PSB6_BOVIN
ID PSB6_BOVIN Reviewed; 239 AA.
AC Q3MHN0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Proteasome subunit beta type-6;
DE EC=3.4.25.1 {ECO:0000250|UniProtKB:P28072};
DE Flags: Precursor;
GN Name=PSMB6;
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=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 35-239 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, PSMB6 displays a
CC peptidylglutamyl-hydrolyzing activity also termed postacidic or
CC caspase-like activity, meaning that the peptides bond hydrolysis occurs
CC directly after acidic residues. {ECO:0000250|UniProtKB:P28072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:P28072};
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:P28072}. Nucleus
CC {ECO:0000250|UniProtKB:P28072}. 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:P28072}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BC105176; AAI05177.1; -; mRNA.
DR RefSeq; NP_001029541.1; NM_001034369.2.
DR PDB; 1IRU; X-ray; 2.75 A; H/V=35-238.
DR PDBsum; 1IRU; -.
DR AlphaFoldDB; Q3MHN0; -.
DR SMR; Q3MHN0; -.
DR STRING; 9913.ENSBTAP00000017816; -.
DR MEROPS; T01.020; -.
DR PaxDb; Q3MHN0; -.
DR PeptideAtlas; Q3MHN0; -.
DR PRIDE; Q3MHN0; -.
DR Ensembl; ENSBTAT00000017816; ENSBTAP00000017816; ENSBTAG00000013390.
DR GeneID; 510069; -.
DR KEGG; bta:510069; -.
DR CTD; 5694; -.
DR VEuPathDB; HostDB:ENSBTAG00000013390; -.
DR VGNC; VGNC:33450; PSMB6.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000155114; -.
DR HOGENOM; CLU_035750_5_2_1; -.
DR InParanoid; Q3MHN0; -.
DR OMA; HKQAYAI; -.
DR OrthoDB; 1172133at2759; -.
DR TreeFam; TF106221; -.
DR EvolutionaryTrace; Q3MHN0; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000013390; Expressed in laryngeal cartilage and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035140; Proteasome_beta6.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF46; PTHR11599:SF46; 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; Acetylation; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT PROPEP 2..34
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239858"
FT CHAIN 35..239
FT /note="Proteasome subunit beta type-6"
FT /id="PRO_0000239859"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 83..104
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 239 AA; 25542 MW; 88BCDA9DF8D7FDAB CRC64;
MAATLVAARG TRPAPAWGPE AIAPDWENRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI
ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH SIELNEPPLV HTAASLFKEM
CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM GGMMVRQPFA IGGSGSSYIY GYVDATYREG
MTKEECLQFT ANALALAMER DGSSGGVIRL AAIAEPGVER QVLLGDQIPK FTIATLPPL
