ID   CSN1_CAEEL              Reviewed;         601 AA.
AC   Q9GS00;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=COP9 signalosome complex subunit 1;
DE            Short=Signalosome subunit 1;
GN   Name=csn-1; ORFNames=Y59A8A.1;
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; CSN-4; CSN-5
RP   AND RBX-1.
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: Essential component of the COP9 signalosome complex (CSN), a
CC       complex involved in various cellular and developmental processes. The
CC       CSN complex is an essential regulator of the ubiquitin (Ubl)
CC       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. 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, csn-4 and csn-5. May interact with
CC       itself. Interacts with rbx-1. {ECO:0000269|PubMed:12781129}.
CC   -!- INTERACTION:
CC       Q9GS00; O01422: csn-2; NbExp=4; IntAct=EBI-331408, EBI-331413;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus
CC       {ECO:0000269|PubMed:12781129}.
CC   -!- SIMILARITY: Belongs to the CSN1 family. {ECO:0000305}.
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DR   EMBL; AL132895; CAC14399.1; -; Genomic_DNA.
DR   RefSeq; NP_507507.1; NM_075106.4.
DR   AlphaFoldDB; Q9GS00; -.
DR   SMR; Q9GS00; -.
DR   BioGRID; 45146; 23.
DR   ComplexPortal; CPX-3386; COP9 signalosome complex.
DR   DIP; DIP-26112N; -.
DR   IntAct; Q9GS00; 6.
DR   STRING; 6239.Y59A8A.1; -.
DR   iPTMnet; Q9GS00; -.
DR   EPD; Q9GS00; -.
DR   PaxDb; Q9GS00; -.
DR   PeptideAtlas; Q9GS00; -.
DR   PRIDE; Q9GS00; -.
DR   EnsemblMetazoa; Y59A8A.1.1; Y59A8A.1.1; WBGene00000813.
DR   GeneID; 180168; -.
DR   UCSC; Y59A8A.1; c. elegans.
DR   CTD; 180168; -.
DR   WormBase; Y59A8A.1; CE26200; WBGene00000813; csn-1.
DR   eggNOG; KOG0686; Eukaryota.
DR   GeneTree; ENSGT00510000046608; -.
DR   HOGENOM; CLU_444991_0_0_1; -.
DR   InParanoid; Q9GS00; -.
DR   OMA; GIRDYCT; -.
DR   OrthoDB; 859626at2759; -.
DR   PhylomeDB; Q9GS00; -.
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:Q9GS00; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000813; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0008180; C:COP9 signalosome; IPI:ComplexPortal.
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: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   InterPro; IPR033008; CSN1.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR019585; Rpn7/CSN1.
DR   InterPro; IPR045135; Rpn7_N.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR14145; PTHR14145; 1.
DR   PANTHER; PTHR14145:SF2; PTHR14145:SF2; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF10602; RPN7; 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..601
FT                   /note="COP9 signalosome complex subunit 1"
FT                   /id="PRO_0000120963"
FT   DOMAIN          338..500
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   601 AA;  68402 MW;  CBF1ED041363688A CRC64;
     MQNELLDDPM DTGAPAAEAA AADEPLPPAH GIDREVTPKP AGNPDLMQQS LDNPAIPMHL
     IEKRDDRRES CDDGYSLTVN ESAIDIESLA CSYDSNAFFL RARFIARHCP ILRADAYISL
     INYLKEHTTD ITHYVAFFNE LESELARKEF KNRQLNFQIP LRDQKWIEEN GATWQSTTDQ
     LQAEYKRHKD EGVKESTRRA MEDLFQHYMM AGKIDEAIRL YSRGIRDYCT QLKHSINMWI
     NWMEVAICAN DWGKLDTVTN TAYRSLKDAD DAEKNSQQSQ QAPPQRGENA PYMVERDPNA
     PIQTLTNRQL IETALAKCLA AQVLLKLRNK RYSQVVETIL QIKTECLQSK WFVTSSDLGI
     YGMLSAMATM SRADLKLQVS GNGTFRKLLE SEPQLIELLG SYTSSRFGRC FEIMRSVKPR
     LLLDPFISRN VDELFEKIRQ KCVLQYLQPY STIKMATMAE AVGMSSAELQ LSLLELIEQK
     HVSLKIDQNE GIVRILDERD ENAILKRVNV TCDRATQKAK SLLWKTTLAG ANIHSISDKE
     TRPKRKNQKE SAKFDRNFGG IDVDEDPRGI AGPSGLSDDF NIAYDQQPQQ QVQYLEDLGD
     I