GenomeNet

Database: UniProt
Entry: A0A340Y738_LIPVE
LinkDB: A0A340Y738_LIPVE
Original site: A0A340Y738_LIPVE 
ID   A0A340Y738_LIPVE        Unreviewed;       239 AA.
AC   A0A340Y738;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=COP9 signalosome complex subunit 7a isoform X4 {ECO:0000313|RefSeq:XP_007469471.1};
GN   Name=COPS7A {ECO:0000313|RefSeq:XP_007469471.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007469471.1};
RN   [1] {ECO:0000313|RefSeq:XP_007469471.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_007469471.1; XM_007469409.1.
DR   AlphaFoldDB; A0A340Y738; -.
DR   GeneID; 103091538; -.
DR   CTD; 50813; -.
DR   OrthoDB; 931897at2759; -.
DR   Proteomes; UP000265300; Unplaced.
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300}.
FT   DOMAIN          1..159
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          194..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  26336 MW;  033110A1B0E0BA5B CRC64;
     MSAEVKVTGQ NQEQFLLLAK SAKGAALATL IHQVLEAPGV YVFGELLDMP NVRELAESDF
     ASTFRLLTVF AYGTYADYLA EARNLPPLTE AQKNKLRHLS VVTLAAKVKC IPYAVLLEAL
     ALRNVRQLED LVIEAVYADV LRGSLDQRNQ RLEVDYSIGR DIQRQDLSAI ARTLQEWCVG
     CEVVLSGIEE QVSRANQHKE QQKPRRARGS EGAPRFGPSR TEGTVVSSGM WGPSCLPAP
//
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