ID A0A091HW36_CALAN Unreviewed; 274 AA.
AC A0A091HW36;
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 7b {ECO:0000313|EMBL:KFP00524.1};
GN ORFNames=N300_13362 {ECO:0000313|EMBL:KFP00524.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP00524.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP00524.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP00524.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL217930; KFP00524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HW36; -.
DR STRING; 9244.A0A091HW36; -.
DR Proteomes; UP000054308; 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: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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT DOMAIN 1..169
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 237..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 30927 MW; CB2E25738F205EEA CRC64;
MAGEQKPSCN LLEQFILLAK GTSGSALTAL INQVLEAPGV YVFGELLELT SVQELAEGSN
AAYYQLLNLF AYGTYPDYVV LNLVFLTLTA NKDNLPELTA TQKNKLKHLT IVSLASRMKC
IPYSVLLKDL DMRNLRELED LIIEAVYTDI IQGKLDQRNQ VLEVDFCIGR DIQKKDISNI
VKTLQEWCDG CESVLLGIEQ QVLRANQYKE NHHRTQQQVE MEVTNIKKTL KATASSSAQE
MEQQLVEREC PPHTEQRQPT KKMSKVKGLV SSRH
//
