CSN7_DROME
ID CSN7_DROME Reviewed; 278 AA.
AC Q9V4S8; Q6NLA1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=COP9 signalosome complex subunit 7;
DE Short=Dch7;
DE Short=Signalosome subunit 7;
GN Name=CSN7; ORFNames=CG2038;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION, SUBCELLULAR LOCATION, PROBABLE COMPOSITION OF THE CSN
RP COMPLEX, AND INTERACTION WITH CSN2 AND CSN4.
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 [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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-235; SER-238 AND
RP SER-249, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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. In the complex, it
CC probably interacts directly with CSN2 and CSN4.
CC {ECO:0000269|PubMed:10531038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus
CC {ECO:0000305|PubMed:10531038}.
CC -!- DOMAIN: The PCI domain is necessary and sufficient for the interactions
CC with other CSN subunits of the complex.
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS93704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF59097.2; -; Genomic_DNA.
DR EMBL; BT012433; AAS93704.1; ALT_FRAME; mRNA.
DR RefSeq; NP_610379.2; NM_136535.3.
DR AlphaFoldDB; Q9V4S8; -.
DR SMR; Q9V4S8; -.
DR BioGRID; 61669; 8.
DR DIP; DIP-22982N; -.
DR IntAct; Q9V4S8; 4.
DR STRING; 7227.FBpp0087821; -.
DR MoonProt; Q9V4S8; -.
DR iPTMnet; Q9V4S8; -.
DR PaxDb; Q9V4S8; -.
DR PRIDE; Q9V4S8; -.
DR DNASU; 35816; -.
DR EnsemblMetazoa; FBtr0088742; FBpp0087821; FBgn0028836.
DR GeneID; 35816; -.
DR KEGG; dme:Dmel_CG2038; -.
DR CTD; 35816; -.
DR FlyBase; FBgn0028836; CSN7.
DR VEuPathDB; VectorBase:FBgn0028836; -.
DR eggNOG; KOG3250; Eukaryota.
DR GeneTree; ENSGT00940000169585; -.
DR HOGENOM; CLU_054426_2_0_1; -.
DR InParanoid; Q9V4S8; -.
DR OMA; GTYKQFR; -.
DR OrthoDB; 1396757at2759; -.
DR PhylomeDB; Q9V4S8; -.
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 SignaLink; Q9V4S8; -.
DR BioGRID-ORCS; 35816; 1 hit in 3 CRISPR screens.
DR ChiTaRS; CSN7; fly.
DR GenomeRNAi; 35816; -.
DR PRO; PR:Q9V4S8; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028836; Expressed in wing disc and 27 other tissues.
DR ExpressionAtlas; Q9V4S8; baseline and differential.
DR Genevisible; Q9V4S8; DM.
DR GO; GO:0008180; C:COP9 signalosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:FlyBase.
DR GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
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 InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR041481; CSN7_helixI.
DR InterPro; IPR027530; Csn7B.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR PANTHER; PTHR15350:SF8; PTHR15350:SF8; 1.
DR Pfam; PF18392; CSN7a_helixI; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Nucleus; Oogenesis;
KW Phosphoprotein; Reference proteome; Signalosome.
FT CHAIN 1..278
FT /note="COP9 signalosome complex subunit 7"
FT /id="PRO_0000121002"
FT DOMAIN 1..167
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 233..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 278 AA; 31068 MW; CAB00E6C0E0A9BA8 CRC64;
MTQDMLLGNE EPSKSKETFL EKFCVLAKSS TGAALLDVIR QALEAPNVFV FGELLAEPSV
LQLKDGPDSK HFETLNLFAY GTYKEYRAQP EKFIELTPAM QKKLQHLTIV SLAIKAKSIP
YALLLSELEI DNVRHLEDII IEAIYADIIH GKLFQNTRIL EVDYAQGRDI PPGYTGQIVE
TLQAWVNSCD SVSNCIEMQI KYANAEKSKR LINKERVEQD LINLKKVLKS QTSDSDESMQ
IDTHGPGTSG GLGQSELRKK PSKLRNPRSA AVGLKFSK
