMed:15486099). Interacts with itself (PubMed:9811788). In the
CC complex, it is located in the center and probably interacts directly
CC with CSN4 and CSN6A or CSN6B (PubMed:9811788, PubMed:12615944). Also
CC exists as monomeric form (PubMed:9811788). Interacts with CYT1 in vitro
CC and in planta (PubMed:23424245). Interacts with FLZ3 (Ref.11).
CC {ECO:0000269|PubMed:12615944, ECO:0000269|PubMed:15486099,
CC ECO:0000269|PubMed:23424245, ECO:0000269|PubMed:9811788,
CC ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC Q9FVU9; Q9ZT84: GA3OX2; NbExp=3; IntAct=EBI-697501, EBI-25512974;
CC Q9FVU9; Q9LYC1: GID1B; NbExp=3; IntAct=EBI-697501, EBI-963686;
CC Q9FVU9; O82255: GRXC13; NbExp=3; IntAct=EBI-697501, EBI-4444060;
CC Q9FVU9; P93830: IAA17; NbExp=3; IntAct=EBI-697501, EBI-632243;
CC Q9FVU9; Q9SZ67: WRKY19; NbExp=3; IntAct=EBI-697501, EBI-2356712;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9811788}. Nucleus
CC {ECO:0000269|PubMed:9811788}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in flowers
CC and roots. Expressed at lower level in seedlings and siliques.
CC {ECO:0000269|PubMed:9811788}.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity of the
CC CSN complex resulting in deneddylation of cullins. It constitutes the
CC catalytic center of the complex (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no effect on the
CC derubylation of CUL1 (PubMed:15486099, PubMed:17307927). Csn5a and
CC csn5b double mutants are lethal at the seedling stage
CC (PubMed:17307927). {ECO:0000269|PubMed:15486099,
CC ECO:0000269|PubMed:17307927}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
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; AF087412; AAC36343.1; -; mRNA.
DR EMBL; AF395061; AAL58104.1; -; mRNA.
DR EMBL; AC016162; AAG51882.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35176.1; -; Genomic_DNA.
DR EMBL; AF411778; AAL06468.1; -; mRNA.
DR EMBL; AY124816; AAM70525.1; -; mRNA.
DR PIR; H96736; H96736.
DR PIR; T52042; T52042.
DR RefSeq; NP_177279.1; NM_105792.2.
DR AlphaFoldDB; Q9FVU9; -.
DR SMR; Q9FVU9; -.
DR BioGRID; 28683; 48.
DR IntAct; Q9FVU9; 64.
DR STRING; 3702.AT1G71230.1; -.
DR MEROPS; M67.A02; -.
DR PaxDb; Q9FVU9; -.
DR PRIDE; Q9FVU9; -.
DR ProteomicsDB; 222703; -.
DR EnsemblPlants; AT1G71230.1; AT1G71230.1; AT1G71230.
DR GeneID; 843463; -.
DR Gramene; AT1G71230.1; AT1G71230.1; AT1G71230.
DR KEGG; ath:AT1G71230; -.
DR Araport; AT1G71230; -.
DR TAIR; locus:2032288; AT1G71230.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_053034_0_2_1; -.
DR InParanoid; Q9FVU9; -.
DR OMA; YSEGYKP; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; Q9FVU9; -.
DR PRO; PR:Q9FVU9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVU9; baseline and differential.
DR Genevisible; Q9FVU9; AT.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019784; F:deNEDDylase activity; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0010387; P:COP9 signalosome assembly; IMP:TAIR.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IGI:TAIR.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:TAIR.
DR GO; GO:0000338; P:protein deneddylation; IGI:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:2000082; P:regulation of L-ascorbic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IGI:TAIR.
DR InterPro; IPR037740; CSN5.
DR InterPro; IPR040961; CSN5_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF33; PTHR10410:SF33; 1.
DR Pfam; PF18323; CSN5_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Developmental protein; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Phytochrome signaling pathway; Protease;
KW Reference proteome; Signalosome; Zinc.
FT CHAIN 1..358
FT /note="COP9 signalosome complex subunit 5b"
FT /id="PRO_0000194842"
FT DOMAIN 59..196
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 338..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..155
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8LAZ7"
FT MUTAGEN 142
FT /note="H->A: No effect on CSN complex integrity and no
FT effect on CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 144
FT /note="H->A: No effect on CSN complex integrity and no
FT effect on CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 149
FT /note="C->A: No effect on CSN complex integrity and no
FT effect on CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 155
FT /note="D->N: No effect on CSN complex integrity and no
FT effect on CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT MUTAGEN 175
FT /note="D->E,N: No effect on CSN complex integrity and no
FT effect on CUL1 derubylation."
FT /evidence="ECO:0000269|PubMed:15486099"
FT CONFLICT 160
FT /note="R -> T (in Ref. 1; AAC36343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40318 MW; 4890F2D35F6FB410 CRC64;
MEGSSSTIAR KTWELENSIL TVDSPDSTSD NIFYYDDTSQ TRFQQEKPWE NDPHYFKRVK
ISALALLKMV VHARSGGTIE IMGLMQGKTD GDTIIVMDAF ALPVEGTETR VNAQDDAYEY
MVEYSQTNKL AGRLENVVGW YHSHPGYGCW LSGIDVSTQR LNQQHQEPFL AVVIDPTRTV
SAGKVEIGAF RTYSKGYKPP DEPVSEYQTI PLNKIEDFGV HCKQYYSLDV TYFKSSLDSH
LLDLLWNKYW VNTLSSSPLL GNGDYVAGQI SDLAEKLEQA ESHLVQSRFG GVVPSSLHKK
KEDESQLTKI TRDSAKITVE QVHGLMSQVI KDELFNSMRQ SNNKSPTDSS DPDPMITY
