CSN5_XENTR
ID CSN5_XENTR Reviewed; 334 AA.
AC Q6P635; Q28HI7;
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; Synonyms=csn5; ORFNames=TTpA010d21.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-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; CR760870; CAJ82897.1; -; mRNA.
DR EMBL; BC062499; AAH62499.1; -; mRNA.
DR RefSeq; NP_989109.1; NM_203778.1.
DR AlphaFoldDB; Q6P635; -.
DR SMR; Q6P635; -.
DR STRING; 8364.ENSXETP00000050270; -.
DR MEROPS; M67.A13; -.
DR PaxDb; Q6P635; -.
DR DNASU; 394714; -.
DR GeneID; 394714; -.
DR KEGG; xtr:394714; -.
DR CTD; 10987; -.
DR Xenbase; XB-GENE-952827; cops5.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_053034_0_2_1; -.
DR InParanoid; Q6P635; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; Q6P635; -.
DR Reactome; R-XTR-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-XTR-8951664; Neddylation.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
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 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_0000194839"
FT DOMAIN 55..192
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 138..151
FT /note="JAMM motif"
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 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 151
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; 37637 MW; 666D9D99866B2E10 CRC64;
MAMAGSSVAQ KTWELSNNMQ EVQSIDEIYK YDKKQQQEIL AAKPWTKDHH YFKYCKVSAL
ALLKMVMHAR SGGNLEVMGL MLGKVDGETM IIMDSFALPV EGTETRVNAQ AAAYEYMAAY
IENAKQVGRL ENAIGWYHSH PGYGCWLSGI DVSTQMLNQQ FQEPFVAVVI DPTRTISAGK
VNLGAFRTYP KGYKPPDEGP SEYQTIPLNK IEDFGVHCKQ YYALEVTYFK SSLDRKLLEL
LWNKYWVNTL SSSSLLTNAD YTTGQVFDLS EKLEQSEAQL GRGSFMLGLE THDRKSEDKL
AKATRDSCKT TIEAIHGLMS QVIKDKLFNQ INTA
