CSN4_DROME
ID CSN4_DROME Reviewed; 407 AA.
AC Q9V345; Q9XYW5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=COP9 signalosome complex subunit 4;
DE Short=Dch4;
DE Short=Signalosome subunit 4;
GN Name=CSN4; ORFNames=CG8725;
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 [MRNA], SUBCELLULAR LOCATION, PROBABLE COMPOSITION OF
RP THE CSN COMPLEX, AND INTERACTION WITH CSN7.
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=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND COMPONENT OF THE CSN COMPLEX WITH CSN5 AND CSN7.
RX PubMed=12223399; DOI=10.1242/dev.129.19.4399;
RA Oron E., Mannervik M., Rencus S., Harari-Steinberg O.,
RA Neuman-Silberberg S., Segal D., Chamovitz D.A.;
RT "COP9 signalosome subunits 4 and 5 regulate multiple pleiotropic pathways
RT in Drosophila melanogaster.";
RL Development 129:4399-4409(2002).
RN [6]
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:12223399,
CC 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. Interacts directly
CC with CSN7. {ECO:0000269|PubMed:10531038}.
CC -!- INTERACTION:
CC Q9V345; P22745: bam; NbExp=5; IntAct=EBI-141466, EBI-88504;
CC Q9V345; Q9VCY3: CSN6; NbExp=3; IntAct=EBI-141466, EBI-183494;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus
CC {ECO:0000305|PubMed:10531038}.
CC -!- SIMILARITY: Belongs to the CSN4 family. {ECO:0000305}.
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DR EMBL; AF129082; AAD28607.1; -; mRNA.
DR EMBL; AE013599; AAF59157.1; -; Genomic_DNA.
DR EMBL; BT004883; AAO45239.1; -; mRNA.
DR RefSeq; NP_001163080.1; NM_001169609.2.
DR RefSeq; NP_477444.1; NM_058096.4.
DR AlphaFoldDB; Q9V345; -.
DR SMR; Q9V345; -.
DR BioGRID; 61621; 35.
DR DIP; DIP-52178N; -.
DR IntAct; Q9V345; 12.
DR STRING; 7227.FBpp0087935; -.
DR PaxDb; Q9V345; -.
DR PRIDE; Q9V345; -.
DR DNASU; 35759; -.
DR EnsemblMetazoa; FBtr0088859; FBpp0087935; FBgn0027054.
DR EnsemblMetazoa; FBtr0301230; FBpp0290448; FBgn0027054.
DR GeneID; 35759; -.
DR KEGG; dme:Dmel_CG8725; -.
DR CTD; 35759; -.
DR FlyBase; FBgn0027054; CSN4.
DR VEuPathDB; VectorBase:FBgn0027054; -.
DR eggNOG; KOG1497; Eukaryota.
DR GeneTree; ENSGT00940000153510; -.
DR HOGENOM; CLU_028132_1_0_1; -.
DR InParanoid; Q9V345; -.
DR OMA; KNIMHTV; -.
DR OrthoDB; 866823at2759; -.
DR PhylomeDB; Q9V345; -.
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 Reactome; R-DME-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q9V345; -.
DR BioGRID-ORCS; 35759; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 35759; -.
DR PRO; PR:Q9V345; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0027054; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; Q9V345; baseline and differential.
DR Genevisible; Q9V345; DM.
DR GO; GO:0008180; C:COP9 signalosome; IPI:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
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:0048140; P:male germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0000338; P:protein deneddylation; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR037754; CSN4.
DR InterPro; IPR041406; CSN4_HTH.
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 PANTHER; PTHR10855:SF2; PTHR10855:SF2; 1.
DR Pfam; PF18420; CSN4_RPN5_eIF3a; 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 Cytoplasm; Developmental protein; Differentiation; Nucleus; Oogenesis;
KW Reference proteome; Signalosome.
FT CHAIN 1..407
FT /note="COP9 signalosome complex subunit 4"
FT /id="PRO_0000120992"
FT DOMAIN 204..373
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT CONFLICT 16
FT /note="L -> Q (in Ref. 1; AAD28607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46473 MW; BB7B552ABC8848F0 CRC64;
MAANYGISTA ALRSQLMGLI NFTGTHKDQA DKYRQLLKTV LTNTGQELID GLRLFVEAIV
NEHVSLVISR QILNDVGSEL SKLPDDLSKM LSHFTLEKVN PRVISFEEQV AGIRFHLANI
YERNQQWRDA ATVLVGIPLE TGQKQYSVEC KLGTYLKIAR LYLEDNDSVQ AELFINRASL
LQAETNSEEL QVLYKVCYAR VLDYRRKFIE AAQRYNELSY RKIVDQGERM TALKKALICT
VLASAGQQRS RMLATLFKDE RCQHLPAYGI LEKMYLERII RRSELQEFEA LLQDHQKAAT
SDGSSILDRA VFEHNLLSAS KLYNNITFEE LGALLDIPAV KAEKIASQMI TEGRMNGHID
QISAIVHFEN RELLPQWDRQ IQSLCYQVNS IIEKISVAEP DWMDNLN
