CSN2_DROME
ID CSN2_DROME Reviewed; 444 AA.
AC Q94899; A4V0G9; Q8MSX8; Q9V3Z0;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=COP9 signalosome complex subunit 2;
DE Short=Dch2;
DE Short=Signalosome subunit 2;
DE AltName: Full=Alien protein;
GN Name=alien {ECO:0000312|FlyBase:FBgn0013746};
GN Synonyms=CSN2 {ECO:0000303|PubMed:12426099}; ORFNames=CG9556;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
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] {ECO:0000312|EMBL:AAN10685.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAN10685.1}
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] {ECO:0000312|EMBL:AAL39981.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-363, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:8817453};
RX PubMed=8817453; DOI=10.1016/0925-4773(96)00532-1;
RA Goubeaud A., Knirr S., Renkawitz-Pohl R., Paululat A.;
RT "The Drosophila gene alien is expressed in the muscle attachment sites
RT during embryogenesis and encodes a protein highly conserved between plants,
RT Drosophila and vertebrates.";
RL Mech. Dev. 57:59-68(1996).
RN [6] {ECO:0000305}
RP INTERACTION WITH RPN6.
RX PubMed=12426099; DOI=10.1016/s0378-1119(02)00930-7;
RA Lier S., Paululat A.;
RT "The proteasome regulatory particle subunit Rpn6 is required for Drosophila
RT development and interacts physically with signalosome subunit Alien/CSN2.";
RL Gene 298:109-119(2002).
RN [7] {ECO:0000305}
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:0000250|UniProtKB:Q15647,
CC ECO:0000269|PubMed:10531038, 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 with Rpn6.
CC {ECO:0000269|PubMed:12426099}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus
CC {ECO:0000305|PubMed:10531038}.
CC -!- TISSUE SPECIFICITY: Expressed during embryonic stages 11-14 in the
CC muscle attachment sites (apodemes); pharynx attachment to the roof of
CC the mouth and in the epidermis of the head for the dorsal and ventral
CC prothoracic pharyngeal muscle attachment. From stage 16 onwards
CC expression is seen in all thoracic and abdominal apodemes.
CC {ECO:0000269|PubMed:8817453}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally with high levels during
CC oogenesis, and zygotically. {ECO:0000269|PubMed:8817453}.
CC -!- SIMILARITY: Belongs to the CSN2 family. {ECO:0000269|PubMed:12737805}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB49932.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM49874.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF129079; AAD28604.1; -; mRNA.
DR EMBL; AE014134; AAF52736.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10685.1; -; Genomic_DNA.
DR EMBL; AY069836; AAL39981.1; -; mRNA.
DR EMBL; AY118505; AAM49874.1; ALT_INIT; mRNA.
DR EMBL; U57758; AAB49932.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001260276.1; NM_001273347.1.
DR RefSeq; NP_001285771.1; NM_001298842.1.
DR RefSeq; NP_523517.1; NM_078793.6.
DR RefSeq; NP_723438.1; NM_164843.3.
DR AlphaFoldDB; Q94899; -.
DR SMR; Q94899; -.
DR BioGRID; 60337; 16.
DR DIP; DIP-19507N; -.
DR IntAct; Q94899; 3.
DR STRING; 7227.FBpp0303869; -.
DR PaxDb; Q94899; -.
DR PRIDE; Q94899; -.
DR DNASU; 34225; -.
DR EnsemblMetazoa; FBtr0079780; FBpp0079381; FBgn0013746.
DR EnsemblMetazoa; FBtr0079781; FBpp0089195; FBgn0013746.
DR EnsemblMetazoa; FBtr0339550; FBpp0308633; FBgn0013746.
DR EnsemblMetazoa; FBtr0343095; FBpp0309805; FBgn0013746.
DR GeneID; 34225; -.
DR KEGG; dme:Dmel_CG9556; -.
DR CTD; 34225; -.
DR FlyBase; FBgn0013746; alien.
DR VEuPathDB; VectorBase:FBgn0013746; -.
DR eggNOG; KOG1464; Eukaryota.
DR GeneTree; ENSGT00530000063301; -.
DR HOGENOM; CLU_028981_0_1_1; -.
DR InParanoid; Q94899; -.
DR OMA; EEQYDFE; -.
DR OrthoDB; 1108845at2759; -.
DR PhylomeDB; Q94899; -.
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 BioGRID-ORCS; 34225; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34225; -.
DR PRO; PR:Q94899; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0013746; Expressed in cleaving embryo and 34 other tissues.
DR ExpressionAtlas; Q94899; baseline and differential.
DR Genevisible; Q94899; DM.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0008231; C:repressor ecdysone receptor complex; IPI:FlyBase.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:FlyBase.
DR GO; GO:0007562; P:eclosion; IMP:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0000338; P:protein deneddylation; ISS:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR InterPro; IPR037750; COPS2.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10678:SF3; PTHR10678:SF3; 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..444
FT /note="COP9 signalosome complex subunit 2"
FT /id="PRO_0000120974"
FT DOMAIN 255..417
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 51527 MW; 3E471578DD495B57 CRC64;
MSDNDDDFMC DDDEDYGLEY SEDSNSEPDV DLENQYYNSK ALKEEEPKAA LASFQKVLDL
ENGEKGEWGF KALKQMIKIN FRLCNYDEMM VRYKQLLTYI KSAVTRNHSE KSINSILDYI
STSKNMALLQ NFYETTLDAL RDAKNDRLWF KTNTKLGKLY FDRSDFTKLQ KILKQLHQSC
QTDDGEDDLK KGTQLLEIYA LEIQMYTVQK NNKKLKALYE QSLHIKSAIP HPLIMGVIRE
CGGKMHLREG EFEKAHTDFF EAFKNYDESG SPRRTTCLKY LVLANMLMKS GINPFDSQEA
KPYKNDPEIL AMTNLVNSYQ NNDINEFETI LRQHRSNIMA DQFIREHIED LLRNIRTQVL
IKLIRPYKNI AIPFIANALN IEPAEVESLL VSCILDDTIK GRIDQVNQVL QLDKINSSAS
RYNALEKWSN QIQSLQFAVV QKMA
