CSN6_CAEEL
ID CSN6_CAEEL Reviewed; 426 AA.
AC Q95PZ0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=COP9 signalosome complex subunit 6;
DE Short=Signalosome subunit 6;
GN Name=csn-6; ORFNames=Y67H2A.6;
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 RBX-1; CSN-2 AND
RP 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. Interacts with rbx-1.
CC {ECO:0000269|PubMed:12781129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus
CC {ECO:0000269|PubMed:12781129}.
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; AL132951; CAC44307.1; -; Genomic_DNA.
DR RefSeq; NP_001255726.1; NM_001268797.1.
DR AlphaFoldDB; Q95PZ0; -.
DR SMR; Q95PZ0; -.
DR BioGRID; 43378; 6.
DR ComplexPortal; CPX-3386; COP9 signalosome complex.
DR DIP; DIP-27463N; -.
DR IntAct; Q95PZ0; 3.
DR STRING; 6239.Y67H2A.6b; -.
DR iPTMnet; Q95PZ0; -.
DR EPD; Q95PZ0; -.
DR PaxDb; Q95PZ0; -.
DR PeptideAtlas; Q95PZ0; -.
DR PRIDE; Q95PZ0; -.
DR EnsemblMetazoa; Y67H2A.6a.1; Y67H2A.6a.1; WBGene00000818.
DR GeneID; 178289; -.
DR UCSC; Y67H2A.6; c. elegans.
DR CTD; 178289; -.
DR WormBase; Y67H2A.6a; CE28377; WBGene00000818; csn-6.
DR eggNOG; KOG3050; Eukaryota.
DR GeneTree; ENSGT00950000183073; -.
DR HOGENOM; CLU_633450_0_0_1; -.
DR InParanoid; Q95PZ0; -.
DR PhylomeDB; Q95PZ0; -.
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:Q95PZ0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000818; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q95PZ0; baseline.
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:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
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; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Nucleus; Oogenesis;
KW Reference proteome; Signalosome.
FT CHAIN 1..426
FT /note="COP9 signalosome complex subunit 6"
FT /id="PRO_0000194863"
FT DOMAIN 14..155
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 320..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47527 MW; 5E62AE7D089426A0 CRC64;
MALNAPSGSC SSKVLLHPLV IMQMSEHYSR TKVQQGPTVK KVFGAILGRQ NGRQVEAINS
FVLKMETEEM AEPVTFSTEH LLQRADQYLE VFPELQVIGL YCAGEDDNLT PEEKPLLSKL
TNAVRNSEKA GQIDATLFLK LNSITAGTTR KLPLFAFEAD VTDQEKHKPI EWILVSEESE
RVGVNHIAKL STKHGKDGKS VGKKHAEAQD AAMSMLQNRV DLIVAYLEKV QDGTLQPNFE
ILKEANLLAQ KLKTIDRYAA EFTDSFEKEE KTMTVFSLMP RLTTLLGNMQ NVWNKLSAQR
ADLLADDGFH GKSTSRWAHP VRFKSQHLGR PQQADDDDYF DDEDLENDMS GPRRKIHAAD
SPAGSRRRRV PPRAMNFLGR NSGMQAATDE MELSGQEENM GSNYIPDVPR PSATAHNESD
ESSQAS
