ID A0A2K5NX66_CERAT Unreviewed; 410 AA.
AC A0A2K5NX66;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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};
GN Name=PSMD11 {ECO:0000313|Ensembl:ENSCATP00000042129.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000042129.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000042129.1}
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}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family.
CC {ECO:0000256|ARBA:ARBA00007454}.
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DR AlphaFoldDB; A0A2K5NX66; -.
DR Ensembl; ENSCATT00000066562.1; ENSCATP00000042129.1; ENSCATG00000043638.1.
DR GeneTree; ENSGT00530000063301; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000043638; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.570; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040780; Rpn6_C_helix.
DR InterPro; IPR040773; Rpn6_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
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 Pfam; PF18055; RPN6_N; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 321..392
FT /note="PCI"
FT /evidence="ECO:0000259|SMART:SM00088"
SQ SEQUENCE 410 AA; 46114 MW; C95B5462CC648B55 CRC64;
MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT
GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE
KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL
SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD
SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQADVE RKLSQMILDK
KFHGILDQGE GVLIIFDEPP VDKTYEAALE TIQNMSKVVD SLYNKAKKLT
//
