ID   PSB1_RAT                Reviewed;         240 AA.
AC   P18421;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 3.
DT   08-NOV-2023, entry version 161.
DE   RecName: Full=Proteasome subunit beta type-1;
DE   AltName: Full=Macropain subunit C5;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit C5;
DE   AltName: Full=Proteasome component C5;
DE   AltName: Full=Proteasome gamma chain;
DE   Flags: Precursor;
GN   Name=Psmb1;
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 [MRNA].
RX   PubMed=2338147; DOI=10.1016/0014-5793(90)80773-c;
RA   Tamura T., Tanaka K., Kumatori A., Yamada F., Tsurumi C., Fujiwara T.,
RA   Ichihara A., Tokunaga F., Aruga R., Iwanaga S.;
RT   "cDNA cloning and sequencing of component C5 of proteasomes from rat
RT   hepatoma cells.";
RL   FEBS Lett. 264:91-94(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-47.
RC   TISSUE=Liver;
RX   PubMed=2335242; DOI=10.1016/0014-5793(90)81417-m;
RA   Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T.,
RA   Shimonishi Y.;
RT   "The NH2-terminal residues of rat liver proteasome (multicatalytic
RT   proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated.";
RL   FEBS Lett. 263:373-375(1990).
RN   [3]
RP   INDUCTION BY NICOTINE.
RX   PubMed=15582157; DOI=10.1016/j.molbrainres.2004.09.010;
RA   Kane J.K., Konu O., Ma J.Z., Li M.D.;
RT   "Nicotine coregulates multiple pathways involved in protein
RT   modification/degradation in rat brain.";
RL   Brain Res. Mol. Brain Res. 132:181-191(2004).
RN   [4]
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: Non-catalytic component of the 20S core proteasome complex
CC       involved in the proteolytic degradation of most intracellular proteins.
CC       This complex plays numerous essential roles within the cell by
CC       associating with different regulatory particles. Associated with two
CC       19S regulatory particles, forms the 26S proteasome and thus
CC       participates in the ATP-dependent degradation of ubiquitinated
CC       proteins. The 26S proteasome plays a key role in the maintenance of
CC       protein homeostasis by removing misfolded or damaged proteins that
CC       could impair cellular functions, and by removing proteins whose
CC       functions are no longer required. Associated with the PA200 or PA28,
CC       the 20S proteasome mediates ubiquitin-independent protein degradation.
CC       This type of proteolysis is required in several pathways including
CC       spermatogenesis (20S-PA200 complex) or generation of a subset of MHC
CC       class I-presented antigenic peptides (20S-PA28 complex).
CC       {ECO:0000250|UniProtKB:P20618}.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC       complex made of 28 subunits that are arranged in four stacked rings.
CC       The two outer rings are each formed by seven alpha subunits, and the
CC       two inner rings are formed by seven beta subunits. The proteolytic
CC       activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC       Interacts with SERPINB2. Interacts with RFPL4A.
CC       {ECO:0000250|UniProtKB:O09061, ECO:0000250|UniProtKB:P20618}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20618}. Nucleus
CC       {ECO:0000250|UniProtKB:P20618}. Note=Translocated from the cytoplasm
CC       into the nucleus following interaction with AKIRIN2, which bridges the
CC       proteasome with the nuclear import receptor IPO9.
CC       {ECO:0000250|UniProtKB:P20618}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: Up-regulated in prefrontal cortex (PFC) after nicotine
CC       exposure. Down-regulated by theophylline (THP) and 1,3-dinitrobenzene
CC       (DNB), two reprotoxic agents thought to induce infertility.
CC       {ECO:0000269|PubMed:15582157, ECO:0000269|PubMed:16988215}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; X52783; CAA36987.1; -; mRNA.
DR   PIR; S09696; S09696.
DR   RefSeq; NP_446042.1; NM_053590.1.
DR   PDB; 6EPC; EM; 12.30 A; 6=1-240.
DR   PDB; 6EPD; EM; 15.40 A; 6=1-240.
DR   PDB; 6EPE; EM; 12.80 A; 6=1-240.
DR   PDB; 6EPF; EM; 11.80 A; 6=1-240.
DR   PDB; 6TU3; EM; 2.70 A; M/a=1-240.
DR   PDBsum; 6EPC; -.
DR   PDBsum; 6EPD; -.
DR   PDBsum; 6EPE; -.
DR   PDBsum; 6EPF; -.
DR   PDBsum; 6TU3; -.
DR   AlphaFoldDB; P18421; -.
DR   SMR; P18421; -.
DR   BioGRID; 250178; 2.
DR   IntAct; P18421; 2.
DR   STRING; 10116.ENSRNOP00000002037; -.
DR   MEROPS; T01.986; -.
DR   GlyCosmos; P18421; 2 sites, No reported glycans.
DR   GlyGen; P18421; 2 sites.
DR   iPTMnet; P18421; -.
DR   PhosphoSitePlus; P18421; -.
DR   jPOST; P18421; -.
DR   PaxDb; 10116-ENSRNOP00000002037; -.
DR   GeneID; 94198; -.
DR   KEGG; rno:94198; -.
DR   UCSC; RGD:621092; rat.
DR   AGR; RGD:621092; -.
DR   CTD; 5689; -.
DR   RGD; 621092; Psmb1.
DR   eggNOG; KOG0179; Eukaryota.
DR   InParanoid; P18421; -.
DR   OrthoDB; 158278at2759; -.
DR   PhylomeDB; P18421; -.
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-174113; SCF-beta-TrCP mediated degradation of Emi1.
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-6798695; Neutrophil degranulation.
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:P18421; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
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:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   CDD; cd03757; proteasome_beta_type_1; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
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:SF2; PROTEASOME SUBUNIT BETA TYPE-1; 1.
DR   Pfam; PF00227; Proteasome; 1.
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; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Glycoprotein; Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT   PROPEP          1..27
FT                   /evidence="ECO:0000269|PubMed:2335242"
FT                   /id="PRO_0000259625"
FT   CHAIN           28..240
FT                   /note="Proteasome subunit beta type-1"
FT                   /id="PRO_0000148032"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         149
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O09061"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         203
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   CARBOHYD        57
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        208
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           85..106
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           112..125
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          148..151
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          157..168
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           169..179
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           195..210
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          218..225
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          231..236
FT                   /evidence="ECO:0007829|PDB:6TU3"
SQ   SEQUENCE   240 AA;  26479 MW;  B79EB682CDB95A01 CRC64;
     MLSTAAYRDP DRELVMGPQG SAGPVQMRFS PYAFNGGTVL AIAGEDFSIV ASDTRLSEGF
     SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS
     TILYSRRFFP YYVYNIIEGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV
     GFKNMQNVEH VPLTLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVPLRKD
//