ID   PSB1_BOVIN              Reviewed;         241 AA.
AC   Q2TBX6;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Proteasome subunit beta type-1;
DE   Flags: Precursor;
GN   Name=PSMB1;
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 MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-241 OF COMPLEX WITH 20S
RP   PROTEASOME.
RX   PubMed=12015144; DOI=10.1016/s0969-2126(02)00748-7;
RA   Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N.,
RA   Tsukihara T.;
RT   "The structure of the mammalian 20S proteasome at 2.75 A resolution.";
RL   Structure 10:609-618(2002).
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       (PubMed:12015144). Interacts with SERPINB2. Interacts with RFPL4A (By
CC       similarity). {ECO:0000250|UniProtKB:O09061,
CC       ECO:0000250|UniProtKB:P20618, ECO:0000269|PubMed:12015144}.
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   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; BC109494; AAI09495.1; -; mRNA.
DR   RefSeq; NP_001033628.1; NM_001038539.2.
DR   PDB; 1IRU; X-ray; 2.75 A; 1/M=29-241.
DR   PDB; 7DR6; EM; 4.10 A; J/U=1-241.
DR   PDB; 7DR7; EM; 3.30 A; J/U=1-241.
DR   PDB; 7DRW; EM; 4.20 A; U/m=1-241.
DR   PDBsum; 1IRU; -.
DR   PDBsum; 7DR6; -.
DR   PDBsum; 7DR7; -.
DR   PDBsum; 7DRW; -.
DR   AlphaFoldDB; Q2TBX6; -.
DR   SMR; Q2TBX6; -.
DR   IntAct; Q2TBX6; 1.
DR   STRING; 9913.ENSBTAP00000010108; -.
DR   MEROPS; T01.990; -.
DR   PaxDb; Q2TBX6; -.
DR   PeptideAtlas; Q2TBX6; -.
DR   PRIDE; Q2TBX6; -.
DR   GeneID; 514237; -.
DR   KEGG; bta:514237; -.
DR   CTD; 5689; -.
DR   eggNOG; KOG0179; Eukaryota.
DR   InParanoid; Q2TBX6; -.
DR   OrthoDB; 1092660at2759; -.
DR   EvolutionaryTrace; Q2TBX6; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR035202; Proteasome_beta1.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF59; PTHR11599:SF59; 1.
DR   Pfam; PF00227; Proteasome; 1.
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   3D-structure; Acetylation; Cytoplasm; Glycoprotein; Nucleus;
KW   Phosphoprotein; Proteasome; Reference proteome.
FT   PROPEP          1..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000259622"
FT   CHAIN           29..241
FT                   /note="Proteasome subunit beta type-1"
FT                   /id="PRO_0000239853"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         150
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O09061"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   MOD_RES         204
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20618"
FT   CARBOHYD        58
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        209
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           86..107
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   TURN            126..129
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          134..141
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          158..167
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           170..180
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           196..213
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          219..227
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          230..237
FT                   /evidence="ECO:0007829|PDB:1IRU"
SQ   SEQUENCE   241 AA;  26246 MW;  8682655C19CF2ACD CRC64;
     MLSSVAAYSG AGRDLAMEPH SSVGPLQLRF SPYAFNGGTV LAIAGEDFSI VASDTRLSEG
     FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL KMYKHSNNKA MTTGAIAAML
     STILYSRRFF PYYVYNIIGG LDEEGKGAVY SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ
     VGFKNMQNVE HVPLSLDRAM RLVKDVFISA AERDVYTGDA LKVCIVTKEG IRGETVPLRK
     D