CSN6_DROME
ID CSN6_DROME Reviewed; 341 AA.
AC Q9VCY3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=COP9 signalosome complex subunit 6;
DE Short=Dch6;
DE Short=Signalosome subunit 6;
GN Name=CSN6; ORFNames=CG6932;
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=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 [4]
RP IDENTIFICATION, SUBCELLULAR LOCATION, AND PROBABLE COMPOSITION OF THE CSN
RP 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 [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 -!- INTERACTION:
CC Q9VCY3; Q9V345: CSN4; NbExp=3; IntAct=EBI-183494, EBI-141466;
CC Q9VCY3; Q9XZ58: CSN5; NbExp=2; IntAct=EBI-183494, EBI-97187;
CC Q9VCY3; Q9VCY3: CSN6; NbExp=2; IntAct=EBI-183494, EBI-183494;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus
CC {ECO:0000305|PubMed:10531038}.
CC -!- MISCELLANEOUS: Although strongly related to metalloprotease proteins,
CC it lacks the JAMM motif that probably constitutes the catalytic center.
CC Its function as protease is therefore unsure.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF56022.1; -; Genomic_DNA.
DR EMBL; AY070607; AAL48078.1; -; mRNA.
DR RefSeq; NP_524451.1; NM_079727.3.
DR PDB; 4E0Q; X-ray; 2.50 A; A/B=51-187.
DR PDBsum; 4E0Q; -.
DR AlphaFoldDB; Q9VCY3; -.
DR SMR; Q9VCY3; -.
DR BioGRID; 67615; 7.
DR IntAct; Q9VCY3; 3.
DR MINT; Q9VCY3; -.
DR STRING; 7227.FBpp0083658; -.
DR MEROPS; M67.972; -.
DR PaxDb; Q9VCY3; -.
DR PRIDE; Q9VCY3; -.
DR DNASU; 42661; -.
DR EnsemblMetazoa; FBtr0084265; FBpp0083658; FBgn0028837.
DR GeneID; 42661; -.
DR KEGG; dme:Dmel_CG6932; -.
DR CTD; 42661; -.
DR FlyBase; FBgn0028837; CSN6.
DR VEuPathDB; VectorBase:FBgn0028837; -.
DR eggNOG; KOG3050; Eukaryota.
DR GeneTree; ENSGT00950000183073; -.
DR HOGENOM; CLU_027018_1_2_1; -.
DR InParanoid; Q9VCY3; -.
DR OMA; DLVGWYT; -.
DR OrthoDB; 1455324at2759; -.
DR PhylomeDB; Q9VCY3; -.
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; Q9VCY3; -.
DR BioGRID-ORCS; 42661; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42661; -.
DR PRO; PR:Q9VCY3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0028837; Expressed in embryonic/larval hemocyte (Drosophila) and 35 other tissues.
DR Genevisible; Q9VCY3; DM.
DR GO; GO:0008180; C:COP9 signalosome; ISS:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0000338; P:protein deneddylation; ISS:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR CDD; cd08063; MPN_CSN6; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033859; MPN_CSN6.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW Oogenesis; Reference proteome; Signalosome.
FT CHAIN 1..341
FT /note="COP9 signalosome complex subunit 6"
FT /id="PRO_0000194864"
FT DOMAIN 54..188
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4E0Q"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:4E0Q"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:4E0Q"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:4E0Q"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4E0Q"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:4E0Q"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:4E0Q"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4E0Q"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:4E0Q"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:4E0Q"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:4E0Q"
SQ SEQUENCE 341 AA; 38306 MW; CA9C05F03593C47A CRC64;
MEQMEVDVDM SAKPSTSSSA AAGSSMAVDK TADQNPQPQG NIMAAAGTSG SVTISLHPLV
IMNISEHWTR FRAQHGEPRQ VYGALIGKQK GRNIEIMNSF ELKTDVIGDE TVINKDYYNK
KEQQYKQVFS DLDFIGWYTT GDNPTADDIK IQRQIAAINE CPIMLQLNPL SRSVDHLPLK
LFESLIDLVD GEATMLFVPL TYTLATEEAE RIGVDHVARM TSNESGEKSV VAEHLVAQDS
AIKMLNTRIK IVLQYIRDVE AGKLRANQEI LREAYALCHR LPVMQVPAFQ EEFYTQCNDV
GLISYLGTLT KGCNDMHHFV NKFNMLYDRQ GSARRMRGLY Y
