PRS10_BOVIN
ID PRS10_BOVIN Reviewed; 389 AA.
AC Q2KIW6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=26S proteasome regulatory subunit 10B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT4;
DE AltName: Full=Proteasome 26S subunit ATPase 6;
GN Name=PSMC6;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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. PSMC6 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:P62333}.
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, a base containing 6 ATPases including PSMC6 and
CC few additional components. Interacts with PAAF1.
CC {ECO:0000250|UniProtKB:P62333}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; BC112482; AAI12483.1; -; mRNA.
DR RefSeq; NP_001039705.1; NM_001046240.2.
DR AlphaFoldDB; Q2KIW6; -.
DR SMR; Q2KIW6; -.
DR CORUM; Q2KIW6; -.
DR IntAct; Q2KIW6; 9.
DR STRING; 9913.ENSBTAP00000020886; -.
DR PaxDb; Q2KIW6; -.
DR PeptideAtlas; Q2KIW6; -.
DR PRIDE; Q2KIW6; -.
DR GeneID; 518637; -.
DR KEGG; bta:518637; -.
DR CTD; 5706; -.
DR eggNOG; KOG0651; Eukaryota.
DR InParanoid; Q2KIW6; -.
DR OrthoDB; 571919at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:InterPro.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
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 InterPro; IPR035263; PSMC6.
DR PANTHER; PTHR23073:SF76; PTHR23073:SF76; 1.
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 CHAIN 1..389
FT /note="26S proteasome regulatory subunit 10B"
FT /id="PRO_0000263085"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62333"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62333"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62333"
SQ SEQUENCE 389 AA; 44074 MW; A8D421295753CACD CRC64;
MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV
LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY
NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK
TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG
RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH
IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLGNVCTEA GMFAIRADHD
FVVQEDFMKA VRKVADSKKL ESKLDYKPV