PRS6A_MOUSE
ID PRS6A_MOUSE Reviewed; 442 AA.
AC O88685; Q99JN8;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=26S proteasome regulatory subunit 6A;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT5;
DE AltName: Full=Proteasome 26S subunit ATPase 3;
DE AltName: Full=Tat-binding protein 1;
DE Short=TBP-1;
GN Name=Psmc3; Synonyms=Tbp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=9714759; DOI=10.1016/s0167-4781(98)00105-5;
RA Nakamura T., Tanaka T., Takagi H., Sato M.;
RT "Cloning and heterogeneous in vivo expression of Tat binding protein-1
RT (TBP-1) in the mouse.";
RL Biochim. Biophys. Acta 1399:93-100(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10945464; DOI=10.1006/geno.2000.6231;
RA Sakao Y., Kawai T., Takeuchi O., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Takeda K., Akira S.;
RT "Mouse proteasomal ATPases Psmc3 and Psmc4: genomic organization and gene
RT targeting.";
RL Genomics 67:1-7(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CAST/EiJ; TISSUE=Brain;
RA Farber C.R., Corva P.M., Medrano J.F.;
RT "Characterization of quantitative trait loci influencing growth and
RT adiposity using congenic mouse strains.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in complex
RT with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
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. PSMC3 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:P17980}.
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 PSMC3 and
CC few additional components. Interacts with PAAF1.
CC {ECO:0000250|UniProtKB:P17980}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC Note=Colocalizes with TRIM5 in cytoplasmic bodies.
CC {ECO:0000269|PubMed:22078707}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; D49686; BAA32559.1; -; mRNA.
DR EMBL; AB040858; BAB16347.1; -; Genomic_DNA.
DR EMBL; AY902337; AAX90622.1; -; Genomic_DNA.
DR EMBL; AL691439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005783; AAH05783.1; -; mRNA.
DR CCDS; CCDS16423.1; -.
DR RefSeq; NP_032974.2; NM_008948.2.
DR AlphaFoldDB; O88685; -.
DR SMR; O88685; -.
DR BioGRID; 202428; 62.
DR IntAct; O88685; 4.
DR MINT; O88685; -.
DR STRING; 10090.ENSMUSP00000071054; -.
DR iPTMnet; O88685; -.
DR PhosphoSitePlus; O88685; -.
DR SwissPalm; O88685; -.
DR CPTAC; non-CPTAC-3856; -.
DR EPD; O88685; -.
DR jPOST; O88685; -.
DR MaxQB; O88685; -.
DR PaxDb; O88685; -.
DR PeptideAtlas; O88685; -.
DR PRIDE; O88685; -.
DR ProteomicsDB; 291805; -.
DR Antibodypedia; 1816; 549 antibodies from 36 providers.
DR DNASU; 19182; -.
DR Ensembl; ENSMUST00000067663; ENSMUSP00000071054; ENSMUSG00000002102.
DR GeneID; 19182; -.
DR KEGG; mmu:19182; -.
DR UCSC; uc008kuf.2; mouse.
DR CTD; 5702; -.
DR MGI; MGI:1098754; Psmc3.
DR VEuPathDB; HostDB:ENSMUSG00000002102; -.
DR eggNOG; KOG0652; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR InParanoid; O88685; -.
DR OMA; HEKAAMG; -.
DR OrthoDB; 571919at2759; -.
DR TreeFam; TF105648; -.
DR BRENDA; 5.6.1.5; 3474.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19182; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Psmc3; mouse.
DR PRO; PR:O88685; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88685; protein.
DR Bgee; ENSMUSG00000002102; Expressed in floor plate of midbrain and 285 other tissues.
DR ExpressionAtlas; O88685; baseline and differential.
DR Genevisible; O88685; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0043921; P:modulation by host of viral transcription; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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; IPR035254; PSMC3.
DR PANTHER; PTHR23073:SF90; PTHR23073:SF90; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT CHAIN 1..442
FT /note="26S proteasome regulatory subunit 6A"
FT /id="PRO_0000084699"
FT BINDING 230..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17980"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17980"
FT CONFLICT 170
FT /note="E -> D (in Ref. 1; BAA32559 and 2; BAB16347)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="C -> S (in Ref. 1; BAA32559 and 2; BAB16347)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="Y -> H (in Ref. 1; BAA32559 and 2; BAB16347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49549 MW; AECCFD5BAFF26C5B CRC64;
MQEMNLLPTP ESPVTRQEKM ATVWDEAEQD GIGEEVLKMS TEEIVQRTRL LDSEIKIMKS
EVLRVTHELQ AMKDKIKENS EKIKVNKTLP YLVSNVIELL DVDPNDQEED GANIDLDSQR
KGKCAVIKTS TRQTYFLPVI GLVDAEKLKP GDLVGVNKDS YLILETLPTE YDSRVKAMEV
DERPTEQYSD IGGLDKQIQE LVEAIVLPMN HKEKFENLGI QPPKGVLMYG PPGTGKTLLA
RACAAQTKAT FLKLAGPQLV QMFIGDGAKL VRDAFALAKE KAPSIIFIDE LDAIGTKRFD
SEKAGDREVQ RTMLELLNQL DGFQPNTQVK VIAATNRVDI LDPALLRSGR LDRKIEFPMP
NEEARARIMQ IHSRKMNVSP DVNYEELARC TDDFNGAQCK AVCVEAGMIA LRRGATELTH
EDYMEGILEV QAKKKANLQY YA
