ID   F4JD01_ARATH            Unreviewed;       223 AA.
AC   F4JD01;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   Name=PBF1 {ECO:0000313|EMBL:AEE80113.1, ECO:0000313|TAIR:AT3G60820};
GN   OrderedLocusNames=At3g60820 {ECO:0000313|Araport:AT3G60820,
GN   ECO:0000313|EMBL:AEE80113.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE80113.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:AEE80113.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=11130713; DOI=10.1038/35048706;
RG   European Union Chromosome 3 Arabidopsis Sequencing Consortium;
RG   Institute for Genomic Research;
RG   Kazusa DNA Research Institute;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Blocker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M.,
RA   Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N.,
RA   Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L.,
RA   Weissenbach J., Saurin W., Quetier F., Schafer M., Muller-Auer S.,
RA   Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N.,
RA   Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P.,
RA   Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S.,
RA   Simionati B., Conrad A., Hornischer K., Kauer G., Lohnert T.H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schon O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwalder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S.,
RA   Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC       complex which is characterized by its ability to cleave peptides with
CC       Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC       slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC       activity. {ECO:0000256|RuleBase:RU004203}.
CC   -!- SUBUNIT: Component of the 20S core complex of the 26S proteasome. The
CC       26S proteasome is composed of a core protease (CP), known as the 20S
CC       proteasome, capped at one or both ends by the 19S regulatory particle
CC       (RP/PA700). The 20S proteasome core is composed of 28 subunits that are
CC       arranged in four stacked rings, resulting in a barrel-shaped structure.
CC       The two end rings are each formed by seven alpha subunits, and the two
CC       central rings are each formed by seven beta subunits. The catalytic
CC       chamber with the active sites is on the inside of the barrel.
CC       {ECO:0000256|ARBA:ARBA00011517}.
CC   -!- SUBUNIT: Component of the proteasome complex.
CC       {ECO:0000256|RuleBase:RU004203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC       Nucleus {ECO:0000256|RuleBase:RU004203}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family.
CC       {ECO:0000256|RuleBase:RU004203}.
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DR   EMBL; CP002686; AEE80113.1; -; Genomic_DNA.
DR   RefSeq; NP_001030905.1; NM_001035828.2.
DR   AlphaFoldDB; F4JD01; -.
DR   SMR; F4JD01; -.
DR   iPTMnet; F4JD01; -.
DR   ProteomicsDB; 195647; -.
DR   EnsemblPlants; AT3G60820.2; AT3G60820.2; AT3G60820.
DR   GeneID; 825253; -.
DR   Gramene; AT3G60820.2; AT3G60820.2; AT3G60820.
DR   Araport; AT3G60820; -.
DR   TAIR; AT3G60820; PBF1.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4JD01; baseline and differential.
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; IEA:InterPro.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
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.
PE   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|RuleBase:RU004203};
KW   Nucleus {ECO:0000256|RuleBase:RU004203};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F4JD01,
KW   ECO:0007829|ProteomicsDB:F4JD01};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548}.
SQ   SEQUENCE   223 AA;  24685 MW;  E3040079F353D9B1 CRC64;
     MTKQHANWSP YDNNGGTCVA IAGSDYCVIA ADTRMSTGYS ILSRDYSKIH KLADRAVLSS
     SGFQADVKAL QKVLKSRHLI YQHQHNKQMS CPAMAQLLSN TLYFKRFFPY YAFNVLGGLD
     EEGKGCVFTY DAVGSYERVG YGAQGSGSTL IMPFLDNQLK SPSPLLLPKQ DSNTPLSEAE
     AVDLVKTVFA SATERDIYTV NKLEIMILKA DGIKTELMDL RKD
//