ID   CSN3_RAT                Reviewed;         423 AA.
AC   Q68FW9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=COP9 signalosome complex subunit 3;
DE            Short=SGN3;
DE            Short=Signalosome subunit 3;
GN   Name=Cops3; Synonyms=Csn3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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/ICSBP,
CC       possibly via its association with CK2 and PKD kinases (By similarity).
CC       CSN-dependent phosphorylation of TP53 and JUN promotes and protects
CC       degradation by the Ubl system, respectively (By similarity). Essential
CC       to maintain the survival of epiblast cells and thus the development of
CC       the postimplantation embryo (By similarity).
CC       {ECO:0000250|UniProtKB:O88543, ECO:0000250|UniProtKB:Q9UNS2}.
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, COPS4, COPS8 and COPS9 (By similarity). Interacts with CK2 and
CC       PKD (By similarity). Interacts with the translation initiation factor
CC       EIF3S6 and IKBKG (By similarity). Interacts with ERCC6 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UNS2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UNS2}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9UNS2}.
CC   -!- SIMILARITY: Belongs to the CSN3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC079143; AAH79143.1; -; mRNA.
DR   RefSeq; NP_001004200.1; NM_001004200.1.
DR   AlphaFoldDB; Q68FW9; -.
DR   SMR; Q68FW9; -.
DR   BioGRID; 252124; 1.
DR   STRING; 10116.ENSRNOP00000004438; -.
DR   iPTMnet; Q68FW9; -.
DR   PhosphoSitePlus; Q68FW9; -.
DR   jPOST; Q68FW9; -.
DR   PaxDb; Q68FW9; -.
DR   PRIDE; Q68FW9; -.
DR   Ensembl; ENSRNOT00000091471; ENSRNOP00000069208; ENSRNOG00000053943.
DR   GeneID; 287367; -.
DR   KEGG; rno:287367; -.
DR   UCSC; RGD:1303002; rat.
DR   CTD; 8533; -.
DR   RGD; 1303002; Cops3.
DR   eggNOG; KOG2582; Eukaryota.
DR   GeneTree; ENSGT00940000153653; -.
DR   HOGENOM; CLU_028825_0_1_1; -.
DR   InParanoid; Q68FW9; -.
DR   OMA; NHYHDLV; -.
DR   OrthoDB; 929822at2759; -.
DR   PhylomeDB; Q68FW9; -.
DR   TreeFam; TF101146; -.
DR   Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   PRO; PR:Q68FW9; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000053943; Expressed in quadriceps femoris and 20 other tissues.
DR   Genevisible; Q68FW9; RN.
DR   GO; GO:0008180; C:COP9 signalosome; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0000338; P:protein deneddylation; ISO:RGD.
DR   GO; GO:1902162; P:regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:RGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR037753; CSN3.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10758:SF1; PTHR10758:SF1; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   Signalosome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNS2"
FT   CHAIN           2..423
FT                   /note="COP9 signalosome complex subunit 3"
FT                   /id="PRO_0000312647"
FT   DOMAIN          197..365
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          402..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNS2"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNS2"
SQ   SEQUENCE   423 AA;  47859 MW;  B43417898A44B2C4 CRC64;
     MASALEQFVN SVRQLSAQGQ MTQLCELINK SGELLAKNLS HLDTVLGALD VQEHSLGVLA
     VLFVKFSMPS VPDFETLFSQ VQLFISTCNG EHIRYATDTF AGLCHQLTNA LVERKQPLRG
     IGILKQAIDK MQMNTNQLTS VHADLCQLCL LAKCFKPALP YLDVDMMDIC KENGAYDAKH
     FLCYYYYGGM IYTGLKNFER ALYFYEQAIT TPAMAVSHIM LESYKKYILV SLILLGKVQQ
     LPKYTSQIVG RFIKPLSNAY HELAQVYSTN NPSELRNLVN KHSETFTRDN NMGLVKQCLS
     SLYKKNIQRL TKTFLTLSLQ DMASRVQLSG PQEAEKYVLH MIEDGEIFAS INQKDGMVSF
     HDNPEKYNNP AMLHNIDQEM LKCIELDERL KAMDQEITVN PQFVQKSMGS QEDDSGNKPS
     SYS