PSB3_BOVIN
ID PSB3_BOVIN Reviewed; 205 AA.
AC P33672; Q3T059;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Proteasome subunit beta type-3;
DE AltName: Full=Proteasome chain 13;
DE AltName: Full=Proteasome component C10-II;
DE AltName: Full=Proteasome theta chain;
GN Name=PSMB3;
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=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 14-79; 89-114; 121-141; 160-170 AND 183-205.
RX PubMed=1510924; DOI=10.1021/bi00147a020;
RA Dick L.R., Moomaw C.R., Pramanik B.C., DeMartino G.N., Slaughter C.A.;
RT "Identification and localization of a cysteinyl residue critical for the
RT trypsin-like catalytic activity of the proteasome.";
RL Biochemistry 31:7347-7355(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH 20S 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 {ECO:0000250|UniProtKB:P49720}.
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:P49720}. Nucleus
CC {ECO:0000250|UniProtKB:P49720}. 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:P49720}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BC102554; AAI02555.1; -; mRNA.
DR PIR; A42762; A42762.
DR PIR; B42762; B42762.
DR PIR; C42762; C42762.
DR PIR; D42762; D42762.
DR PIR; G42762; G42762.
DR RefSeq; NP_001029768.1; NM_001034596.2.
DR PDB; 1IRU; X-ray; 2.75 A; J/X=1-205.
DR PDB; 7DR6; EM; 4.10 A; H/S=1-205.
DR PDB; 7DR7; EM; 3.30 A; H/S=1-205.
DR PDB; 7DRW; EM; 4.20 A; S/k=1-205.
DR PDBsum; 1IRU; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DR7; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; P33672; -.
DR SMR; P33672; -.
DR STRING; 9913.ENSBTAP00000004984; -.
DR MEROPS; T01.983; -.
DR PaxDb; P33672; -.
DR PeptideAtlas; P33672; -.
DR PRIDE; P33672; -.
DR Ensembl; ENSBTAT00000004984; ENSBTAP00000004984; ENSBTAG00000003830.
DR Ensembl; ENSBTAT00000073382; ENSBTAP00000061900; ENSBTAG00000003830.
DR GeneID; 533874; -.
DR KEGG; bta:533874; -.
DR CTD; 5691; -.
DR VEuPathDB; HostDB:ENSBTAG00000003830; -.
DR VGNC; VGNC:33447; PSMB3.
DR eggNOG; KOG0180; Eukaryota.
DR GeneTree; ENSGT00550000074820; -.
DR HOGENOM; CLU_035750_10_0_1; -.
DR InParanoid; P33672; -.
DR OMA; GWGAIVH; -.
DR OrthoDB; 1170036at2759; -.
DR TreeFam; TF106216; -.
DR EvolutionaryTrace; P33672; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000003830; Expressed in oocyte and 104 other tissues.
DR ExpressionAtlas; P33672; 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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03759; proteasome_beta_type_3; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR033811; Proteasome_beta_3.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF62; PTHR11599:SF62; 1.
DR Pfam; PF00227; Proteasome; 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; Direct protein sequencing; Nucleus;
KW Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49720"
FT CHAIN 2..205
FT /note="Proteasome subunit beta type-3"
FT /id="PRO_0000148056"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P49720"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49720"
FT CONFLICT 89
FT /note="S -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 57..77
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1IRU"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:1IRU"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1IRU"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:7DR7"
FT STRAND 185..200
FT /evidence="ECO:0007829|PDB:1IRU"
SQ SEQUENCE 205 AA; 22993 MW; 62551E484D5042FD CRC64;
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV
QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF
ICSLDLIGCP MVTDDFVVSG TCTEQMYGMC ESLWEPNMDP EHLFETISQA MLNAVDRDAV
SGMGVIVHII EKDKITTRTL KARMD
