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Database: UniProt
Entry: A0A093PIL5_9PASS
LinkDB: A0A093PIL5_9PASS
Original site: A0A093PIL5_9PASS 
ID   A0A093PIL5_9PASS        Unreviewed;       226 AA.
AC   A0A093PIL5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=COP9 signalosome complex subunit 7a {ECO:0000313|EMBL:KFW74100.1};
DE   Flags: Fragment;
GN   ORFNames=N305_07297 {ECO:0000313|EMBL:KFW74100.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW74100.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW74100.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW74100.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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.
CC       {ECO:0000256|ARBA:ARBA00025037}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008482}.
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DR   EMBL; KL668721; KFW74100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093PIL5; -.
DR   STRING; 328815.ENSMVIP00005018883; -.
DR   Proteomes; UP000053258; Unassembled WGS sequence.
DR   GO; GO:0008180; C:COP9 signalosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
DR   InterPro; IPR045237; COPS7/eIF3m.
DR   InterPro; IPR041481; CSN7_helixI.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR15350; COP9 SIGNALOSOME COMPLEX SUBUNIT 7/DENDRITIC CELL PROTEIN GA17; 1.
DR   PANTHER; PTHR15350:SF7; COP9 SIGNALOSOME COMPLEX SUBUNIT 7A; 1.
DR   Pfam; PF18392; CSN7a_helixI; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258}.
FT   DOMAIN          1..110
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          179..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          150..177
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW74100.1"
FT   NON_TER         226
FT                   /evidence="ECO:0000313|EMBL:KFW74100.1"
SQ   SEQUENCE   226 AA;  25210 MW;  27DA6A4ABF9B17D0 CRC64;
     PVSPQLADSE FSPVFRLLTI FAYGTYADYL AEAANLPPLT EAQKNKLRHL SVVTLAAKIK
     CIPYSVLLEQ LQLKNVRQLE DLVIEAVYAD VLRGSLDQRN QRLEVDYSIG RDIRREELST
     ITRTLQEWCQ GCEVVLSGIE EQVSRANQHK EQQLALKQQI ESEVANLKKT IKVTTAAAAA
     ATSQDPEQHL TELREPAPGT NQRQASKKTS KAKGLRGSAK IWSKSN
//
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