ID   CSN3_CAEEL              Reviewed;         501 AA.
AC   Q9N425;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 4.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=COP9 signalosome complex subunit 3;
DE            Short=Signalosome subunit 3;
GN   Name=csn-3; ORFNames=Y38C1AA.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CSN-2 AND CSN-4.
RX   PubMed=12781129; DOI=10.1016/s0960-9822(03)00336-1;
RA   Pintard L., Kurz T., Glaser S., Willis J.H., Peter M., Bowerman B.;
RT   "Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin
RT   for degradation at the meiosis-to-mitosis transition in C. elegans.";
RL   Curr. Biol. 13:911-921(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
CC       embryogenesis and oogenesis and is required to regulate microtubule
CC       stability in the early embryo. Mediates mei-3/katanin targeting for
CC       degradation at the meiosis to mitosis transition via deneddylation of
CC       cul-3. {ECO:0000269|PubMed:12781129}.
CC   -!- SUBUNIT: Component of the CSN complex, probably composed of csn-1, csn-
CC       2, csn-3, csn-4, csn-5, csn-6 and csn-7. Within the complex it probably
CC       interacts directly with csn-2 and csn-4. May interact with itself.
CC       {ECO:0000269|PubMed:12781129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus
CC       {ECO:0000269|PubMed:12781129}.
CC   -!- SIMILARITY: Belongs to the CSN3 family. {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; FO081257; CCD70246.1; -; Genomic_DNA.
DR   RefSeq; NP_499878.3; NM_067477.5.
DR   AlphaFoldDB; Q9N425; -.
DR   SMR; Q9N425; -.
DR   BioGRID; 41997; 17.
DR   ComplexPortal; CPX-3386; COP9 signalosome complex.
DR   IntAct; Q9N425; 2.
DR   STRING; 6239.Y38C1AA.2; -.
DR   EPD; Q9N425; -.
DR   PaxDb; Q9N425; -.
DR   PeptideAtlas; Q9N425; -.
DR   EnsemblMetazoa; Y38C1AA.2.1; Y38C1AA.2.1; WBGene00000815.
DR   GeneID; 176834; -.
DR   KEGG; cel:CELE_Y38C1AA.2; -.
DR   UCSC; Y38C1AA.2; c. elegans.
DR   CTD; 176834; -.
DR   WormBase; Y38C1AA.2; CE33861; WBGene00000815; csn-3.
DR   eggNOG; KOG2582; Eukaryota.
DR   HOGENOM; CLU_562892_0_0_1; -.
DR   InParanoid; Q9N425; -.
DR   OMA; YMLLYLY; -.
DR   OrthoDB; 916528at2759; -.
DR   PhylomeDB; Q9N425; -.
DR   Reactome; R-CEL-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-CEL-8951664; Neddylation.
DR   PRO; PR:Q9N425; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00000815; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0008180; C:COP9 signalosome; IPI:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0060184; P:cell cycle switching; IMP:ComplexPortal.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR   GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IMP:ComplexPortal.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0000338; P:protein deneddylation; IC:ComplexPortal.
DR   GO; GO:1905879; P:regulation of oogenesis; IMP:ComplexPortal.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:WormBase.
DR   InterPro; IPR037753; CSN3.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR10758:SF1; PTHR10758:SF1; 1.
DR   Pfam; PF01399; PCI; 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..501
FT                   /note="COP9 signalosome complex subunit 3"
FT                   /id="PRO_0000120982"
FT   DOMAIN          275..445
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ   SEQUENCE   501 AA;  55884 MW;  0D204CFCF1ACBD61 CRC64;
     MTTFFNKLFT GASSSSSAAA SSGMDLGSME SLCAAINELC SEKHVSENVG ELAAGIVRKN
     KELFEKKSND VEAFLLHCSP NVGSAAMVAA IKGMFDTSAA KNNETGTDRA VELLNHYVDE
     NNFVGGHLKL VPEIIFPLLR DVGLYCLEKK NKPEIGQRII MKALGSMFPR NGSNAPNVLT
     SAHGVLFACA LETKDYASVE PFIDLHVDEI ANENCIQDQE KSDNRERDFG DVFLGRMKKG
     AAFGSQPVAH NPHLHPKYVL DYLYNGACIL IELKRFEDAL FLLEICVGMP AFSVQDQHLD
     SFKKYVLISL ILKGKVDVTE NGDKSAIRHF KTKSPEYKQF SEIRFSRSSN THSAVESLVK
     SAKDRLRKDG NTEIAKYLVV EMKKKTIMSL TRMFTSIRIS EIEELAFLKS RDQVTELIGQ
     LVEEQRITVR IDGDMVFWTE LSPVPSKNDV ENKIRIVDHL NTLLHEKNTT MKAGSGRMRP
     SVMYNEDEGL SMPPTESKFF S