CSN4_RAT
ID CSN4_RAT Reviewed; 406 AA.
AC Q68FS2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=COP9 signalosome complex subunit 4;
DE Short=SGN4;
DE Short=Signalosome subunit 4;
DE AltName: Full=JAB1-containing signalosome subunit 4;
GN Name=Cops4; Synonyms=Csn4;
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=Testis;
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 INTERACTION WITH TOR1A AND STON2, AND SUBCELLULAR LOCATION.
RX PubMed=21102408; DOI=10.1038/emboj.2010.285;
RA Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
RT "CSN complex controls the stability of selected synaptic proteins via a
RT torsinA-dependent process.";
RL EMBO J. 30:181-193(2011).
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 (PubMed:21102408).
CC Interacts with STON2; controls STON2 neddylation levels
CC (PubMed:21102408). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BT78, ECO:0000269|PubMed:21102408}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BT78}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BT78}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000269|PubMed:21102408}.
CC -!- SIMILARITY: Belongs to the CSN4 family. {ECO:0000305}.
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DR EMBL; BC079384; AAH79384.1; -; mRNA.
DR RefSeq; NP_001004275.1; NM_001004275.1.
DR AlphaFoldDB; Q68FS2; -.
DR SMR; Q68FS2; -.
DR BioGRID; 262300; 1.
DR IntAct; Q68FS2; 18.
DR MINT; Q68FS2; -.
DR STRING; 10116.ENSRNOP00000003046; -.
DR iPTMnet; Q68FS2; -.
DR PhosphoSitePlus; Q68FS2; -.
DR jPOST; Q68FS2; -.
DR PaxDb; Q68FS2; -.
DR PRIDE; Q68FS2; -.
DR GeneID; 360915; -.
DR KEGG; rno:360915; -.
DR CTD; 51138; -.
DR RGD; 1302952; Cops4.
DR VEuPathDB; HostDB:ENSRNOG00000023650; -.
DR eggNOG; KOG1497; Eukaryota.
DR HOGENOM; CLU_028132_1_0_1; -.
DR InParanoid; Q68FS2; -.
DR OMA; KNIMHTV; -.
DR OrthoDB; 866823at2759; -.
DR PhylomeDB; Q68FS2; -.
DR TreeFam; TF101147; -.
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 Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:Q68FS2; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000023650; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q68FS2; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0008180; C:COP9 signalosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
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 1: Evidence at protein 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_0000120989"
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; 46290 MW; B0F34DFC48E8DDA2 CRC64;
MAAAVRQDLA QLMNSSGSHK DLAGKYRQIL EKAIQLSGTE QLEALKAFVE AMVNENVSLV
ISRQLLTDFC THLPNLPDST AKEVYHFTLE KVQPRVISFE EQVASIRQRL 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
