PSB8_RAT
ID PSB8_RAT Reviewed; 276 AA.
AC P28064; Q6MGA4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Proteasome subunit beta type-8;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C13;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C13;
DE AltName: Full=Proteasome component C13;
DE AltName: Full=Proteasome subunit beta-5i;
DE Flags: Precursor;
GN Name=Psmb8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-276.
RX PubMed=1451788; DOI=10.1016/0014-5793(92)80211-x;
RA Aki M., Tamura T., Fuminori T., Iwanaga S., Kawamura Y., Shimbara N.,
RA Kagawa S., Tanaka K., Ichihara A.;
RT "cDNA cloning of rat proteasome subunit RC1, a homologue of RING10 located
RT in the human MHC class II region.";
RL FEBS Lett. 301:65-68(1992).
RN [3]
RP INDUCTION BY THP AND DNB.
RX PubMed=16988215; DOI=10.1095/biolreprod.106.053173;
RA Tengowski M.W., Feng D., Sutovsky M., Sutovsky P.;
RT "Differential expression of genes encoding constitutive and inducible 20S
RT proteasomal core subunits in the testis and epididymis of theophylline- or
RT 1,3-dinitrobenzene-exposed rats.";
RL Biol. Reprod. 76:149-163(2007).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides. May participate in the generation of spliced peptides
CC resulting from the ligation of two separate proteasomal cleavage
CC products that are not contiguous in the parental protein (By
CC similarity). Required for adipocyte differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P28062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB5. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. Directly interacts with POMP (By similarity). Interacts with
CC TAP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level). Down-
CC regulated by theophylline (THP), a reprotoxic agent thought to induce
CC infertility. {ECO:0000269|PubMed:16988215}.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- MISCELLANEOUS: Encoded in the MHC class II region.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BX883043; CAE83942.1; -; Genomic_DNA.
DR EMBL; D10729; BAA01572.1; -; mRNA.
DR PIR; S21126; S21126.
DR RefSeq; NP_542945.2; NM_080767.2.
DR AlphaFoldDB; P28064; -.
DR SMR; P28064; -.
DR STRING; 10116.ENSRNOP00000000528; -.
DR MEROPS; T01.012; -.
DR PhosphoSitePlus; P28064; -.
DR jPOST; P28064; -.
DR PaxDb; P28064; -.
DR PRIDE; P28064; -.
DR GeneID; 24968; -.
DR KEGG; rno:24968; -.
DR UCSC; RGD:3426; rat.
DR CTD; 5696; -.
DR RGD; 3426; Psmb8.
DR VEuPathDB; HostDB:ENSRNOG00000000456; -.
DR eggNOG; KOG0175; Eukaryota.
DR HOGENOM; CLU_035750_7_1_1; -.
DR InParanoid; P28064; -.
DR OMA; IQIEMAH; -.
DR OrthoDB; 929961at2759; -.
DR PhylomeDB; P28064; -.
DR TreeFam; TF106223; -.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-RNO-4641257; Degradation of AXIN.
DR Reactome; R-RNO-4641258; Degradation of DVL.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-69481; G2/M Checkpoints.
DR Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P28064; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000456; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P28064; baseline and differential.
DR Genevisible; P28064; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:RGD.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035705; Proteasome_beta8.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF53; PTHR11599:SF53; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Hydrolase; Immunity; Nucleus; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026601"
FT CHAIN 73..276
FT /note="Proteasome subunit beta type-8"
FT /id="PRO_0000026602"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 72..73
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT CONFLICT 6
FT /note="L -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..24
FT /note="EWAAVDAGS -> SGLAVDAE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="L -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 30570 MW; 0955C80D2F969A97 CRC64;
MALLDLCGAP RGQRPEWAAV DAGSGLRSDP GHYSFSVQAP ELALPRGMQP TEFLRSFGDD
QERKVQIEMA HGTTTLAFKF QHGVIVAVDS RASAGSYIAT IRVNKVIEIN PYLLGTMSGC
AADCQYWERL LAKECRLYYL RNGERISVSA ASKLLSNMML QYRGMGLSMG SMICGWDKKG
PGLYYVDDNG TRLSGQMFST GSGNTYAYGV MDSGYRQDLS PEEAYDLARR AIVYATHRDS
YSGGVVNMYH MKKDGWVKVE STDVSDLLHK YREATL
