CSN5_CAEEL
ID CSN5_CAEEL Reviewed; 368 AA.
AC P91001;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE Short=Signalosome subunit 5;
DE EC=3.4.-.-;
DE AltName: Full=JAB1 homolog;
GN Name=csn-5; ORFNames=B0547.1;
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 INTERACTION WITH LAG-1.
RX PubMed=10615043; DOI=10.1126/science.287.5450.116;
RA Walhout A.J.M., Sordella R., Lu X., Hartley J.L., Temple G.F., Brasch M.A.,
RA Thierry-Mieg N., Vidal M.;
RT "Protein interaction mapping in C. elegans using proteins involved in
RT vulval development.";
RL Science 287:116-122(2000).
RN [3]
RP INTERACTION WITH GLH-1 AND GLH-3.
RX PubMed=12435362; DOI=10.1006/dbio.2002.0832;
RA Smith P., Leung-Chiu W.-M., Montgomery R., Orsborn A., Kuznicki K.,
RA Gressman-Coberly E., Mutapcic L., Bennett K.;
RT "The GLH proteins, Caenorhabditis elegans P granule components, associate
RT with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a
RT predicted cytoskeletal protein.";
RL Dev. Biol. 251:333-347(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CSN-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).
RN [5]
RP FUNCTION, AND INTERACTION WITH KGB-1.
RX PubMed=17699606; DOI=10.1242/dev.005181;
RA Orsborn A.M., Li W., McEwen T.J., Mizuno T., Kuzmin E., Matsumoto K.,
RA Bennett K.L.;
RT "GLH-1, the C. elegans P granule protein, is controlled by the JNK KGB-1
RT and by the COP9 subunit CSN-5.";
RL Development 134:3383-3392(2007).
CC -!- FUNCTION: Probable protease subunit of the COP9 signalosome complex
CC (CSN), a complex involved in various cellular and developmental
CC processes. The CSN complex is an essential regulator of the ubiquitin
CC (Ubl) 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. In the complex, it probably acts as the
CC catalytic center that mediates the cleavage of Nedd8 from cullins. It
CC however has no metalloprotease activity by itself and requires the
CC other subunits of the CSN complex (By similarity). The CSN complex
CC plays an essential role in embryogenesis and oogenesis and is required
CC to regulate microtubule stability in the early embryo. Mediates mei-
CC 3/katanin targeting for degradation at the meiosis to mitosis
CC transition via deneddylation of cul-3. May stabilize glh-1 protein
CC levels by antagonizing kgb-1 (PubMed:17699606). {ECO:0000250,
CC ECO:0000269|PubMed:12781129, ECO:0000303|PubMed:17699606}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
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 (PubMed:12781129). Interacts with glh-1
CC and glh-3 (PubMed:12435362). Interacts with lag-1 (PubMed:10615043).
CC Interacts with kgb-1 (PubMed:17699606). {ECO:0000269|PubMed:10615043,
CC ECO:0000269|PubMed:12435362, ECO:0000269|PubMed:12781129,
CC ECO:0000269|PubMed:17699606}.
CC -!- INTERACTION:
CC P91001; P34689: glh-1; NbExp=3; IntAct=EBI-313007, EBI-1571791;
CC P91001; O01836: glh-3; NbExp=2; IntAct=EBI-313007, EBI-1571750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12781129}. Nucleus
CC {ECO:0000269|PubMed:12781129}.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity of the
CC CSN complex resulting in deneddylation of cullins. It constitutes the
CC catalytic center of the complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; FO080232; CCD62206.1; -; Genomic_DNA.
DR PIR; T29320; T29320.
DR RefSeq; NP_500841.1; NM_068440.4.
DR AlphaFoldDB; P91001; -.
DR SMR; P91001; -.
DR BioGRID; 42464; 63.
DR ComplexPortal; CPX-3386; COP9 signalosome complex.
DR DIP; DIP-26100N; -.
DR IntAct; P91001; 45.
DR MINT; P91001; -.
DR STRING; 6239.B0547.1; -.
DR MEROPS; M67.002; -.
DR iPTMnet; P91001; -.
DR EPD; P91001; -.
DR PaxDb; P91001; -.
DR PeptideAtlas; P91001; -.
DR EnsemblMetazoa; B0547.1.1; B0547.1.1; WBGene00000817.
DR GeneID; 177342; -.
DR KEGG; cel:CELE_B0547.1; -.
DR UCSC; B0547.1.1; c. elegans.
DR CTD; 177342; -.
DR WormBase; B0547.1; CE06722; WBGene00000817; csn-5.
DR eggNOG; KOG1554; Eukaryota.
DR GeneTree; ENSGT00550000074850; -.
DR HOGENOM; CLU_053034_0_2_1; -.
DR InParanoid; P91001; -.
DR OMA; AYEYMSV; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; P91001; -.
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; P91001; -.
DR PRO; PR:P91001; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000817; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0031672; C:A band; IDA:WormBase.
DR GO; GO:0008180; C:COP9 signalosome; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR GO; GO:0019784; F:deNEDDylase activity; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:WormBase.
DR GO; GO:0060184; P:cell cycle switching; IMP:ComplexPortal.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IMP:ComplexPortal.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0000338; P:protein deneddylation; IGI:WormBase.
DR GO; GO:1905879; P:regulation of oogenesis; IMP:ComplexPortal.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR InterPro; IPR037740; CSN5.
DR InterPro; IPR040961; CSN5_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR10410:SF6; PTHR10410:SF6; 1.
DR Pfam; PF18323; CSN5_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Hydrolase;
KW Metal-binding; Metalloprotease; Nucleus; Oogenesis; Protease;
KW Reference proteome; Signalosome; Zinc.
FT CHAIN 1..368
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194840"
FT DOMAIN 56..193
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 347..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 139..152
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 368 AA; 41008 MW; 0DA27521156E0E70 CRC64;
MEVDNVKPSS SVPQRNWEKE NNVQNVDSIF EYNNKQQVEI RNAKPWDKDP HYFKQIKISA
IALLKMTMHA KRGGNLEIMG LLQGRIDANS FIILDVFALP VEGTETRVNA QAQAYEYMTV
YSEMCDTEGR KEKVVGWYHS HPGYGCWLSG IDVSTQTLNQ KFQEPWVAIV IDPLRTMSAG
KVDIGAFRTY PEGYRPPDDV PSEYQSIPLA KIEDFGVHCK RYYSLDVSFF KSQLDAHILT
SLWNSYWIST LSSSPLFSNV EFLNNQIQDI NQKLSAVDKK LQLNDRSVDG HEALMKVVTD
AKAVGDELET GRISHLVKQL LFARQAGGGC GCSHASAGSP MDIAVATEPE KAGPSPSAPE
PAVEMADA
