CSN3_DROME
ID CSN3_DROME Reviewed; 445 AA.
AC Q8SYG2; Q9VPA3; Q9XYW4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=COP9 signalosome complex subunit 3;
DE Short=Dch3;
DE Short=Signalosome subunit 3;
GN Name=CSN3; ORFNames=CG18332;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE, SUBCELLULAR LOCATION, AND PROBABLE COMPOSITION OF THE
RP CSN COMPLEX.
RX PubMed=10531038; DOI=10.1016/s0960-9822(00)80023-8;
RA Freilich S., Oron E., Kapp Y., Nevo-Caspi Y., Orgad S., Segal D.,
RA Chamovitz D.A.;
RT "The COP9 signalosome is essential for development of Drosophila
RT melanogaster.";
RL Curr. Biol. 9:1187-1190(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION OF CSN COMPLEX.
RX PubMed=12737805; DOI=10.1016/s1534-5807(03)00121-7;
RA Doronkin S., Djagaeva I., Beckendorf S.K.;
RT "The COP9 signalosome promotes degradation of Cyclin E during early
RT Drosophila oogenesis.";
RL Dev. Cell 4:699-710(2003).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes. The CSN
CC complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC pathway by mediating the deneddylation of the cullin subunits of the
CC SCF-type E3 ligase complexes, leading to decrease the Ubl ligase
CC activity of SCF. The CSN complex plays an essential role in oogenesis
CC and embryogenesis and is required for proper photoreceptor R cell
CC differentiation and promote lamina glial cell migration or axon
CC targeting. It also promotes Ubl-dependent degradation of cyclin E
CC (CycE) during early oogenesis. {ECO:0000269|PubMed:12737805}.
CC -!- SUBUNIT: Component of the CSN complex, probably composed of CSN1b,
CC alien/CSN2, CSN3, CSN4, CSN5, CSN6, CSN7 and CSN8.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus
CC {ECO:0000305|PubMed:10531038}.
CC -!- SIMILARITY: Belongs to the CSN3 family. {ECO:0000305}.
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DR EMBL; AF129081; AAD28606.1; -; mRNA.
DR EMBL; AE014296; AAF51652.1; -; Genomic_DNA.
DR EMBL; AY071575; AAL49197.1; -; mRNA.
DR RefSeq; NP_524190.2; NM_079466.3.
DR AlphaFoldDB; Q8SYG2; -.
DR SMR; Q8SYG2; -.
DR BioGRID; 65565; 18.
DR IntAct; Q8SYG2; 9.
DR STRING; 7227.FBpp0077927; -.
DR PaxDb; Q8SYG2; -.
DR PRIDE; Q8SYG2; -.
DR EnsemblMetazoa; FBtr0078269; FBpp0077927; FBgn0027055.
DR GeneID; 40308; -.
DR KEGG; dme:Dmel_CG18332; -.
DR CTD; 1448; -.
DR FlyBase; FBgn0027055; CSN3.
DR VEuPathDB; VectorBase:FBgn0027055; -.
DR eggNOG; KOG2582; Eukaryota.
DR GeneTree; ENSGT00940000153653; -.
DR HOGENOM; CLU_028825_0_1_1; -.
DR InParanoid; Q8SYG2; -.
DR OMA; NHYHDLV; -.
DR OrthoDB; 929822at2759; -.
DR PhylomeDB; Q8SYG2; -.
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8951664; Neddylation.
DR BioGRID-ORCS; 40308; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40308; -.
DR PRO; PR:Q8SYG2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0027055; Expressed in embryonic/larval hemocyte (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q8SYG2; baseline and differential.
DR Genevisible; Q8SYG2; DM.
DR GO; GO:0008180; C:COP9 signalosome; ISS:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0048142; P:germarium-derived cystoblast division; IMP:FlyBase.
DR GO; GO:0048140; P:male germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0000338; P:protein deneddylation; ISS:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR037753; CSN3.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF1; PTHR10758:SF1; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Differentiation; Nucleus; Oogenesis;
KW Reference proteome; Signalosome.
FT CHAIN 1..445
FT /note="COP9 signalosome complex subunit 3"
FT /id="PRO_0000120983"
FT DOMAIN 217..381
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 104
FT /note="E -> K (in Ref. 1; AAD28606)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="V -> A (in Ref. 1; AAD28606)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="H -> Y (in Ref. 1; AAD28606)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="Q -> H (in Ref. 4; AAL49197)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="D -> E (in Ref. 1; AAD28606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50703 MW; 95CDFDA27C5B1171 CRC64;
MGSALENYVN QVRTLSASGS YRELAEELPE SLSLLARNWS ILDNVLETLD MQQHSLGVLY
VLLAKLHSAS TANPEPVQLI QLMRDFVQRN NNEQLRYAVC AFYETCHLFT EFVVQKNLSI
LGIRIISRAI DQIRQLETQL TPIHADLCLL SLKAKNFSVV LPYLDADITD ISTVAAECKT
QQQQQSQHAD ANNDAKYFLL YFYYGGMIYT AVKNYERALY FFEVCITTPA MAMSHIMLEA
YKKFLMVSLI VEGKIAYIPK NTQVIGRFMK PMANHYHDLV NVYANSSSEE LRIIILKYSE
AFTRDNNMGL AKQVATSLYK RNIQRLTKTF LTLSLSDVAS RVQLASAVEA ERYILNMIKS
GEIYASINQK DGMVLFKDDP EKYNSPEMFL NVQNNITHVL DQVRQINKME EEIILNPMYV
KKALGSQDDD LTSQHPKTFS GDPTD
