CSN4_CAEEL
ID CSN4_CAEEL Reviewed; 412 AA.
AC Q9N359;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=COP9 signalosome complex subunit 4;
DE Short=Signalosome subunit 4;
GN Name=csn-4; ORFNames=Y55F3AM.15;
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-2; CSN-3
RP AND CSN-6.
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. In the complex, it probably
CC interacts directly with csn-1, csn-2, csn-3 and csn-6. Interacts with
CC itself. {ECO:0000269|PubMed:12781129}.
CC -!- INTERACTION:
CC Q9N359; Q94261: cif-1; NbExp=3; IntAct=EBI-331347, EBI-318834;
CC Q9N359; O01422: csn-2; NbExp=3; IntAct=EBI-331347, EBI-331413;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus
CC {ECO:0000269|PubMed:12781129}.
CC -!- SIMILARITY: Belongs to the CSN4 family. {ECO:0000305}.
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DR EMBL; FO081813; CCD74073.1; -; Genomic_DNA.
DR RefSeq; NP_500034.1; NM_067633.4.
DR AlphaFoldDB; Q9N359; -.
DR SMR; Q9N359; -.
DR BioGRID; 42085; 25.
DR ComplexPortal; CPX-3386; COP9 signalosome complex.
DR DIP; DIP-27076N; -.
DR IntAct; Q9N359; 13.
DR STRING; 6239.Y55F3AM.15; -.
DR EPD; Q9N359; -.
DR PaxDb; Q9N359; -.
DR PeptideAtlas; Q9N359; -.
DR EnsemblMetazoa; Y55F3AM.15.1; Y55F3AM.15.1; WBGene00000816.
DR GeneID; 176927; -.
DR KEGG; cel:CELE_Y55F3AM.15; -.
DR UCSC; Y55F3AM.15; c. elegans.
DR CTD; 176927; -.
DR WormBase; Y55F3AM.15; CE25482; WBGene00000816; csn-4.
DR eggNOG; KOG1497; Eukaryota.
DR GeneTree; ENSGT00940000153510; -.
DR HOGENOM; CLU_028132_1_0_1; -.
DR InParanoid; Q9N359; -.
DR OMA; AKLCNKY; -.
DR OrthoDB; 866823at2759; -.
DR PhylomeDB; Q9N359; -.
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 SignaLink; Q9N359; -.
DR PRO; PR:Q9N359; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000816; Expressed in embryo 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 Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR037754; CSN4.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040134; PSMD12/CSN4.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10855; PTHR10855; 1.
DR PANTHER; PTHR10855:SF2; PTHR10855:SF2; 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..412
FT /note="COP9 signalosome complex subunit 4"
FT /id="PRO_0000120991"
FT DOMAIN 216..378
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 412 AA; 46133 MW; 9BBB0EA566B923F9 CRC64;
MSGEIERSQE VAVIFAQDTD HKAQYEALAK LCNKYLPQNA MGRVDTAEII KIIDTVIALE
TGSMVVSRQF VSLITERLDN QHLESECVKA ISEGILAIIK TRTISYEDQV CILRLMLASL
YEKEGRIKDA AQALIAINSD TSPKFNGPQA AKEGAKAQLC IRITKLLLDC SEIDEAEQYV
NRTSILMVDL GANPDIQIEH KALQARVSDA KRRFVEAAQR YYELSATEQL PNSDKLTALG
KAIVCVLLAK PGPQRSRLLT LIFKDERAPK CASFELIAKM YLTKVIHKDE LEEFEHQLQD
HQKADEHGES ILKGVIQEHN ITAISQLYIN ISFKTLGQLL GVDTEAAESM AGEMISSERL
HGYIDQTNGI LHFEDSNPMR VWDSQILSTL EQINKVSDMI VARHSEFAEF LT
