ID   PSB8_PIG                Reviewed;         104 AA.
AC   Q29576;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Proteasome subunit beta type-8;
DE            EC=3.4.25.1;
DE   AltName: Full=Macropain subunit C13;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit C13;
DE   AltName: Full=Proteasome component C13;
DE   AltName: Full=Proteasome subunit beta-5i;
DE   Flags: Fragment;
GN   Name=PSMB8;
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: 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. May participate in the generation of spliced peptides
CC       resulting from the ligation of two separate proteasomal cleavage
CC       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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by interferon gamma (at protein level).
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; F14798; CAA23263.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000037739; -.
DR   PaxDb; 9823-ENSSSCP00000001580; -.
DR   PeptideAtlas; Q29576; -.
DR   eggNOG; KOG0175; Eukaryota.
DR   InParanoid; Q29576; -.
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:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
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; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   PANTHER; PTHR32194:SF1; PROTEASOME SUBUNIT BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Differentiation; Hydrolase; Immunity; Nucleus; Protease;
KW   Proteasome; Reference proteome; Threonine protease; Zymogen.
FT   CHAIN           <1..>104
FT                   /note="Proteasome subunit beta type-8"
FT                   /id="PRO_0000148074"
FT   NON_TER         1
FT   NON_TER         104
SQ   SEQUENCE   104 AA;  11604 MW;  E5EA18ABBA22189C CRC64;
     RLYYLRNGAR ISVSAASKLX SNMMYQYRGM GLSMGSMICG WDKKGPGLYY VDENGTRLSG
     NMFSTGSGNT YAYGVMDSGH RYDLSIEEAY DLGRRAIVHA THRD
//