ID A0A2K6FYP2_PROCO Unreviewed; 231 AA.
AC A0A2K6FYP2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=COP9 signalosome subunit 7B {ECO:0000313|Ensembl:ENSPCOP00000019117.1};
GN Name=COPS7B {ECO:0000313|Ensembl:ENSPCOP00000019117.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000019117.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000019117.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6FYP2; -.
DR Ensembl; ENSPCOT00000029764.1; ENSPCOP00000019117.1; ENSPCOG00000021484.1.
DR GeneTree; ENSGT00940000157155; -.
DR Proteomes; UP000233160; 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:SF8; COP9 SIGNALOSOME COMPLEX SUBUNIT 7B; 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:UP000233160}.
FT DOMAIN 1..126
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 190..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..186
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 203..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 26591 MW; 921A2E9983C5D0F2 CRC64;
MTAHREFTSV YMEFRNLLQI MLAEGANAAY LQLLNLFAYG TYPDYIANKE SLPELSKAQQ
NKLKHLTIVS LASRMKCIPY SVLLKDLEMR NLRELEDLII EAVYTDIIQG KLDQRNQLLE
VDFCIGRDIR KKDINNIVKT LHEWCDGCEA VLLGIEQQVL RANQYKENHN RTQQQVEAEV
TNIKKTLKAT ASSSAQEMEQ QLAERECPPH AEQRQPTKKM SKVKGLVSSR H
//
