ID   PSB3_SCHPO              Reviewed;         204 AA.
AC   Q9Y7T8;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Probable proteasome subunit beta type-3;
GN   Name=pup3; ORFNames=SPCC63.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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 (By similarity). {ECO:0000250}.
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       ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
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; CU329672; CAB40016.1; -; Genomic_DNA.
DR   PIR; T41513; T41513.
DR   RefSeq; NP_587985.1; NM_001022976.2.
DR   AlphaFoldDB; Q9Y7T8; -.
DR   SMR; Q9Y7T8; -.
DR   BioGRID; 275966; 9.
DR   STRING; 4896.SPCC63.12c.1; -.
DR   iPTMnet; Q9Y7T8; -.
DR   MaxQB; Q9Y7T8; -.
DR   PaxDb; Q9Y7T8; -.
DR   EnsemblFungi; SPCC63.12c.1; SPCC63.12c.1:pep; SPCC63.12c.
DR   GeneID; 2539401; -.
DR   KEGG; spo:SPCC63.12c; -.
DR   PomBase; SPCC63.12c; pup3.
DR   VEuPathDB; FungiDB:SPCC63.12c; -.
DR   eggNOG; KOG0180; Eukaryota.
DR   HOGENOM; CLU_035750_10_0_1; -.
DR   InParanoid; Q9Y7T8; -.
DR   OMA; GWGAIVH; -.
DR   PhylomeDB; Q9Y7T8; -.
DR   Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR   Reactome; R-SPO-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-SPO-5689603; UCH proteinases.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR   Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-SPO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-SPO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q9Y7T8; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:UniProt.
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   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..204
FT                   /note="Probable proteasome subunit beta type-3"
FT                   /id="PRO_0000148069"
SQ   SEQUENCE   204 AA;  22661 MW;  80C3964E8A40A00E CRC64;
     MSIMEYNGGS CVAMAGKNCV AIASDLRLGV QSISLTNNFP KVFAMGDKTY LGLTGLATDV
     QTLYELFRYK VNLYKFREER QIQPKTFANL VSSTLYEKRF GPYFSFPVVA GVSNDNTPFI
     CGFDSIGCID FAEDFIVSGT ATEQLYGMCE SVYEPNLEPD DLFETISQAL LNAQDRDCIS
     GWGCVVYVIT ADKCIKRLVK GRQD