CSN5_DROME
ID CSN5_DROME Reviewed; 327 AA.
AC Q9XZ58; Q7KN57; Q9UB04;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE Short=Dch5;
DE Short=Signalosome subunit 5;
DE EC=3.4.-.-;
DE AltName: Full=JAB1 homolog;
GN Name=CSN5; Synonyms=quo; ORFNames=CG14884;
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 CSN2.
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;
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, SUBUNIT, AND COMPONENT OF THE CSN COMPLEX WITH CSN4 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.
RX PubMed=12397113; DOI=10.1242/dev.129.21.5053;
RA Doronkin S., Djagaeva I., Beckendorf S.K.;
RT "CSN5/Jab1 mutations affect axis formation in the Drosophila oocyte by
RT activating a meiotic checkpoint.";
RL Development 129:5053-5064(2002).
RN [7]
RP FUNCTION, AND MUTANTS CSN5-1; CSN5-2 AND CSN5-3.
RX PubMed=11779478; DOI=10.1016/s0896-6273(01)00576-1;
RA Suh G.S.B., Poeck B., Chouard T., Oron E., Segal D., Chamovitz D.A.,
RA Zipursky S.L.;
RT "Drosophila JAB1/CSN5 acts in photoreceptor cells to induce glial cells.";
RL Neuron 33:35-46(2002).
RN [8]
RP INTERACTION WITH TRC8.
RX PubMed=12032852; DOI=10.1038/sj.onc.1205437;
RA Gemmill R.M., Bemis L.T., Lee J.P., Sozen M.A., Baron A., Zeng C.,
RA Erickson P.F., Hooper J.E., Drabkin H.A.;
RT "The TRC8 hereditary kidney cancer gene suppresses growth and functions
RT with VHL in a common pathway.";
RL Oncogene 21:3507-3516(2002).
RN [9]
RP FUNCTION, ENZYME ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-135; HIS-137
RP AND ASP-148.
RX PubMed=12183637; DOI=10.1126/science.1075901;
RA Cope G.A., Suh G.S.B., Aravind L., Schwarz S.E., Zipursky S.L.,
RA Koonin E.V., Deshaies R.J.;
RT "Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8
RT from Cul1.";
RL Science 298:608-611(2002).
RN [10]
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 [11]
RP MUTAGENESIS OF THR-100.
RX PubMed=15735686; DOI=10.1038/sj.onc.1208509;
RA Gemmill R.M., Lee J.P., Chamovitz D.A., Segal D., Hooper J.E.,
RA Drabkin H.A.;
RT "Growth suppression induced by the TRC8 hereditary kidney cancer gene is
RT dependent upon JAB1/CSN5.";
RL Oncogene 24:3503-3511(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-302 AND THR-303, AND
RP 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: Probable protease subunit of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes. The CSN complex is an essential regulator of the ubiquitin
CC (Ubl) conjugation pathway by mediating the deneddylation of the cullin
CC subunits of the SCF-type E3 ligase complexes, leading to decrease the
CC Ubl ligase activity of SCF. In the complex, it probably acts as the
CC catalytic center that mediates the cleavage of Nedd8 from cullins. It
CC however has no metalloprotease activity by itself and requires the
CC other subunits of the CSN complex. The CSN complex plays an essential
CC role in oogenesis and embryogenesis and is required for proper
CC photoreceptor R cell differentiation and promote lamina glial cell
CC migration or axon targeting. It also promotes Ubl-dependent degradation
CC of cyclin E (CycE) during early oogenesis. Also involved in regulation
CC of axis formation by checkpoint-dependent, translational control of
CC Gurken. {ECO:0000269|PubMed:11779478, ECO:0000269|PubMed:12183637,
CC ECO:0000269|PubMed:12223399, ECO:0000269|PubMed:12397113,
CC ECO:0000269|PubMed:12737805}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:12183637};
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 CSN2. Also exists as monomeric form. Interacts via its MPN domain
CC with Trc8. {ECO:0000269|PubMed:10531038, ECO:0000269|PubMed:12032852,
CC ECO:0000269|PubMed:12223399}.
CC -!- INTERACTION:
CC Q9XZ58; Q9VCY3: CSN6; NbExp=2; IntAct=EBI-97187, EBI-183494;
CC Q9XZ58; Q7KRW1: Trc8; NbExp=3; IntAct=EBI-97187, EBI-1011633;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus
CC {ECO:0000305|PubMed:10531038}.
CC -!- TISSUE SPECIFICITY: Expressed in the optic lobe neuropil.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity of the
CC CSN complex resulting in deneddylation of cullins. It constitutes the
CC catalytic center of the complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27862.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF129083; AAD28608.1; -; mRNA.
DR EMBL; AE014297; AAF55321.1; -; Genomic_DNA.
DR EMBL; AF132563; AAD27862.2; ALT_INIT; mRNA.
DR RefSeq; NP_477442.1; NM_058094.5.
DR AlphaFoldDB; Q9XZ58; -.
DR SMR; Q9XZ58; -.
DR BioGRID; 67045; 18.
DR DIP; DIP-22022N; -.
DR IntAct; Q9XZ58; 6.
DR STRING; 7227.FBpp0082743; -.
DR MEROPS; M67.A13; -.
DR iPTMnet; Q9XZ58; -.
DR PaxDb; Q9XZ58; -.
DR PRIDE; Q9XZ58; -.
DR EnsemblMetazoa; FBtr0083292; FBpp0082743; FBgn0027053.
DR GeneID; 42000; -.
DR KEGG; dme:Dmel_CG14884; -.
DR CTD; 42000; -.
DR FlyBase; FBgn0027053; CSN5.
DR VEuPathDB; VectorBase:FBgn0027053; -.
DR eggNOG; KOG1554; Eukaryota.
DR GeneTree; ENSGT00550000074850; -.
DR HOGENOM; CLU_053034_0_1_1; -.
DR InParanoid; Q9XZ58; -.
DR OMA; ALWNKYW; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; Q9XZ58; -.
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; 42000; 1 hit in 1 CRISPR screen.
DR ChiTaRS; CSN5; fly.
DR GenomeRNAi; 42000; -.
DR PRO; PR:Q9XZ58; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027053; Expressed in cleaving embryo and 25 other tissues.
DR ExpressionAtlas; Q9XZ58; baseline and differential.
DR Genevisible; Q9XZ58; DM.
DR GO; GO:0008180; C:COP9 signalosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:FlyBase.
DR GO; GO:0019784; F:deNEDDylase activity; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140758; F:metal-dependent deNEDDylase activity; IDA:FlyBase.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IMP: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:0048142; P:germarium-derived cystoblast division; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0048140; P:male germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0007275; P:multicellular organism development; IMP:FlyBase.
DR GO; GO:0035207; P:negative regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IMP:FlyBase.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:0000338; P:protein deneddylation; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR InterPro; IPR037740; CSN5.
DR InterPro; IPR040961; CSN5_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF6; PTHR10410:SF6; 1.
DR Pfam; PF18323; CSN5_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Hydrolase;
KW Metal-binding; Metalloprotease; Nucleus; Oogenesis; Phosphoprotein;
KW Protease; Reference proteome; Signalosome; Zinc.
FT CHAIN 1..327
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194841"
FT DOMAIN 52..189
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 135..148
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 100
FT /note="T->I: In csn5-3; disrupts R cell projections.
FT Impairs the interaction with Trc8."
FT /evidence="ECO:0000269|PubMed:15735686"
FT MUTAGEN 135
FT /note="H->A: Abolishes ability to deneddylate cul1."
FT /evidence="ECO:0000269|PubMed:12183637"
FT MUTAGEN 137
FT /note="H->A: Abolishes ability to deneddylate cul1."
FT /evidence="ECO:0000269|PubMed:12183637"
FT MUTAGEN 146
FT /note="G->D: In csn5-2; disrupts R cell projections."
FT MUTAGEN 148
FT /note="D->N: Abolishes ability to deneddylate cul1."
FT /evidence="ECO:0000269|PubMed:12183637"
FT MUTAGEN 160
FT /note="E->V: In csn5-1; disrupts R cell projections."
FT CONFLICT 112
FT /note="E -> K (in Ref. 1; AAD28608)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="E -> K (in Ref. 1; AAD28608)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="D -> N (in Ref. 1; AAD28608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 37083 MW; D0E94ED7ECC0ECF2 CRC64;
MDSDAAQKTW ELENNIQTLP SCDEIFRYDA EQQRQIIDAK PWEKDPHFFK DIKISALALL
KMVMHARSGG TLEVMGLMLG KVEDNTMIVM DAFALPVEGT ETRVNAQAQA YEYMTAYMEA
AKEVGRMEHA VGWYHSHPGY GCWLSGIDVS TQMLNQTYQE PFVAIVVDPV RTVSAGKVCL
GAFRTYPKGY KPPNEEPSEY QTIPLNKIED FGVHCKQYYP LEISYFKSAL DRRLLDSLWN
KYWVNTLGSS GLLTNTEYTT GQIMDLSEKL EQSENFLGRG TDVNEKRSED KLSKATRDCS
RSTIELIHGL MAQIVKDKLF NKVGLGK
