CSN5_DANRE
ID CSN5_DANRE Reviewed; 334 AA.
AC Q6PC30;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE Short=Signalosome subunit 5;
DE EC=3.4.-.-;
GN Name=cops5; ORFNames=zgc:73130;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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 E3 ligase complexes, leading to modify the Ubl ligase
CC activity. In the complex, it probably acts as the catalytic center that
CC mediates the cleavage of nedd8 from cullins. It however has no
CC metalloprotease activity by itself and requires the other subunits of
CC the CSN complex. {ECO:0000250|UniProtKB:Q92905}.
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 cops1,
CC cops2, cops3, cops4, cops5, cops6, cops7, cops8 and cops9.
CC {ECO:0000250|UniProtKB:Q92905}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q92905}. Nucleus {ECO:0000250|UniProtKB:Q92905}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000250|UniProtKB:Q92905}.
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 -!- MISCELLANEOUS: The CSN complex is associated with some 'Lys-63'-
CC specific deubiquitination. Such activity is however not mediated by the
CC core CSN complex but by the brcc3/brcc36 component of the BRISC complex
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC059493; AAH59493.1; -; mRNA.
DR RefSeq; NP_957019.1; NM_200725.1.
DR AlphaFoldDB; Q6PC30; -.
DR SMR; Q6PC30; -.
DR STRING; 7955.ENSDARP00000074782; -.
DR MEROPS; M67.A13; -.
DR PaxDb; Q6PC30; -.
DR Ensembl; ENSDART00000080332; ENSDARP00000074782; ENSDARG00000057624.
DR GeneID; 393698; -.
DR KEGG; dre:393698; -.
DR CTD; 10987; -.
DR ZFIN; ZDB-GENE-040426-1686; cops5.
DR eggNOG; KOG1554; Eukaryota.
DR GeneTree; ENSGT00550000074850; -.
DR HOGENOM; CLU_053034_0_1_1; -.
DR InParanoid; Q6PC30; -.
DR OMA; ALWNKYW; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; Q6PC30; -.
DR TreeFam; TF105601; -.
DR Reactome; R-DRE-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DRE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DRE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DRE-8951664; Neddylation.
DR PRO; PR:Q6PC30; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000057624; Expressed in testis and 29 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
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:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000338; P:protein deneddylation; IBA:GO_Central.
DR GO; GO:0060118; P:vestibular receptor cell development; IMP:ZFIN.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Hydrolase; Metal-binding; Metalloprotease;
KW Nucleus; Protease; Reference proteome; Signalosome; Synapse; Zinc.
FT CHAIN 1..334
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194837"
FT DOMAIN 53..190
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 136..149
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 334 AA; 37582 MW; 1484BC4981A45A72 CRC64;
MAGSSIAMKT WELSNSMQEV QSIDEIYKYD KKQQQEILAA KPWTKDHHYF KYCKLSALAL
LKMVMHARSG GNLEVMGLML GKVDGETMII MDSFALPVEG TETRVNAQAA AYEYMAAYIE
NAKQVGRLEN AIGWYHSHPG YGCWLSGIDV STQMLNQQFQ EPFVAVVIDP TRTISAGKVN
LGAFRTYPKG YKPPDEGPSE YQTIPLNKIE DFGVHCKQYY ALEVSYFKSS LDRKLLELLW
NKYWVNTLSS SSLLTNADYT TGQVFDLSEK LEQAEAQLGR GSFMLGLDTH DRKSEDKLAK
ATRDSCKTTI EAIHGLMSQV IKDKLFNQVN TSAN
