ID   CSN4_MACFA              Reviewed;         406 AA.
AC   Q4R5E6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=COP9 signalosome complex subunit 4;
DE            Short=SGN4;
DE            Short=Signalosome subunit 4;
GN   Name=COPS4; ORFNames=QnpA-15976;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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). Also involved in the deneddylation of non-cullin subunits
CC       such as STON2 (By similarity). The complex is also involved in
CC       phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1,
CC       IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD
CC       kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN
CC       promotes and protects degradation by the Ubl system, respectively (By
CC       similarity). {ECO:0000250|UniProtKB:Q9BT78}.
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       COPS1, COPS2, COPS3, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8
CC       (By similarity). Interacts with TOR1A; the interaction is direct and
CC       associates TOR1A and SNAPIN with the CSN complex (By similarity).
CC       Interacts with STON2; controls STON2 neddylation levels (By
CC       similarity). Interacts with ERCC6 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BT78}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BT78}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9BT78}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle {ECO:0000250|UniProtKB:Q9BT78}.
CC   -!- SIMILARITY: Belongs to the CSN4 family. {ECO:0000305}.
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DR   EMBL; AB169597; BAE01679.1; -; mRNA.
DR   RefSeq; NP_001270140.1; NM_001283211.1.
DR   AlphaFoldDB; Q4R5E6; -.
DR   SMR; Q4R5E6; -.
DR   STRING; 9541.XP_005554966.1; -.
DR   Ensembl; ENSMFAT00000001937; ENSMFAP00000027751; ENSMFAG00000045246.
DR   GeneID; 101925908; -.
DR   CTD; 51138; -.
DR   VEuPathDB; HostDB:ENSMFAG00000045246; -.
DR   eggNOG; KOG1497; Eukaryota.
DR   GeneTree; ENSGT00940000153510; -.
DR   OMA; KNIMHTV; -.
DR   OrthoDB; 866823at2759; -.
DR   Proteomes; UP000233100; Chromosome 5.
DR   Bgee; ENSMFAG00000045246; Expressed in skeletal muscle tissue and 13 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:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0000338; P:protein deneddylation; ISS:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR037754; CSN4.
DR   InterPro; IPR041406; CSN4_HTH.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR040134; PSMD12/CSN4.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10855; PTHR10855; 1.
DR   PANTHER; PTHR10855:SF2; PTHR10855:SF2; 1.
DR   Pfam; PF18420; CSN4_RPN5_eIF3a; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoplasmic vesicle; Nucleus; Reference proteome;
KW   Signalosome; Synapse.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT78"
FT   CHAIN           2..406
FT                   /note="COP9 signalosome complex subunit 4"
FT                   /id="PRO_0000326553"
FT   DOMAIN          197..366
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT78"
FT   MOD_RES         25
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT78"
SQ   SEQUENCE   406 AA;  46269 MW;  4EFF9079058EB609 CRC64;
     MAAAVRQDLA QLMNSSGSHK DLAGKYRQIL EKAIQLSGAE QLEALKAFVE AMVNENVSLV
     ISRQLLTDFC THLPNLPDST AKEIYHFTLE KIQPRVISFE EQVASIRQHL ASIYEKEEDW
     RNAAQVLVGI PLETGQKQYN VDYKLETYLK IARLYLEDDD PVQAEAYINR ASLLQNESTN
     EQLQIHYKVC YARVLDYRRK FIEAAQRYNE LSYKTIVHES ERLEALKHAL HCTILASAGQ
     QRSRMLATLF KDERCQQLAA YGILEKMYLD RIIRGNQLQE FAAMLMPHQK ATTADGSSIL
     DRAVIEHNLL SASKLYNNIT FEELGALLEI PAAKAEKIAS QMITEGRMNG FIDQIDGIVH
     FETREALPTW DKQIQSLCFQ VNNLLEKISQ TAPEWTAQAM EAQMAQ