ID   PSB3_PICMA              Reviewed;         204 AA.
AC   O65084;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Proteasome subunit beta type-3;
DE   AltName: Full=20S proteasome alpha subunit C;
DE   AltName: Full=20S proteasome subunit beta-3;
GN   Name=PBC1; Synonyms=SB65;
OS   Picea mariana (Black spruce) (Abies mariana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9611216; DOI=10.1093/genetics/149.2.1089;
RA   Perry D.J., Bousquet J.;
RT   "Sequence-tagged-site (STS) markers of arbitrary genes: development,
RT   characterization and analysis of linkage in black spruce.";
RL   Genetics 149:1089-1098(1998).
CC   -!- FUNCTION: Non-catalytic component of the proteasome, a multicatalytic
CC       proteinase complex which is characterized by its ability to cleave
CC       peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC       at neutral or slightly basic pH. The proteasome has an ATP-dependent
CC       proteolytic activity.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
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; AF051246; AAC32146.1; -; mRNA.
DR   AlphaFoldDB; O65084; -.
DR   SMR; O65084; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
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   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..204
FT                   /note="Proteasome subunit beta type-3"
FT                   /id="PRO_0000148068"
SQ   SEQUENCE   204 AA;  22908 MW;  F6F92CEB4BDC17A6 CRC64;
     MSIFEYNGSA LVAMVGKNCF AIASDRRLGV QLQTIATDFQ RIFKIHDKLY VGLSGLATDV
     QTLYQRFAFR HKLYQLREER NMRPETFASL VSALLYEKRF GPYFCQPVIA GLGEDDKPFI
     CTMDSIGAKE LAKDFVVAGT AAESLYGACE SMYKPDMEPE ELFETISQAL LSSIDRDCLS
     GWGGHVYVVS PNQVIERTLK GRMD