ID PSB8_BOVIN Reviewed; 276 AA. AC Q3T112; Q32S32; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 2. DT 24-JAN-2024, entry version 131. DE RecName: Full=Proteasome subunit beta type-8; DE EC=3.4.25.1; DE AltName: Full=Proteasome subunit beta-5i; DE Flags: Precursor; GN Name=PSMB8; 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 GENOMIC DNA]. RX PubMed=16573526; DOI=10.1111/j.1365-2052.2005.01395.x; RA Childers C.P., Newkirk H.L., Honeycutt D.A., Ramlachan N., Muzney D.M., RA Sodergren E., Gibbs R.A., Weinstock G.M., Womack J.E., Skow L.C.; RT "Comparative analysis of the bovine MHC class IIb sequence identifies RT inversion breakpoints and three unexpected genes."; RL Anim. Genet. 37:121-129(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). May participate in the generation of spliced CC peptides resulting from the ligation of two separate proteasomal CC cleavage 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. CC Nucleus {ECO:0000250}. CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level). 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 -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- CC ProRule:PRU00809}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY957499; AAY34697.1; -; Genomic_DNA. DR EMBL; BC102170; AAI02171.1; -; mRNA. DR RefSeq; NP_001035570.1; NM_001040480.2. DR RefSeq; XP_005223251.1; XM_005223194.2. DR PDB; 7DR6; EM; 4.10 A; 2/Y=1-276. DR PDB; 7DR7; EM; 3.30 A; 2/Y=1-276. DR PDB; 7DRW; EM; 4.20 A; 2/Y=1-276. DR PDBsum; 7DR6; -. DR PDBsum; 7DR7; -. DR PDBsum; 7DRW; -. DR AlphaFoldDB; Q3T112; -. DR EMDB; EMD-30824; -. DR EMDB; EMD-30825; -. DR EMDB; EMD-30828; -. DR SMR; Q3T112; -. DR IntAct; Q3T112; 1. DR STRING; 9913.ENSBTAP00000003955; -. DR MEROPS; T01.012; -. DR PaxDb; 9913-ENSBTAP00000003955; -. DR Ensembl; ENSBTAT00000003955.6; ENSBTAP00000003955.5; ENSBTAG00000003039.6. DR GeneID; 282013; -. DR KEGG; bta:282013; -. DR CTD; 5696; -. DR VEuPathDB; HostDB:ENSBTAG00000003039; -. DR VGNC; VGNC:33452; PSMB8. DR eggNOG; KOG0175; Eukaryota. DR GeneTree; ENSGT00940000157293; -. DR HOGENOM; CLU_035750_7_1_1; -. DR InParanoid; Q3T112; -. DR OMA; IQIEMAH; -. DR OrthoDB; 4492251at2759; -. DR TreeFam; TF106223; -. DR Reactome; R-BTA-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-BTA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-BTA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-BTA-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-BTA-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-BTA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-BTA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-BTA-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-BTA-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-BTA-202424; Downstream TCR signaling. DR Reactome; R-BTA-2467813; Separation of Sister Chromatids. DR Reactome; R-BTA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-BTA-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-BTA-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-BTA-382556; ABC-family proteins mediated transport. DR Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-BTA-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-BTA-4641257; Degradation of AXIN. DR Reactome; R-BTA-4641258; Degradation of DVL. DR Reactome; R-BTA-5358346; Hedgehog ligand biogenesis. DR Reactome; R-BTA-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-BTA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-BTA-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-BTA-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-BTA-5632684; Hedgehog 'on' state. DR Reactome; R-BTA-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-BTA-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-BTA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-BTA-5689603; UCH proteinases. DR Reactome; R-BTA-5689880; Ub-specific processing proteases. DR Reactome; R-BTA-68867; Assembly of the pre-replicative complex. DR Reactome; R-BTA-68949; Orc1 removal from chromatin. DR Reactome; R-BTA-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-BTA-69481; G2/M Checkpoints. DR Reactome; R-BTA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-BTA-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-BTA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-BTA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-BTA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-BTA-8939902; Regulation of RUNX2 expression and activity. DR Reactome; R-BTA-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-BTA-8948751; Regulation of PTEN stability and activity. DR Reactome; R-BTA-8951664; Neddylation. DR Reactome; R-BTA-9020702; Interleukin-1 signaling. DR Reactome; R-BTA-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-BTA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000003039; Expressed in blood and 106 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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; IEA:Ensembl. DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR CDD; cd03761; proteasome_beta_type_5; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1. DR PANTHER; PTHR32194:SF1; PROTEASOME SUBUNIT BETA; 1. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS00854; PROTEASOME_BETA_1; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Differentiation; Hydrolase; Immunity; Nucleus; KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen. FT PROPEP 1..72 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000239856" FT CHAIN 73..276 FT /note="Proteasome subunit beta type-8" FT /id="PRO_0000239857" 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 10..11 FT /note="PG -> TR (in Ref. 2; AAI02171)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="L -> F (in Ref. 2; AAI02171)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="A -> D (in Ref. 2; AAI02171)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="L -> Q (in Ref. 2; AAI02171)" FT /evidence="ECO:0000305" FT CONFLICT 187..189 FT /note="DEN -> NDS (in Ref. 2; AAI02171)" FT /evidence="ECO:0000305" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:7DR7" FT HELIX 121..141 FT /evidence="ECO:0007829|PDB:7DR7" FT HELIX 148..161 FT /evidence="ECO:0007829|PDB:7DR7" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 183..186 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:7DR7" FT HELIX 204..211 FT /evidence="ECO:0007829|PDB:7DR7" FT TURN 212..214 FT /evidence="ECO:0007829|PDB:7DR7" FT HELIX 221..238 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 244..250 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:7DR7" FT HELIX 264..271 FT /evidence="ECO:0007829|PDB:7DR7" SQ SEQUENCE 276 AA; 30268 MW; 5FE3755A1C1BF361 CRC64; MALLDVCGAP GGQRGDWAVP LAGSRQRSDP GHYGFSLRSP ELALPRGMQP TEFFRSLGGN GESKVQIEMA HGTTTLAFKF QHGVIVAVDS RASAGNYIAT LKVNKVIEIN PYLLGTMSGC AADCLYWERL LAKECRLYYL RNGERISVSA ASKLLSNMMC QYRGMGLSMG SMICGWDKKG PGLYYVDENG TRLSGNMFST GSGNSHAYGV MDSGYRPDLS IEEAYDLGRR AIVHATHRDS YSGGVVNMYH MKEDGWVKVE STDVSDLMHQ YREASQ //