PSB10_BOVIN
ID PSB10_BOVIN Reviewed; 273 AA.
AC Q3T0T1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Proteasome subunit beta type-10;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome subunit beta-2i;
DE Flags: Precursor;
GN Name=PSMB10;
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.
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB7. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level).
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102272; AAI02273.1; -; mRNA.
DR RefSeq; NP_001029212.1; NM_001034040.2.
DR PDB; 7DR6; EM; 4.10 A; 1/X=1-273.
DR PDB; 7DR7; EM; 3.30 A; 1/X=1-273.
DR PDB; 7DRW; EM; 4.20 A; 1/X=1-273.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3T0T1; -.
DR SMR; Q3T0T1; -.
DR IntAct; Q3T0T1; 1.
DR STRING; 9913.ENSBTAP00000024015; -.
DR MEROPS; T01.014; -.
DR PaxDb; Q3T0T1; -.
DR PeptideAtlas; Q3T0T1; -.
DR PRIDE; Q3T0T1; -.
DR Ensembl; ENSBTAT00000024015; ENSBTAP00000024015; ENSBTAG00000018040.
DR GeneID; 282328; -.
DR KEGG; bta:282328; -.
DR CTD; 5699; -.
DR VEuPathDB; HostDB:ENSBTAG00000018040; -.
DR VGNC; VGNC:97305; PSMB10.
DR eggNOG; KOG0173; Eukaryota.
DR GeneTree; ENSGT00940000161047; -.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; Q3T0T1; -.
DR OMA; RVSYGFY; -.
DR OrthoDB; 977476at2759; -.
DR TreeFam; TF106222; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000018040; Expressed in blood and 106 other tissues.
DR ExpressionAtlas; Q3T0T1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:1990111; C:spermatoproteasome 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:0002376; P:immune system process; IEA:InterPro.
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; IPR034384; Proteasome_beta2/10.
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:SF41; PTHR11599:SF41; 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; Acetylation; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..39
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239850"
FT CHAIN 40..273
FT /note="Proteasome subunit beta type-10"
FT /id="PRO_0000239851"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 39..40
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P40306"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40306"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 187..202
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:7DR7"
SQ SEQUENCE 273 AA; 29099 MW; 8868CF63F4B412A6 CRC64;
MQKTVLEPQR GFSFENCERN AALQRALPGL RVPHARKTGT TIAGLVFQDG VILGADTRAT
NDSVVADKIC EKIHFIAPKI YCCGAGVAAD AEMTTRMAAS NMELHALSTG RECRVATVTR
MLRQTLFRYQ GYVGASLIVG GVDFTGPQLY SVHPHGSYSR LPFTALGSGQ DAAIAVLEDR
FQPNMTLEAA QELLVEAITA GILGDLGSGG NVDACVITAA GAKMLRALSS PTKPIERSSQ
YRFAPGTTPV LSQTVVPLTL ELVEETVQAM DVE
