PRS8_BOVIN
ID PRS8_BOVIN Reviewed; 406 AA.
AC P62194; A6H7C5; O35051; P47210; P52915; P52916;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=26S proteasome regulatory subunit 8;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
DE AltName: Full=Proteasome 26S subunit ATPase 5;
DE AltName: Full=Proteasome subunit p45;
DE AltName: Full=p45/SUG;
GN Name=PSMC5; Synonyms=SUG1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9701609;
RA Zhu X., Craft C.M.;
RT "Interaction of phosducin and phosducin isoforms with a 26S proteasomal
RT subunit, SUG1.";
RL Mol. Vis. 4:13-13(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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. PSMC5 belongs to the heterohexameric ring of AAA (ATPases
CC associated with diverse cellular activities) proteins that unfolds
CC ubiquitinated target proteins that are concurrently translocated into a
CC proteolytic chamber and degraded into peptides.
CC {ECO:0000250|UniProtKB:P62195}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex
CC (By similarity). The 26S proteasome consists of a 20S core particle
CC (CP) and two 19S regulatory subunits (RP) (By similarity). The
CC regulatory particle is made of a lid composed of 9 subunits, a base
CC containing 6 ATPases including PSMC5 and few additional components (By
CC similarity). Component of a complex with USP49 and RUVBL1 (By
CC similarity). Interacts with PRPF19 (By similarity). Interacts with
CC TRIM5 (By similarity). Interacts with NDC80 (By similarity). Interacts
CC with PAAF1 (By similarity). Interacts, in vitro, with the thyroid
CC hormone receptor (in a thyroid hormone T3-dependent manner) and with
CC retinoid X receptor (RXR) (By similarity). Interacts with ERCC6 (By
CC similarity). {ECO:0000250|UniProtKB:P62195,
CC ECO:0000250|UniProtKB:P62196, ECO:0000250|UniProtKB:P62198}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62195}. Nucleus
CC {ECO:0000250|UniProtKB:P62195}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF069053; AAC19266.1; -; mRNA.
DR EMBL; BC146195; AAI46196.1; -; mRNA.
DR RefSeq; NP_776866.1; NM_174441.2.
DR AlphaFoldDB; P62194; -.
DR BMRB; P62194; -.
DR SMR; P62194; -.
DR BioGRID; 159304; 1.
DR STRING; 9913.ENSBTAP00000028048; -.
DR PaxDb; P62194; -.
DR PeptideAtlas; P62194; -.
DR PRIDE; P62194; -.
DR Ensembl; ENSBTAT00000028048; ENSBTAP00000028048; ENSBTAG00000021061.
DR GeneID; 282015; -.
DR KEGG; bta:282015; -.
DR CTD; 5705; -.
DR VEuPathDB; HostDB:ENSBTAG00000021061; -.
DR VGNC; VGNC:33459; PSMC5.
DR eggNOG; KOG0728; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; P62194; -.
DR OMA; TANCRVA; -.
DR OrthoDB; 571919at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000021061; Expressed in laryngeal cartilage and 105 other tissues.
DR ExpressionAtlas; P62194; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; ISS:UniProtKB.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISS:UniProtKB.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0031531; F:thyrotropin-releasing hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62195"
FT CHAIN 2..406
FT /note="26S proteasome regulatory subunit 8"
FT /id="PRO_0000084720"
FT REGION 186..406
FT /note="May mediate interaction with PRPF9"
FT /evidence="ECO:0000250|UniProtKB:P62196"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62195"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62195"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62195"
SQ SEQUENCE 406 AA; 45626 MW; 29C6410C4A85A7F7 CRC64;
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK
