ID   CSN7A_PONAB             Reviewed;         275 AA.
AC   Q5R762;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=COP9 signalosome complex subunit 7a;
DE            Short=SGN7a;
DE            Short=Signalosome subunit 7a;
DE   AltName: Full=JAB1-containing signalosome subunit 7a;
GN   Name=COPS7A; Synonyms=CSN7A;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. The CSN
CC       complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC       pathway by mediating the deneddylation of the cullin subunits of SCF-
CC       type E3 ligase complexes, leading to decrease the Ubl ligase activity
CC       of SCF-type complexes such as SCF, CSA or DDB2. The complex is also
CC       involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA,
CC       ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD
CC       kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and
CC       protects degradation by the Ubl system, respectively (By similarity).
CC       {ECO:0000250}.
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       In the complex, it probably interacts directly with COPS1, COPS2,
CC       COPS4, COPS5, COPS6 and COPS8. Interacts with PMF1. Interacts with the
CC       translation initiation factor EIF3S6. Interacts with CK2 and PKD.
CC       Interacts directly with ID3. {ECO:0000250|UniProtKB:Q9CZ04,
CC       ECO:0000250|UniProtKB:Q9UBW8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- PTM: Phosphorylated by CK2 and PKD kinases.
CC   -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR860256; CAH92398.1; -; mRNA.
DR   EMBL; CR859228; CAH91409.1; -; mRNA.
DR   RefSeq; NP_001126414.1; NM_001132942.1.
DR   AlphaFoldDB; Q5R762; -.
DR   SMR; Q5R762; -.
DR   STRING; 9601.ENSPPYP00000004784; -.
DR   Ensembl; ENSPPYT00000004974; ENSPPYP00000004784; ENSPPYG00000004198.
DR   GeneID; 100173397; -.
DR   KEGG; pon:100173397; -.
DR   CTD; 50813; -.
DR   eggNOG; KOG3250; Eukaryota.
DR   GeneTree; ENSGT00940000159873; -.
DR   HOGENOM; CLU_054426_1_0_1; -.
DR   InParanoid; Q5R762; -.
DR   OMA; DIDSRGH; -.
DR   OrthoDB; 1396757at2759; -.
DR   TreeFam; TF101149; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0008180; C:COP9 signalosome; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
DR   GO; GO:0000338; P:protein deneddylation; IEA:Ensembl.
DR   InterPro; IPR045237; COPS7/eIF3m.
DR   InterPro; IPR037757; COPS7A.
DR   InterPro; IPR041481; CSN7_helixI.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR15350; PTHR15350; 1.
DR   PANTHER; PTHR15350:SF7; PTHR15350:SF7; 1.
DR   Pfam; PF18392; CSN7a_helixI; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Signalosome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBW8"
FT   CHAIN           2..275
FT                   /note="COP9 signalosome complex subunit 7a"
FT                   /id="PRO_0000120998"
FT   DOMAIN          2..159
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          227..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          185..233
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBW8"
SQ   SEQUENCE   275 AA;  30277 MW;  20888B35BFFF6326 CRC64;
     MSAEVKVTGQ NQEQFLLLAK SAKGAALATL IHQVLEAPGV YVFGELLDMP NVRELAESDF
     ASTFRLLTVF AYGTYADYLA EARNLPPLTE AQKNKLRHLS VVTLAAKVKC IPYAVLLEAL
     ALRNVRQLED LVIEAVYADV LRGSLDQRNQ RLEVDYSIGR DIQRQDLSAI ARTLQEWCVG
     CEVVLSGIEE QVSRANQHKE QQLGLKQQIE SEVANLKKTI KVTTAAAAAA TSQDPEQHLT
     ELREPAPGTN QRQPSKKASK GKGLRGSAKI WSKSN