CSN4_ARATH
ID CSN4_ARATH Reviewed; 397 AA.
AC Q8L5U0; Q9FMM1; Q9SW74;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=COP9 signalosome complex subunit 4;
DE Short=AtS4;
DE Short=Signalosome subunit 4;
DE AltName: Full=Constitutive photomorphogenesis protein 8;
DE AltName: Full=Protein FUSCA 4;
GN Name=CSN4; Synonyms=COP8, FUS4; OrderedLocusNames=At5g42970;
GN ORFNames=MBD2.17;
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, FUNCTION, INTERACTION WITH CSN1; CSN5B; CSN7 AND CSN8,
RP AND MUTANT FUS4-414.
RC STRAIN=cv. Columbia;
RX PubMed=10521526; DOI=10.2307/3871091;
RA Serino G., Tsuge T., Kwok S., Matsui M., Wei N., Deng X.-W.;
RT "Arabidopsis cop8 and fus4 mutations define the same gene that encodes
RT subunit 4 of the COP9 signalosome.";
RL Plant Cell 11:1967-1980(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND INTERACTION WITH CSN3; CSN5B AND CSN7.
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (SEP-2004) 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 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 [9]
RP INTERACTION WITH CSN1; CSN2; CSN3; CSN4; CSN5; CSN6; CSN7 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 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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:10521526, 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. Interacts with itself. In the complex, it is located in the
CC center and probably interacts directly with CSN1, CSN2, CSN3, CSN4,
CC CSN5A or CSN5B, CSN6A or CSN6B, CSN7 and CSN8. Interacts with COP10.
CC Binds to the translation initiation factors TIF3E1 (PubMed:19704582).
CC {ECO:0000269|PubMed:10521526, ECO:0000269|PubMed:11742986,
CC ECO:0000269|PubMed:11877375, ECO:0000269|PubMed:12615944,
CC ECO:0000269|PubMed:19704582}.
CC -!- INTERACTION:
CC Q8L5U0; P45432: CSN1; NbExp=3; IntAct=EBI-531074, EBI-530996;
CC Q8L5U0; Q8W575: CSN3; NbExp=5; IntAct=EBI-531074, EBI-531055;
CC Q8L5U0; Q94JU3: CSN7; NbExp=5; IntAct=EBI-531074, EBI-531152;
CC Q8L5U0; P43255: CSN8; NbExp=3; IntAct=EBI-531074, EBI-530981;
CC Q8L5U0; Q8LGH4: CUL4; NbExp=2; IntAct=EBI-531074, EBI-541750;
CC Q8L5U0; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-531074, EBI-15193683;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CSN4 family. {ECO:0000305}.
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DR EMBL; AF176089; AAD51742.1; -; mRNA.
DR EMBL; AF395060; AAL58103.1; -; mRNA.
DR EMBL; AB008264; BAB09199.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94896.1; -; Genomic_DNA.
DR EMBL; AY087068; AAM64629.1; -; mRNA.
DR EMBL; AK176360; BAD44123.1; -; mRNA.
DR PIR; T52302; T52302.
DR RefSeq; NP_199111.1; NM_123663.3.
DR AlphaFoldDB; Q8L5U0; -.
DR SMR; Q8L5U0; -.
DR BioGRID; 19562; 25.
DR IntAct; Q8L5U0; 13.
DR STRING; 3702.AT5G42970.1; -.
DR iPTMnet; Q8L5U0; -.
DR PaxDb; Q8L5U0; -.
DR PRIDE; Q8L5U0; -.
DR ProteomicsDB; 222621; -.
DR EnsemblPlants; AT5G42970.1; AT5G42970.1; AT5G42970.
DR GeneID; 834312; -.
DR Gramene; AT5G42970.1; AT5G42970.1; AT5G42970.
DR KEGG; ath:AT5G42970; -.
DR Araport; AT5G42970; -.
DR TAIR; locus:2159961; AT5G42970.
DR eggNOG; KOG1497; Eukaryota.
DR HOGENOM; CLU_028132_1_0_1; -.
DR InParanoid; Q8L5U0; -.
DR OMA; KNIMHTV; -.
DR OrthoDB; 866823at2759; -.
DR PhylomeDB; Q8L5U0; -.
DR PRO; PR:Q8L5U0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L5U0; baseline and differential.
DR Genevisible; Q8L5U0; AT.
DR GO; GO:0008180; C:COP9 signalosome; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:TAIR.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; 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 Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040134; PSMD12/CSN4.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10855; PTHR10855; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Developmental protein; Nucleus;
KW Phytochrome signaling pathway; Reference proteome; Signalosome.
FT CHAIN 1..397
FT /note="COP9 signalosome complex subunit 4"
FT /id="PRO_0000120993"
FT DOMAIN 197..365
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 251..265
FT /note="Missing: In fu4-414; induces seedlings defects and
FT lethality after the seedling stage."
FT CONFLICT 244
FT /note="V -> F (in Ref. 5; AAM64629)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="M -> V (in Ref. 1; AAD51742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44957 MW; 1E8AEF28C35B28F0 CRC64;
MDEALTNASA IGDQRQKIEQ YKLILSSVLS SNDLLQAQRF IDHILSDDVP LVVSRQLLQS
FAQELGRLEP ETQKEIAQFT LTQIQPRVVS FEEQALVIRE KLAGLYESEQ EWSKAAQMLS
GIDLDSGMRA VDDNFKLSKC IQIARLYLED DDAVNAEAFI NKASFLVSNS QNEVLNLQYK
VCYARILDMK RKFLEAALRY YGISQIEQRQ IGDEEIDENA LEQALSAAVT CTILAGAGPQ
RSRVLATLYK DERCSKLKIY PILQKVYLER ILRRPEIDAF SEELRPHQKA SLPDKSTVLD
RAMIEHNLLS ASKLYTNIRF DELGTLLAID PRKAEKIAAN MIGQDRMRGS IDQEEAVIHF
EDDVEELQQW DQQISGLCQA LNDILDGMAK KGMSVPV
