CSN7_ARATH
ID CSN7_ARATH Reviewed; 260 AA.
AC Q94JU3; O81247;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=COP9 signalosome complex subunit 7;
DE Short=CSN complex subunit 7;
DE AltName: Full=Protein FUSCA 5;
GN Name=CSN7; Synonyms=FUS5; OrderedLocusNames=At1g02090;
GN ORFNames=T7I23.24, T7I23.25;
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] (ISOFORM 2), PHOSPHORYLATION, AND SUBUNIT.
RX PubMed=10330469; DOI=10.2307/3870818;
RA Karniol B., Malec P., Chamovitz D.A.;
RT "Arabidopsis FUSCA5 encodes a novel phosphoprotein that is a component of
RT the COP9 complex.";
RL Plant Cell 11:839-848(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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] (ISOFORM 1).
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] (ISOFORM 1).
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 INTERACTION WITH TIF3E1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11029466; DOI=10.1074/jbc.m006721200;
RA Yahalom A., Kim T.-H., Winter E., Karniol B., von Arnim A.G.,
RA Chamovitz D.A.;
RT "Arabidopsis eIF3e (INT-6) associates with both eIF3c and the COP9
RT signalosome subunit CSN7.";
RL J. Biol. Chem. 276:334-340(2001).
RN [8]
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 [9]
RP INTERACTION WITH CSN1; CSN4; CSN6 AND CSN8.
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 [10]
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 [11]
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).
RN [12]
RP FUNCTION, AND INTERACTION WITH TSO2 AND RNR2A.
RX PubMed=21614643; DOI=10.1007/s11103-011-9795-8;
RA Halimi Y., Dessau M., Pollak S., Ast T., Erez T., Livnat-Levanon N.,
RA Karniol B., Hirsch J.A., Chamovitz D.A.;
RT "COP9 signalosome subunit 7 from Arabidopsis interacts with and regulates
RT the small subunit of ribonucleotide reductase (RNR2).";
RL Plant Mol. Biol. 77:77-89(2011).
RN [13]
RP INTERACTION WITH CSN1.
RX PubMed=23818606; DOI=10.1073/pnas.1302418110;
RA Lee J.H., Yi L., Li J., Schweitzer K., Borgmann M., Naumann M., Wu H.;
RT "Crystal structure and versatile functional roles of the COP9 signalosome
RT subunit 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11845-11850(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-169, MUTAGENESIS OF ASP-12;
RP GLU-44; HIS-71; LYS-144 AND GLU-153, INTERACTION WITH CSN1; CSN6A AND CSN8,
RP FUNCTION, AND DOMAIN.
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).
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. Regulates the TSO2
CC subcellular localization. May be involved in nucleic acid binding.
CC {ECO:0000269|PubMed:11337587, ECO:0000269|PubMed:18854373,
CC ECO:0000269|PubMed:21614643}.
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 CSN complex, it probably interacts directly with CSN4.
CC Interacts (via PCI domain) with CSN1 (via PCI domain) and CSN8 (via PCI
CC domain), and (via C-terminal tail) with CSN6A, TSO2 and RNR2A. Cannot
CC interact simultaneously with CSN1 and CSN8 to form ternary complexes.
CC Also exists as a monomeric form. Binds to the translation initiation
CC factors TIF3E1 and TIF3H1 (PubMed:15548739, PubMed:19704582).
CC {ECO:0000269|PubMed:10330469, ECO:0000269|PubMed:11029466,
CC ECO:0000269|PubMed:12615944, ECO:0000269|PubMed:15548739,
CC ECO:0000269|PubMed:18854373, ECO:0000269|PubMed:19704582,
CC ECO:0000269|PubMed:21614643, ECO:0000269|PubMed:23818606}.
CC -!- INTERACTION:
CC Q94JU3; P45432: CSN1; NbExp=3; IntAct=EBI-531152, EBI-530996;
CC Q94JU3; Q8L5U0: CSN4; NbExp=5; IntAct=EBI-531152, EBI-531074;
CC Q94JU3; P43255: CSN8; NbExp=3; IntAct=EBI-531152, EBI-530981;
CC Q94JU3; Q9C5Z3: TIF3E1; NbExp=6; IntAct=EBI-531152, EBI-1635572;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11029466}. Nucleus
CC {ECO:0000269|PubMed:11029466}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CSN7ii;
CC IsoId=Q94JU3-1; Sequence=Displayed;
CC Name=2; Synonyms=CSN7i;
CC IsoId=Q94JU3-2; Sequence=VSP_011914;
CC -!- DOMAIN: The PCI domain is not sufficient to efficiently mediate CSN
CC complex assembly and for biological activity.
CC {ECO:0000269|PubMed:18854373}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10330469}.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF063852; AAC25563.1; -; mRNA.
DR EMBL; AF395065; AAL58108.1; -; mRNA.
DR EMBL; AF395066; AAL58109.1; -; mRNA.
DR EMBL; U89959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE27379.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27380.1; -; Genomic_DNA.
DR EMBL; AF372934; AAK50074.1; -; mRNA.
DR EMBL; AY133518; AAM91348.1; -; mRNA.
DR EMBL; AY087971; AAM65518.1; -; mRNA.
DR PIR; T52188; T52188.
DR RefSeq; NP_563645.1; NM_100089.3. [Q94JU3-1]
DR RefSeq; NP_849576.1; NM_179245.3. [Q94JU3-2]
DR PDB; 3CHM; X-ray; 1.50 A; A=2-169.
DR PDBsum; 3CHM; -.
DR AlphaFoldDB; Q94JU3; -.
DR SMR; Q94JU3; -.
DR BioGRID; 24477; 20.
DR IntAct; Q94JU3; 10.
DR STRING; 3702.AT1G02090.1; -.
DR iPTMnet; Q94JU3; -.
DR PaxDb; Q94JU3; -.
DR PRIDE; Q94JU3; -.
DR ProteomicsDB; 224517; -. [Q94JU3-1]
DR EnsemblPlants; AT1G02090.1; AT1G02090.1; AT1G02090. [Q94JU3-1]
DR EnsemblPlants; AT1G02090.2; AT1G02090.2; AT1G02090. [Q94JU3-2]
DR GeneID; 839241; -.
DR Gramene; AT1G02090.1; AT1G02090.1; AT1G02090. [Q94JU3-1]
DR Gramene; AT1G02090.2; AT1G02090.2; AT1G02090. [Q94JU3-2]
DR KEGG; ath:AT1G02090; -.
DR Araport; AT1G02090; -.
DR TAIR; locus:2205593; AT1G02090.
DR eggNOG; KOG3250; Eukaryota.
DR InParanoid; Q94JU3; -.
DR OMA; GTYKQFR; -.
DR PhylomeDB; Q94JU3; -.
DR EvolutionaryTrace; Q94JU3; -.
DR PRO; PR:Q94JU3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94JU3; baseline and differential.
DR Genevisible; Q94JU3; AT.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Nucleus; Phosphoprotein; Phytochrome signaling pathway; Reference proteome;
KW Signalosome.
FT CHAIN 1..260
FT /note="COP9 signalosome complex subunit 7"
FT /id="PRO_0000121003"
FT DOMAIN 1..159
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 228..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 224..260
FT /note="GDVDIRGNKEMFGEPSGVMDYEEDGIRPKRRRHPVTR -> RE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10330469,
FT ECO:0000303|PubMed:11742986"
FT /id="VSP_011914"
FT MUTAGEN 12
FT /note="D->A: No effect on the interaction with CSN8."
FT /evidence="ECO:0000269|PubMed:18854373"
FT MUTAGEN 44
FT /note="E->A: Decreased interaction with CSN8. Strongly
FT decreased interaction with CSN8; when associated with A-
FT 71."
FT /evidence="ECO:0000269|PubMed:18854373"
FT MUTAGEN 71
FT /note="H->A: Decreased interaction with CSN8. Strongly
FT decreased interaction with CSN8; when associated with A-
FT 44."
FT /evidence="ECO:0000269|PubMed:18854373"
FT MUTAGEN 144
FT /note="K->A: No effect on the interaction with CSN1, but
FT decreased interaction with CSN8."
FT /evidence="ECO:0000269|PubMed:18854373"
FT MUTAGEN 153
FT /note="E->A: No effect on the interactions with CSN1 and
FT CSN8."
FT /evidence="ECO:0000269|PubMed:18854373"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3CHM"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:3CHM"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3CHM"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3CHM"
FT TURN 134..139
FT /evidence="ECO:0007829|PDB:3CHM"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3CHM"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:3CHM"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3CHM"
SQ SEQUENCE 260 AA; 29469 MW; CBBDA06097E44689 CRC64;
MDIEQKQAEI IDQLVKRAST CKSEALGPLI IEATSHPSLF AFSEILALPN VAQLEGTTDS
VYLDLLRLFA HGTWGDYKCN ATRLPHLSPD QILKLKQLTV LTLAESNKVL PYDTLMVELD
VSNVRELEDF LINECMYAGI VRGKLDQLKR CFEVPFAAGR DLRPGQLGNM LHTLSNWLNT
SENLLISIQD KIKWADNMSE MDKKHRKEAE EGVEEVKKSL SMKGDVDIRG NKEMFGEPSG
VMDYEEDGIR PKRRRHPVTR
