CSN5_XENLA
ID CSN5_XENLA Reviewed; 332 AA.
AC Q6GLM9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE Short=Signalosome subunit 5;
DE EC=3.4.-.-;
GN Name=cops5; Synonyms=csn5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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; BC074434; AAH74434.1; -; mRNA.
DR RefSeq; NP_001086291.1; NM_001092822.1.
DR AlphaFoldDB; Q6GLM9; -.
DR SMR; Q6GLM9; -.
DR MEROPS; M67.A13; -.
DR MaxQB; Q6GLM9; -.
DR DNASU; 444720; -.
DR GeneID; 444720; -.
DR KEGG; xla:444720; -.
DR CTD; 444720; -.
DR Xenbase; XB-GENE-952833; cops5.S.
DR OrthoDB; 1031881at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 444720; Expressed in testis and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0008180; C:COP9 signalosome; IEA:UniProtKB-KW.
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: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: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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..332
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194838"
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 332 AA; 37511 MW; 81019B792BC353CC CRC64;
MAGSSVAQKT WELSNNMQEV QSIDEIYKYD KKQQQEILAA KPWTKDHHYF KYCKVSALAL
LKMVMHARSG GNLEVMGLML GKVDGETMII MDSFALPVEG TETRVNAQAA AYEYMAAYIE
NAKQVGRLEN AIGWYHSHPG YGCWLSGIDV STQMLNQQFQ EPFVAVVIDP TRTISAGKVN
LGAFRTYPKG YKPPDEGPSE YQTIPLNKIE DFGVHCKQYY ALEVTYFKSS LDRKLLELLW
NKYWVNTLSS SSLLTNAEYT TGQVFDLSEK LEQSEAQLGR GSFMLGLESH DRKSEDKLAK
ATRDSCKTTI EAIHGLMSQV IKDKLFNQIN TF
