CSN3_ARATH
ID CSN3_ARATH Reviewed; 429 AA.
AC Q8W575; Q93VY1; Q9LYA4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=COP9 signalosome complex subunit 3;
DE Short=Signalosome subunit 3;
DE AltName: Full=Protein FUSCA 11;
GN Name=CSN3; Synonyms=FUS11; OrderedLocusNames=At5g14250; ORFNames=F18O22.40;
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 [GENOMIC DNA], FUNCTION, AND COMPONENT OF THE CSN
RP COMPLEX WITH CSN3 AND CSN5.
RX PubMed=11684663; DOI=10.1242/dev.128.21.4277;
RA Peng Z., Serino G., Deng X.-W.;
RT "A role of Arabidopsis COP9 signalosome in multifaceted developmental
RT processes revealed by the characterization of its subunit 3.";
RL Development 128:4277-4288(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE.
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 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; 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).
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, ECO:0000269|PubMed:11684663}.
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 CSN1,
CC CSN4, CSN6 and CSN8. Interacts with COP10.
CC {ECO:0000269|PubMed:11877375, ECO:0000269|PubMed:12615944}.
CC -!- INTERACTION:
CC Q8W575; P45432: CSN1; NbExp=3; IntAct=EBI-531055, EBI-530996;
CC Q8W575; Q8L5U0: CSN4; NbExp=5; IntAct=EBI-531055, EBI-531074;
CC Q8W575; Q8W206: CSN6A; NbExp=3; IntAct=EBI-531055, EBI-531094;
CC Q8W575; P43255: CSN8; NbExp=6; IntAct=EBI-531055, EBI-530981;
CC Q8W575; Q8LGH4: CUL4; NbExp=2; IntAct=EBI-531055, EBI-541750;
CC Q8W575; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-531055, EBI-4424568;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8W575-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the CSN3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87764.1; Type=Erroneous gene model prediction; Evidence={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; AF361759; AAK61872.1; -; Genomic_DNA.
DR EMBL; AF361760; AAK61873.1; -; mRNA.
DR EMBL; AF395059; AAL58102.1; -; mRNA.
DR EMBL; AL163817; CAB87764.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92005.1; -; Genomic_DNA.
DR EMBL; AF419585; AAL31917.1; -; mRNA.
DR EMBL; AY113041; AAM47349.1; -; mRNA.
DR EMBL; AY084910; AAM61473.1; -; mRNA.
DR PIR; T48598; T48598.
DR RefSeq; NP_568296.1; NM_121429.5. [Q8W575-1]
DR AlphaFoldDB; Q8W575; -.
DR SMR; Q8W575; -.
DR BioGRID; 16552; 15.
DR IntAct; Q8W575; 13.
DR STRING; 3702.AT5G14250.1; -.
DR PaxDb; Q8W575; -.
DR PRIDE; Q8W575; -.
DR ProteomicsDB; 222701; -. [Q8W575-1]
DR DNASU; 831275; -.
DR EnsemblPlants; AT5G14250.1; AT5G14250.1; AT5G14250. [Q8W575-1]
DR GeneID; 831275; -.
DR Gramene; AT5G14250.1; AT5G14250.1; AT5G14250. [Q8W575-1]
DR KEGG; ath:AT5G14250; -.
DR Araport; AT5G14250; -.
DR TAIR; locus:2145638; AT5G14250.
DR eggNOG; KOG2582; Eukaryota.
DR HOGENOM; CLU_028825_0_1_1; -.
DR InParanoid; Q8W575; -.
DR OMA; NHYHDLV; -.
DR PhylomeDB; Q8W575; -.
DR PRO; PR:Q8W575; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W575; baseline and differential.
DR Genevisible; Q8W575; AT.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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 Alternative splicing; Cytoplasm; Developmental protein; Nucleus;
KW Phytochrome signaling pathway; Reference proteome; Signalosome.
FT CHAIN 1..429
FT /note="COP9 signalosome complex subunit 3"
FT /id="PRO_0000120984"
FT DOMAIN 196..365
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT CONFLICT 149..150
FT /note="DV -> EF (in Ref. 5; AAL31917/AAM47349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 47741 MW; 77AD165F559BCE12 CRC64;
MIGAVNSVEA VITSIQGLSG SPEDLSALHD LLRGAQDSLR AEPGVNFSTL DQLDASKHSL
GYLYFLEVLT CGPVSKEKAA YEIPIIARFI NSCDAGQIRL ASYKFVSLCK ILKDHVIALG
DPLRGVGPLL NAVQKLQVSS KRLTALHPDV LQLCLQAKSY KSGFSILSDD IVEIDQPRDF
FLYSYYGGMI CIGLKRFQKA LELLYNVVTA PMHQVNAIAL EAYKKYILVS LIHNGQFTNT
LPKCASTAAQ RSFKNYTGPY IELGNCYNDG KIGELEALVV ARNAEFEEDK NLGLVKQAVS
SLYKRNILRL TQKYLTLSLQ DIANMVQLGN AKEAEMHVLQ MIQDGQIHAL INQKDGMVRF
LEDPEQYKSS EMIEIMDSVI QRTIGLSKNL LAMDESLSCD PLYLGKVGRE RQRYDFGDDF
DTVPQKFSM
