PSB4_BOVIN
ID PSB4_BOVIN Reviewed; 264 AA.
AC Q3T108;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Proteasome subunit beta type-4;
DE Flags: Precursor;
GN Name=PSMB4;
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 (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 46-264 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 SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300
CC repressor SNIP1. {ECO:0000250|UniProtKB:P28070}.
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). Forms a ternary complex with SMAD1 and OAZ1 before
CC PSMB4 is incorporated into the 20S proteasome (By similarity).
CC Interacts with PRPF19 (By similarity). {ECO:0000250|UniProtKB:P28070,
CC ECO:0000269|PubMed:12015144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28070}. Nucleus
CC {ECO:0000250|UniProtKB:P28070}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BC102182; AAI02183.1; -; mRNA.
DR RefSeq; NP_001029438.1; NM_001034266.2.
DR PDB; 1IRU; X-ray; 2.75 A; 2/N=46-264.
DR PDB; 7DR6; EM; 4.10 A; K/V=1-264.
DR PDB; 7DR7; EM; 3.30 A; K/V=1-264.
DR PDB; 7DRW; EM; 4.20 A; V/n=1-264.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3T108; -.
DR SMR; Q3T108; -.
DR STRING; 9913.ENSBTAP00000028364; -.
DR MEROPS; T01.987; -.
DR PaxDb; Q3T108; -.
DR PeptideAtlas; Q3T108; -.
DR PRIDE; Q3T108; -.
DR Ensembl; ENSBTAT00000028364; ENSBTAP00000028364; ENSBTAG00000021288.
DR GeneID; 506203; -.
DR KEGG; bta:506203; -.
DR CTD; 5692; -.
DR VEuPathDB; HostDB:ENSBTAG00000021288; -.
DR VGNC; VGNC:33448; PSMB4.
DR eggNOG; KOG0185; Eukaryota.
DR GeneTree; ENSGT00390000000698; -.
DR HOGENOM; CLU_072435_2_0_1; -.
DR InParanoid; Q3T108; -.
DR OMA; KGYGTQT; -.
DR OrthoDB; 1228942at2759; -.
DR TreeFam; TF106220; -.
DR EvolutionaryTrace; Q3T108; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021288; Expressed in tongue muscle and 104 other tissues.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR CDD; cd03760; proteasome_beta_type_4; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016295; Proteasome_beta4.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF5; PTHR11599:SF5; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF001213; Psome_endopept_beta; 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; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT PROPEP 1..45
FT /evidence="ECO:0000250"
FT /id="PRO_0000239854"
FT CHAIN 46..264
FT /note="Proteasome subunit beta type-4"
FT /id="PRO_0000239855"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P28070"
FT MOD_RES 102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P28070"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 102..122
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 207..224
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 264 AA; 29031 MW; B2C4029A25FCC76A CRC64;
MEALLESRSG LWAGGPAPGQ FYRIPPTPGS SVDPVSALYG SPITRTQNPM VTGTSVLGLK
FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG DYADFQYLKQ VLGQMVIDEE
LLGDGHSYSP KAIHSWLTRA MYSRRSKMNP LWNTMVIGGY ADGESFLGYV DMLGVAYEAP
SLATGYGAYL AQPLLREVLE KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK
GVEIEGPLSA ETNWDIAHMI SGFE
