PSB7_BOVIN
ID PSB7_BOVIN Reviewed; 277 AA.
AC Q2TBP0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Proteasome subunit beta type-7;
DE EC=3.4.25.1;
DE Flags: Precursor;
GN Name=PSMB7;
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 44-277 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: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a
CC trypsin-like activity. {ECO:0000250|UniProtKB:Q99436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:Q99436};
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 {ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99436}. Nucleus
CC {ECO:0000250|UniProtKB:Q99436}. 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:Q99436}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BC109868; AAI09869.1; -; mRNA.
DR RefSeq; NP_001033616.1; NM_001038527.2.
DR PDB; 1IRU; X-ray; 2.75 A; I/W=44-277.
DR PDBsum; 1IRU; -.
DR AlphaFoldDB; Q2TBP0; -.
DR SMR; Q2TBP0; -.
DR STRING; 9913.ENSBTAP00000003990; -.
DR MEROPS; T01.A02; -.
DR PaxDb; Q2TBP0; -.
DR PRIDE; Q2TBP0; -.
DR GeneID; 511207; -.
DR KEGG; bta:511207; -.
DR CTD; 5695; -.
DR eggNOG; KOG0173; Eukaryota.
DR InParanoid; Q2TBP0; -.
DR OrthoDB; 977476at2759; -.
DR EvolutionaryTrace; Q2TBP0; -.
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:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
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; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035216; Proteasome_beta7.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF42; PTHR11599:SF42; 1.
DR Pfam; PF12465; Pr_beta_C; 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 3D-structure; Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..43
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000329062"
FT CHAIN 44..277
FT /note="Proteasome subunit beta type-7"
FT /id="PRO_0000329063"
FT ACT_SITE 44
FT /note="Nucleophile"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 277 AA; 30009 MW; C3DE3CB1782AEBB3 CRC64;
MAAVSVYERP VGGFSFDNCR RNAVLEADFA KKGYKLPTAR KTGTTIAGVV YKDGIVLGAD
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LSTGRLPRVV
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDKFRPDME EEEAKKLVSE AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PYSVPNKKGT
RFGRYRCEKG TNAVLTEKVT TLEIEVLEET VQTMDTS
