PSB8_BOVIN
ID PSB8_BOVIN Reviewed; 276 AA.
AC Q3T112; Q32S32;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Proteasome subunit beta type-8;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome subunit beta-5i;
DE Flags: Precursor;
GN Name=PSMB8;
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 GENOMIC DNA].
RX PubMed=16573526; DOI=10.1111/j.1365-2052.2005.01395.x;
RA Childers C.P., Newkirk H.L., Honeycutt D.A., Ramlachan N., Muzney D.M.,
RA Sodergren E., Gibbs R.A., Weinstock G.M., Womack J.E., Skow L.C.;
RT "Comparative analysis of the bovine MHC class IIb sequence identifies
RT inversion breakpoints and three unexpected genes.";
RL Anim. Genet. 37:121-129(2006).
RN [2]
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). May participate in the generation of spliced
CC peptides resulting from the ligation of two separate proteasomal
CC cleavage products that are not contiguous in the parental protein (By
CC similarity). Required for adipocyte differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P28062}.
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 PSMB5. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. Directly interacts with POMP.
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}.
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DR EMBL; AY957499; AAY34697.1; -; Genomic_DNA.
DR EMBL; BC102170; AAI02171.1; -; mRNA.
DR RefSeq; NP_001035570.1; NM_001040480.2.
DR RefSeq; XP_005223251.1; XM_005223194.2.
DR PDB; 7DR6; EM; 4.10 A; 2/Y=1-276.
DR PDB; 7DR7; EM; 3.30 A; 2/Y=1-276.
DR PDB; 7DRW; EM; 4.20 A; 2/Y=1-276.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q3T112; -.
DR SMR; Q3T112; -.
DR IntAct; Q3T112; 1.
DR STRING; 9913.ENSBTAP00000003955; -.
DR MEROPS; T01.012; -.
DR PaxDb; Q3T112; -.
DR PRIDE; Q3T112; -.
DR Ensembl; ENSBTAT00000003955; ENSBTAP00000003955; ENSBTAG00000003039.
DR GeneID; 282013; -.
DR KEGG; bta:282013; -.
DR CTD; 5696; -.
DR VEuPathDB; HostDB:ENSBTAG00000003039; -.
DR VGNC; VGNC:33452; PSMB8.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000157293; -.
DR HOGENOM; CLU_035750_7_1_1; -.
DR InParanoid; Q3T112; -.
DR OMA; IQIEMAH; -.
DR OrthoDB; 929961at2759; -.
DR TreeFam; TF106223; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000003039; Expressed in blood and 106 other tissues.
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:0019882; P:antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0052548; P:regulation of endopeptidase activity; IEA:Ensembl.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035705; Proteasome_beta8.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF53; PTHR11599:SF53; 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; Differentiation; Hydrolase; Immunity; Nucleus;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239856"
FT CHAIN 73..276
FT /note="Proteasome subunit beta type-8"
FT /id="PRO_0000239857"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 72..73
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT CONFLICT 10..11
FT /note="PG -> TR (in Ref. 2; AAI02171)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="L -> F (in Ref. 2; AAI02171)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> D (in Ref. 2; AAI02171)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="L -> Q (in Ref. 2; AAI02171)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..189
FT /note="DEN -> NDS (in Ref. 2; AAI02171)"
FT /evidence="ECO:0000305"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 121..141
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:7DR7"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 221..238
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:7DR7"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:7DR7"
SQ SEQUENCE 276 AA; 30268 MW; 5FE3755A1C1BF361 CRC64;
MALLDVCGAP GGQRGDWAVP LAGSRQRSDP GHYGFSLRSP ELALPRGMQP TEFFRSLGGN
GESKVQIEMA HGTTTLAFKF QHGVIVAVDS RASAGNYIAT LKVNKVIEIN PYLLGTMSGC
AADCLYWERL LAKECRLYYL RNGERISVSA ASKLLSNMMC QYRGMGLSMG SMICGWDKKG
PGLYYVDENG TRLSGNMFST GSGNSHAYGV MDSGYRPDLS IEEAYDLGRR AIVHATHRDS
YSGGVVNMYH MKEDGWVKVE STDVSDLMHQ YREASQ
