ID   PSB4_XENLA              Reviewed;         242 AA.
AC   P28024;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Proteasome subunit beta type-4;
DE   AltName: Full=Macropain beta chain;
DE   AltName: Full=Multicatalytic endopeptidase complex beta chain;
DE   AltName: Full=Proteasome beta chain;
DE   AltName: Full=Proteasome chain 3;
DE   Flags: Precursor; Fragment;
GN   Name=psmb4;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=1936248; DOI=10.1016/0014-5793(91)81098-s;
RA   van Riel M.C.H.M., Martens G.J.M.;
RT   "Cloning and sequence analysis of pituitary cDNA encoding the beta-subunit
RT   of Xenopus proteasome.";
RL   FEBS Lett. 291:37-40(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44593.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X62709; CAA44593.1; ALT_INIT; mRNA.
DR   PIR; S17568; S17568.
DR   AlphaFoldDB; P28024; -.
DR   SMR; P28024; -.
DR   MEROPS; T01.987; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   PROPEP          <1..23
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026587"
FT   CHAIN           24..242
FT                   /note="Proteasome subunit beta type-4"
FT                   /id="PRO_0000026588"
FT   ACT_SITE        24
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   242 AA;  26759 MW;  DCEB9D1A13C61D3E CRC64;
     ESVARGTAPG ELHCFPGAGP VRHTLNPMVT GTSVLGVKFD GGVIIAADML GSYGSLARFR
     NISRIMKVNE NTILGASGDY ADYQYLKQVI DQMVIDEELV GDGHNYSPKA IHSWLTRVMY
     NRRSKMNPLW NTVVIGGFYN GESFLGYVDK LGVAYEAPTI ATGFGAYLAQ PLLREVTENK
     ATLSKEEARQ LVDRCMKVLY YRDARSYNRF EITTVTESGV EVEGPLSSET NWEIAHLISG
     FE