ID A0A2K5NN25_CERAT Unreviewed; 379 AA.
AC A0A2K5NN25;
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 13 {ECO:0000256|ARBA:ARBA00015732};
DE AltName: Full=26S proteasome regulatory subunit RPN9 {ECO:0000256|ARBA:ARBA00029749};
DE AltName: Full=26S proteasome regulatory subunit S11 {ECO:0000256|ARBA:ARBA00032323};
DE AltName: Full=26S proteasome regulatory subunit p40.5 {ECO:0000256|ARBA:ARBA00031303};
GN Name=PSMD13 {ECO:0000313|Ensembl:ENSCATP00000038934.1};
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:ENSCATP00000038934.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000038934.1}
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. {ECO:0000256|ARBA:ARBA00002362}.
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 PSMD13, a base containing 6 ATPases
CC and few additional components. {ECO:0000256|ARBA:ARBA00011441}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S11 family.
CC {ECO:0000256|ARBA:ARBA00006207}.
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DR AlphaFoldDB; A0A2K5NN25; -.
DR STRING; 9531.ENSCATP00000038934; -.
DR Ensembl; ENSCATT00000063242.1; ENSCATP00000038934.1; ENSCATG00000042125.1.
DR GeneTree; ENSGT00390000001802; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000042125; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005838; C:proteasome regulatory particle; IEA:Ensembl.
DR GO; GO:0007127; P:meiosis I; IEA:Ensembl.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035298; PSMD13.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10539; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 13; 1.
DR PANTHER; PTHR10539:SF0; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 13; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 171..338
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
SQ SEQUENCE 379 AA; 42580 MW; 73FCF080FBF1B182 CRC64;
MKDVPGFLQQ SQSSGPGQPA VWHRLEELYT KKLWHQLTLQ VLDFVQDPCF AQGDGLIKLY
ENFISEFEHR VNPLSLVEII LHVVRQMTDP NVALTFLEKT REKVKSSDEA VILCKTAIGA
LKLNIGDLQV TKETIEDVEE MLNNLPGVTS VHSRFYDLSS KYYQTVGNHA SYYKDALRFL
GCVDIKDLPV SEQQERAFTL GLAGLLGEGV FNFGELLMHP VLESLRNTDR QWLIDTLYAF
NSGNVERFQT LKTAWGQQPD LAANEAQLLR KIQLLCLMEM TFTRPANHRQ LTFEEIAKSA
KITVNEVELL VMKALSVGLV KGSIDEVDRR AVAATWPVTP VCLNAPCVRI CISDQGNEGP
PGVLSMEMLV EHQAHDILT
//
