ID   PSB1_DICDI              Reviewed;         236 AA.
AC   Q86A21; Q1ZXN1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Proteasome subunit beta type-1;
GN   Name=psmB1; ORFNames=DDB_G0272969;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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       Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; AAFI02000008; EAS66954.1; -; Genomic_DNA.
DR   RefSeq; XP_001134620.1; XM_001134620.1.
DR   AlphaFoldDB; Q86A21; -.
DR   SMR; Q86A21; -.
DR   BioGRID; 1243573; 1.
DR   STRING; 44689.DDB0232957; -.
DR   MEROPS; T01.A14; -.
DR   PaxDb; Q86A21; -.
DR   EnsemblProtists; EAS66954; EAS66954; DDB_G0272969.
DR   GeneID; 8618570; -.
DR   KEGG; ddi:DDB_G0272969; -.
DR   dictyBase; DDB_G0272969; psmB1.
DR   eggNOG; KOG0179; Eukaryota.
DR   HOGENOM; CLU_035750_1_1_1; -.
DR   InParanoid; Q86A21; -.
DR   OMA; IGFKNMQ; -.
DR   PhylomeDB; Q86A21; -.
DR   Reactome; R-DDI-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-DDI-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-DDI-4641258; Degradation of DVL.
DR   Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR   Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-DDI-5689603; UCH proteinases.
DR   Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR   Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q86A21; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IPI:dictyBase.
DR   GO; GO:0005634; C:nucleus; IPI:dictyBase.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:dictyBase.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProt.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IDA:dictyBase.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR035202; Proteasome_beta1.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF59; PTHR11599:SF59; 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..236
FT                   /note="Proteasome subunit beta type-1"
FT                   /id="PRO_0000328481"
SQ   SEQUENCE   236 AA;  26380 MW;  F5BC59291CA38DE2 CRC64;
     METLKLSALP EKDKQQPISH GRFEAYVDNG GTVLAVAGKD YCVIAGDTRM SDGGYGIQTR
     KYTKIFQLTK KCVLATSGMQ ADTIALQKRL KSMLESFEKE HGKPMSTPAI AQFLSNTLYY
     KRFFPYYTFN LVAGVDEQGE GWIWTYDAVG SHERVKYSSQ GSGNQLVIPL LDNQVAKFNQ
     QIVEGNKDVS CEQVVSFVKD SITSAGERDI YTGDFADIVV VDKNGVHWEK FELKLD