CSN6_BOVIN
ID CSN6_BOVIN Reviewed; 324 AA.
AC A6QQ21;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=COP9 signalosome complex subunit 6;
DE Short=SGN6;
DE Short=Signalosome subunit 6;
GN Name=COPS6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes (By
CC similarity). The CSN complex is an essential regulator of the ubiquitin
CC (Ubl) conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl
CC ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By
CC similarity). The complex is also involved in phosphorylation of
CC p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via
CC its association with CK2 and PKD kinases (By similarity). CSN-dependent
CC phosphorylation of TP53 and JUN promotes and protects degradation by
CC the Ubl system, respectively (By similarity). Has some glucocorticoid
CC receptor-responsive activity (By similarity). Stabilizes COP1 through
CC reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate,
CC hence regulates the ubiquitination of COP1 targets, including SFN (By
CC similarity). {ECO:0000250|UniProtKB:Q7L5N1}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9
CC (By similarity). In the complex, it probably interacts directly with
CC COPS2, COPS4, COPS5, COPS7 (COPS7A or COPS7B) and COPS9 (By
CC similarity). Interacts with the translation initiation factor EIF3S6
CC (By similarity). Interacts weakly with RBX1 (By similarity). Directly
CC interacts with COP1 and 14-3-3 protein sigma/SFN (By similarity).
CC Interacts with ERCC6 (By similarity). {ECO:0000250|UniProtKB:Q7L5N1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L5N1}. Nucleus
CC {ECO:0000250|UniProtKB:Q7L5N1}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M67A family, it lacks the
CC JAMM motif that probably constitutes the catalytic center and therefore
CC it probably does not have a protease activity. {ECO:0000305}.
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DR EMBL; BC149601; AAI49602.1; -; mRNA.
DR RefSeq; NP_001095433.1; NM_001101963.2.
DR AlphaFoldDB; A6QQ21; -.
DR SMR; A6QQ21; -.
DR STRING; 9913.ENSBTAP00000003725; -.
DR PaxDb; A6QQ21; -.
DR PRIDE; A6QQ21; -.
DR GeneID; 512756; -.
DR KEGG; bta:512756; -.
DR CTD; 10980; -.
DR eggNOG; KOG3050; Eukaryota.
DR InParanoid; A6QQ21; -.
DR OrthoDB; 1455324at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0000338; P:protein deneddylation; IEA:InterPro.
DR CDD; cd08063; MPN_CSN6; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033859; MPN_CSN6.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; Signalosome.
FT CHAIN 1..324
FT /note="COP9 signalosome complex subunit 6"
FT /id="PRO_0000331507"
FT DOMAIN 38..171
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 324 AA; 35952 MW; 797BD3EA929FE75F CRC64;
MAATAAAANG TGGSSGMEVD AAVVPSVMAS GVTGSVSVAL HPLVILNISD HWIRMRSQEG
RPMQVIGALI GKQEGRNIEV MNSFELLSHT VEEKIIIDKE YYYTKEEQFK QVFKELDFLG
WYTTGGPPDP SDIHVHKQVC EIIESPLFLK LNPMTKHTDL PVSVFESVID IINGEATMLF
AELTYTLATE EAERIGVDHV ARMTATGSGE NSTVAEHLIA QHSAIKMLHS RVKLILEYVK
ASEAGEVPFN HEILREAYAL CHCLPVLSTD KFKTDFYDQC NDVGLMAYLG TITKTCNTMN
QFVNKFNVLY DRQGIGRRMR GLFF