ID A0A673BU84_9TELE Unreviewed; 289 AA.
AC A0A673BU84;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 11 {ECO:0000256|ARBA:ARBA00039723};
DE AltName: Full=26S proteasome regulatory subunit RPN6 {ECO:0000256|ARBA:ARBA00041252};
OS Sphaeramia orbicularis (orbiculate cardinalfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005044152.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005044152.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. In the complex, PSMD11 is required for proteasome assembly.
CC Plays a key role in increased proteasome activity in embryonic stem
CC cells (ESCs): its high expression in ESCs promotes enhanced assembly of
CC the 26S proteasome, followed by higher proteasome activity.
CC {ECO:0000256|ARBA:ARBA00037179}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits including PSMD11, a base containing 6 ATPases
CC and few additional components. {ECO:0000256|ARBA:ARBA00038658}.
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DR AlphaFoldDB; A0A673BU84; -.
DR Ensembl; ENSSORT00005045272.1; ENSSORP00005044152.1; ENSSORG00005020316.1.
DR Proteomes; UP000472271; Unplaced.
DR Gene3D; 1.25.40.570; -; 2.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040780; Rpn6_C_helix.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10678:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11; 1.
DR PANTHER; PTHR10678; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11/COP9 SIGNALOSOME COMPLEX SUBUNIT 2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18503; RPN6_C_helix; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000472271}.
FT DOMAIN 191..271
FT /note="PCI"
FT /evidence="ECO:0000259|SMART:SM00088"
SQ SEQUENCE 289 AA; 31993 MW; 9AD5AFEC6455B29F CRC64;
LCFGPSELGG LLKYAARLVR SLLDLFLDHG GGHGAGGVSC VWSASSGPRP RKRTFLRQAL
EVTSFRLGSQ LLQELKKMDD KALLVEVQLL ESKTYHALSN LPKARAALTS ARTTAALDMQ
SAEEKDWKTI MLMPEDVQAL ISGKLALRYA GRQTDSLKCV ALASQNRSLA DFEQALTEYK
SELRDDPIIS THLTKLYHNL LEQNLIRVIE PFSRVQVGPS PPPESNVERK LSQMILDKKF
TVGILDQGAG VLIVFEEPVV DQTYESALET IHNMSKVVDS LYNKAKKLT
//