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PRS6B_BOVIN
ID   PRS6B_BOVIN             Reviewed;         418 AA.
AC   Q3T030;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=26S proteasome regulatory subunit 6B;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT3;
DE   AltName: Full=Proteasome 26S subunit ATPase 4;
GN   Name=PSMC4;
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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. PSMC4 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:P43686}.
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 PSMC4 and
CC       few additional components. Interacts with NR1I3. Interacts with PAAF1.
CC       Interacts with TRIM5. Interacts with ZFAND1 (By similarity).
CC       {ECO:0000250|UniProtKB:P43686}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P43686}. Nucleus
CC       {ECO:0000250|UniProtKB:P43686}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; BC102595; AAI02596.1; -; mRNA.
DR   RefSeq; NP_001030255.1; NM_001035083.1.
DR   AlphaFoldDB; Q3T030; -.
DR   SMR; Q3T030; -.
DR   STRING; 9913.ENSBTAP00000012391; -.
DR   PaxDb; Q3T030; -.
DR   PeptideAtlas; Q3T030; -.
DR   PRIDE; Q3T030; -.
DR   Ensembl; ENSBTAT00000012391; ENSBTAP00000012391; ENSBTAG00000009414.
DR   GeneID; 510029; -.
DR   KEGG; bta:510029; -.
DR   CTD; 5704; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009414; -.
DR   VGNC; VGNC:33458; PSMC4.
DR   eggNOG; KOG0727; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_0_1; -.
DR   InParanoid; Q3T030; -.
DR   OMA; AYAAQVK; -.
DR   OrthoDB; 571919at2759; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000009414; Expressed in retina and 104 other tissues.
DR   ExpressionAtlas; Q3T030; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; 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:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR   GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; IPR035256; PSMC4.
DR   PANTHER; PTHR23073:SF120; PTHR23073:SF120; 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..418
FT                   /note="26S proteasome regulatory subunit 6B"
FT                   /id="PRO_0000249769"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P43686"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43686"
FT   MOD_RES         25
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P43686"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43686"
FT   MOD_RES         397
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43686"
FT   MOD_RES         401
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43686"
SQ   SEQUENCE   418 AA;  47366 MW;  80F9523C61B88F0C CRC64;
     MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY
     IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID
     RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMYADIGGM DIQKQEVREA
     VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL
     GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
     QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL
     EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK
 
 
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