PSB1_ARATH
ID PSB1_ARATH Reviewed; 223 AA.
AC P42742; P42741; Q570C3; Q6LAD2; Q9SBI6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Proteasome subunit beta type-1;
DE AltName: Full=20S proteasome beta subunit F-1;
DE AltName: Full=Proteasome component 5;
DE AltName: Full=Proteasome subunit beta type-6;
DE AltName: Full=TAS-F22/FAFP98;
DE AltName: Full=TAS-G39.20;
GN Name=PBF1; Synonyms=PRC5; OrderedLocusNames=At3g60820; ORFNames=T4C21_230;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7987412; DOI=10.1046/j.1365-313x.1994.6040537.x;
RA Genschik P., Jamet E., Phillips G., Parmentier Y., Gigot C., Fleck J.;
RT "Molecular characterization of a beta-type proteasome subunit from
RT Arabidopsis thaliana co-expressed at a high level with an alpha-type
RT proteasome subunit early in the cell cycle.";
RL Plant J. 6:537-546(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=9611183; DOI=10.1093/genetics/149.2.677;
RA Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.;
RT "Molecular organization of the 20S proteasome gene family from Arabidopsis
RT thaliana.";
RL Genetics 149:677-692(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder 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.X.,
RA Kaul S., 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 [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-223.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-223.
RA Philipps G., Gigot C.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SUBUNIT.
RX PubMed=10363660; DOI=10.1023/a:1006926322501;
RA Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M.,
RA Finley D., Vierstra R.D.;
RT "Structure and functional analyses of the 26S proteasome subunits from
RT plants.";
RL Mol. Biol. Rep. 26:137-146(1999).
RN [10]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14623884; DOI=10.1074/jbc.m311977200;
RA Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.;
RT "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular
RT analyses revealed the presence of multiple isoforms.";
RL J. Biol. Chem. 279:6401-6413(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, AND SUBUNIT.
RX PubMed=20516081; DOI=10.1074/jbc.m110.136622;
RA Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.;
RT "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse
RT array of plant proteolytic complexes.";
RL J. Biol. Chem. 285:25554-25569(2010).
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: 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:0000269|PubMed:10363660, ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P42742-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Present in all tissues examined. Slightly lower
CC levels in roots. {ECO:0000269|PubMed:7987412}.
CC -!- DEVELOPMENTAL STAGE: Expressed at maximal levels after first day of
CC cell growth.
CC -!- INDUCTION: During cell proliferation. {ECO:0000269|PubMed:7987412}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA47753.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; X67338; CAA47753.1; ALT_INIT; mRNA.
DR EMBL; X79806; CAA56201.1; -; mRNA.
DR EMBL; AF043537; AAC32073.1; -; mRNA.
DR EMBL; AL162295; CAB82686.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80112.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80114.1; -; Genomic_DNA.
DR EMBL; AY062790; AAL32868.1; -; mRNA.
DR EMBL; AY081571; AAM10133.1; -; mRNA.
DR EMBL; AY086619; AAM63678.1; -; mRNA.
DR EMBL; AK220787; BAD94023.1; -; mRNA.
DR EMBL; Z26405; CAA81240.1; -; mRNA.
DR PIR; T47893; T47893.
DR RefSeq; NP_001190146.1; NM_001203217.1. [P42742-1]
DR RefSeq; NP_191641.1; NM_115946.3. [P42742-1]
DR AlphaFoldDB; P42742; -.
DR SMR; P42742; -.
DR BioGRID; 10567; 82.
DR IntAct; P42742; 11.
DR STRING; 3702.AT3G60820.1; -.
DR iPTMnet; P42742; -.
DR PaxDb; P42742; -.
DR PRIDE; P42742; -.
DR ProteomicsDB; 226348; -. [P42742-1]
DR EnsemblPlants; AT3G60820.1; AT3G60820.1; AT3G60820. [P42742-1]
DR EnsemblPlants; AT3G60820.3; AT3G60820.3; AT3G60820. [P42742-1]
DR GeneID; 825253; -.
DR Gramene; AT3G60820.1; AT3G60820.1; AT3G60820. [P42742-1]
DR Gramene; AT3G60820.3; AT3G60820.3; AT3G60820. [P42742-1]
DR KEGG; ath:AT3G60820; -.
DR Araport; AT3G60820; -.
DR TAIR; locus:2101846; AT3G60820.
DR eggNOG; KOG0179; Eukaryota.
DR HOGENOM; CLU_035750_1_1_1; -.
DR InParanoid; P42742; -.
DR OMA; IGFKNMQ; -.
DR PhylomeDB; P42742; -.
DR PRO; PR:P42742; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P42742; baseline and differential.
DR Genevisible; P42742; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
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:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 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 Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..223
FT /note="Proteasome subunit beta type-1"
FT /id="PRO_0000148038"
SQ SEQUENCE 223 AA; 24644 MW; E8050079F353D4C0 CRC64;
MTKQHANWSP YDNNGGTCVA IAGSDYCVIA ADTRMSTGYS ILSRDYSKIH KLADRAVLSS
SGFQADVKAL QKVLKSRHLI YQHQHNKQMS CPAMAQLLSN TLYFKRFFPY YAFNVLGGLD
EEGKGCVFTY DAVGSYERVG YGAQGSGSTL IMPFLDNQLK SPSPLLLPKQ DSNTPLSEAE
AVDLVKTVFA SATERDIYTG DKLEIMILKA DGIKTELMDL RKD
