PRS8_PIG
ID PRS8_PIG Reviewed; 406 AA.
AC P62197; O35051; P47210; P52915; P52916;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=Tat-binding protein homolog 10;
DE Short=TBP10;
DE AltName: Full=p45/SUG;
GN Name=PSMC5;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Brain, and Liver;
RX PubMed=8833236; DOI=10.1007/s003359900050;
RA Leeb T., Rettenberger G., Bruch J., Hameister H., Brenig B.;
RT "The porcine gene TBP10 encodes a protein homologous to the human Tat-
RT binding protein/26S protease subunit family.";
RL Mamm. Genome 7:180-185(1996).
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}.
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DR EMBL; X89718; CAA61863.1; -; Genomic_DNA.
DR EMBL; X89719; CAA61864.1; -; mRNA.
DR RefSeq; NP_999148.1; NM_213983.1.
DR AlphaFoldDB; P62197; -.
DR SMR; P62197; -.
DR IntAct; P62197; 1.
DR STRING; 9823.ENSSSCP00000018317; -.
DR PaxDb; P62197; -.
DR PeptideAtlas; P62197; -.
DR PRIDE; P62197; -.
DR Ensembl; ENSSSCT00005002597; ENSSSCP00005001507; ENSSSCG00005001713.
DR Ensembl; ENSSSCT00015067608; ENSSSCP00015027070; ENSSSCG00015050234.
DR Ensembl; ENSSSCT00035003982; ENSSSCP00035001339; ENSSSCG00035003144.
DR Ensembl; ENSSSCT00045047189; ENSSSCP00045032771; ENSSSCG00045027586.
DR Ensembl; ENSSSCT00060095990; ENSSSCP00060041515; ENSSSCG00060070251.
DR Ensembl; ENSSSCT00070010510; ENSSSCP00070008632; ENSSSCG00070005507.
DR GeneID; 397043; -.
DR KEGG; ssc:397043; -.
DR CTD; 5705; -.
DR eggNOG; KOG0728; Eukaryota.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; P62197; -.
DR OrthoDB; 571919at2759; -.
DR Reactome; R-SSC-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-SSC-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-SSC-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SSC-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-SSC-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-SSC-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-SSC-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-SSC-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-SSC-202424; Downstream TCR signaling.
DR Reactome; R-SSC-2467813; Separation of Sister Chromatids.
DR Reactome; R-SSC-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-SSC-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-SSC-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SSC-382556; ABC-family proteins mediated transport.
DR Reactome; R-SSC-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-SSC-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-SSC-4641257; Degradation of AXIN.
DR Reactome; R-SSC-4641258; Degradation of DVL.
DR Reactome; R-SSC-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-SSC-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-SSC-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-SSC-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-SSC-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-SSC-5632684; Hedgehog 'on' state.
DR Reactome; R-SSC-5658442; Regulation of RAS by GAPs.
DR Reactome; R-SSC-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SSC-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-SSC-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SSC-5689603; UCH proteinases.
DR Reactome; R-SSC-5689880; Ub-specific processing proteases.
DR Reactome; R-SSC-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SSC-68949; Orc1 removal from chromatin.
DR Reactome; R-SSC-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SSC-69481; G2/M Checkpoints.
DR Reactome; R-SSC-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SSC-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SSC-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-SSC-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SSC-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-SSC-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-SSC-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-SSC-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SSC-8951664; Neddylation.
DR Reactome; R-SSC-9020702; Interleukin-1 signaling.
DR Reactome; R-SSC-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SSC-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 12.
DR Genevisible; P62197; SS.
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_0000084723"
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
