ID PSB1_ORYSJ Reviewed; 221 AA. AC O64464; Q0J0L6; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 24-JAN-2024, entry version 144. DE RecName: Full=Proteasome subunit beta type-1; DE AltName: Full=20S proteasome alpha subunit F; DE AltName: Full=20S proteasome subunit beta-6; GN Name=PBF1; OrderedLocusNames=Os09g0505600, LOC_Os09g32800; GN ORFNames=OsJ_29931 {ECO:0000312|EMBL:EAZ45289.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Nipponbare; TISSUE=Root; RX PubMed=10854779; DOI=10.1016/s0378-1119(00)00190-6; RA Sassa H., Oguchi S., Inoue T., Hirano H.; RT "Primary structural features of the 20S proteasome subunits of rice (Oryza RT sativa)."; RL Gene 250:61-66(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). 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 (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}. 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; AB014058; BAA28276.1; -; mRNA. DR EMBL; AC108753; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP008215; BAF25517.1; -; Genomic_DNA. DR EMBL; AP014965; BAT08852.1; -; Genomic_DNA. DR EMBL; CM000146; EAZ45289.1; -; Genomic_DNA. DR EMBL; AK060884; BAG87594.1; -; mRNA. DR EMBL; AK103136; BAG95912.1; -; mRNA. DR RefSeq; XP_015611664.1; XM_015756178.1. DR AlphaFoldDB; O64464; -. DR SMR; O64464; -. DR STRING; 39947.O64464; -. DR PaxDb; 39947-O64464; -. DR EnsemblPlants; Os09t0505600-01; Os09t0505600-01; Os09g0505600. DR GeneID; 4347507; -. DR Gramene; Os09t0505600-01; Os09t0505600-01; Os09g0505600. DR KEGG; osa:4347507; -. DR eggNOG; KOG0179; Eukaryota. DR HOGENOM; CLU_035750_1_1_1; -. DR InParanoid; O64464; -. DR OMA; MLYYKRF; -. DR OrthoDB; 158278at2759; -. DR Proteomes; UP000000763; Chromosome 9. DR Proteomes; UP000007752; Chromosome 9. DR Proteomes; UP000059680; Chromosome 9. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR CDD; cd03757; proteasome_beta_type_1; 1. 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:SF2; PROTEASOME SUBUNIT BETA TYPE-1; 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. DR Genevisible; O64464; OS. PE 2: Evidence at transcript level; KW Cytoplasm; Nucleus; Proteasome; Reference proteome. FT CHAIN 1..221 FT /note="Proteasome subunit beta type-1" FT /id="PRO_0000148039" SQ SEQUENCE 221 AA; 24282 MW; F040EE0C2CEA5C64 CRC64; MSRRGDWVYE NNGGTCVAIA GADYCVVAAD TRLSVGYNIL TRDHSKICEL ADKCALASSG FQGDIKALHK NLAARELLYQ HQHNKRMSCP AMAQLLSNTL YYKRFFPYYA FNVLGGLDSE GKGCVFTYDA VGSYERTGYS AQGTGSALIM PVLDNQLKSP SPLLLPARDA VTPLSETEAV DLVKDVFASA TERDIYTGDK LEIVVINKAG TKREYIDLRK D //