ID   PSB4_PIG                Reviewed;         154 AA.
AC   Q29384;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 125.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
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       SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300
CC       repressor SNIP1. {ECO:0000250|UniProtKB:P28070}.
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       Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is
CC       incorporated into the 20S proteasome. Interacts with PRPF19.
CC       {ECO:0000250|UniProtKB:P28070}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28070}. Nucleus
CC       {ECO:0000250|UniProtKB:P28070}. 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:P28070}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; F14598; CAA23147.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000049519; -.
DR   MEROPS; T01.987; -.
DR   PaxDb; 9823-ENSSSCP00000007062; -.
DR   PeptideAtlas; Q29384; -.
DR   eggNOG; KOG0185; Eukaryota.
DR   InParanoid; Q29384; -.
DR   ChiTaRS; PSMB4; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
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   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   PANTHER; PTHR32194:SF6; PROTEASOME SUBUNIT BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Proteasome;
KW   Reference proteome.
FT   PROPEP          1..45
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026585"
FT   CHAIN           46..>154
FT                   /note="Proteasome subunit beta type-4"
FT                   /id="PRO_0000026586"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P28070"
FT   MOD_RES         102
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P28070"
FT   NON_TER         154
SQ   SEQUENCE   154 AA;  16928 MW;  D36DC15FBA1E6B44 CRC64;
     MESILESRSG HWAGGPAPGQ FYRIPPTPGS IVDPXSVLYG SPITRTQNPM VTGTSVLGVK
     FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG DYADFQYLKQ VLGQMVIDEE
     LLGDGHSYSP KAIHSWLTRA MYNRRFKMNP LWTT
//