CSN2_CAEEL
ID CSN2_CAEEL Reviewed; 495 AA.
AC O01422;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=COP9 signalosome complex subunit 2;
DE Short=Signalosome subunit 2;
GN Name=csn-2; ORFNames=B0025.2;
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-1; CSN-3 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: 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-1, csn-3 and csn-4.
CC {ECO:0000269|PubMed:12781129}.
CC -!- INTERACTION:
CC O01422; Q9GS00: csn-1; NbExp=4; IntAct=EBI-331413, EBI-331408;
CC O01422; Q9N359: csn-4; NbExp=3; IntAct=EBI-331413, EBI-331347;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus
CC {ECO:0000269|PubMed:12781129}.
CC -!- SIMILARITY: Belongs to the CSN2 family. {ECO:0000305}.
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DR EMBL; FO080100; CCD61197.1; -; Genomic_DNA.
DR PIR; T25440; T25440.
DR RefSeq; NP_491740.1; NM_059339.6.
DR AlphaFoldDB; O01422; -.
DR SMR; O01422; -.
DR BioGRID; 37732; 17.
DR ComplexPortal; CPX-3386; COP9 signalosome complex.
DR DIP; DIP-24665N; -.
DR IntAct; O01422; 6.
DR STRING; 6239.B0025.2.2; -.
DR EPD; O01422; -.
DR PaxDb; O01422; -.
DR PeptideAtlas; O01422; -.
DR EnsemblMetazoa; B0025.2.1; B0025.2.1; WBGene00000814.
DR EnsemblMetazoa; B0025.2.2; B0025.2.2; WBGene00000814.
DR GeneID; 172278; -.
DR KEGG; cel:CELE_B0025.2; -.
DR UCSC; B0025.2.1; c. elegans.
DR CTD; 172278; -.
DR WormBase; B0025.2; CE27562; WBGene00000814; csn-2.
DR eggNOG; KOG1464; Eukaryota.
DR GeneTree; ENSGT00530000063301; -.
DR HOGENOM; CLU_028981_0_1_1; -.
DR InParanoid; O01422; -.
DR OMA; EEQYDFE; -.
DR OrthoDB; 1108845at2759; -.
DR PhylomeDB; O01422; -.
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:O01422; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000814; Expressed in embryo and 3 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; IBA:GO_Central.
DR GO; GO:1905879; P:regulation of oogenesis; IMP:ComplexPortal.
DR InterPro; IPR037750; COPS2.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
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 SUPFAM; SSF48452; SSF48452; 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..495
FT /note="COP9 signalosome complex subunit 2"
FT /id="PRO_0000120973"
FT DOMAIN 254..416
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 56781 MW; 8959D0E5D4821B4C CRC64;
MGDEYMDDDE DYGFEYEDDS GSEPDVDMEN QYYTAKGLRS DGKLDEAIKS FEKVLELEGE
KGEWGFKALK QMIKITFGQN RLEKMLEYYR QLLTYIKSAV TKNYSEKSIN AILDYISTSR
QMDLLQHFYE TTLDALKDAK NERLWFKTNT KLGKLFFDLH EFTKLEKIVK QLKVSCKNEQ
GEEDQRKGTQ LLEIYALEIQ MYTEQKNNKA LKWVYELATQ AIHTKSAIPH PLILGTIREC
GGKMHLRDGR FLDAHTDFFE AFKNYDESGS PRRTTCLKYL VLANMLIKSD INPFDSQEAK
PFKNEPEIVA MTQMVQAYQD NDIQAFEQIM AAHQDSIMAD PFIREHTEEL MNNIRTQVLL
RLIRPYTNVR ISYLSQKLKV SQKEVIHLLV DAILDDGLEA KINEESGMIE MPKNKKKMMV
TSLVVPNAGD QGTTKSDSKP GTSSEPSTTT SVTSSILQGP PATSSCHQEL SMDGLRVWAE
RIDSIQSNIG TRIKF
