PSB7A_ARATH
ID PSB7A_ARATH Reviewed; 273 AA.
AC O23710; O81152; Q3EAZ2; Q9T0L7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Proteasome subunit beta type-7-A;
DE EC=3.4.25.1;
DE AltName: Full=20S proteasome beta subunit B-1;
DE AltName: Full=Proteasome component FA;
DE AltName: Full=Proteasome component FB;
DE AltName: Full=Proteasome subunit beta type-2;
DE Flags: Precursor;
GN Name=PBB1; Synonyms=PRCFA, PRCFB; OrderedLocusNames=At3g27430;
GN ORFNames=K1G2.15;
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], AND NUCLEOTIDE SEQUENCE [MRNA] OF 155-273
RP (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=9373170; DOI=10.1016/s0014-5793(97)01228-3;
RA Parmentier Y., Bouchez D., Fleck J., Genschik P.;
RT "The 20S proteasome gene family in Arabidopsis thaliana.";
RL FEBS Lett. 416:281-285(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (ISOFORM 1).
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] (ISOFORM 1).
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 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 [8]
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: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
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:20516081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O23710-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O23710-2; Sequence=VSP_018144, VSP_018145;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; Y13174; CAA73617.1; -; mRNA.
DR EMBL; Y13178; CAA73621.1; -; mRNA.
DR EMBL; AF043530; AAC32066.1; -; mRNA.
DR EMBL; AB024028; BAA95719.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77318.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77319.1; -; Genomic_DNA.
DR EMBL; BT003339; AAO29958.1; -; mRNA.
DR EMBL; BT006306; AAP13414.1; -; mRNA.
DR EMBL; AY086464; AAM63467.1; -; mRNA.
DR PIR; T51977; T51977.
DR RefSeq; NP_566818.1; NM_113658.3. [O23710-1]
DR RefSeq; NP_850641.1; NM_180310.1. [O23710-2]
DR AlphaFoldDB; O23710; -.
DR SMR; O23710; -.
DR BioGRID; 7694; 62.
DR IntAct; O23710; 1.
DR STRING; 3702.AT3G27430.2; -.
DR MEROPS; T01.011; -.
DR PaxDb; O23710; -.
DR PRIDE; O23710; -.
DR ProteomicsDB; 226004; -. [O23710-1]
DR EnsemblPlants; AT3G27430.1; AT3G27430.1; AT3G27430. [O23710-2]
DR EnsemblPlants; AT3G27430.2; AT3G27430.2; AT3G27430. [O23710-1]
DR GeneID; 822364; -.
DR Gramene; AT3G27430.1; AT3G27430.1; AT3G27430. [O23710-2]
DR Gramene; AT3G27430.2; AT3G27430.2; AT3G27430. [O23710-1]
DR KEGG; ath:AT3G27430; -.
DR Araport; AT3G27430; -.
DR TAIR; locus:2086681; AT3G27430.
DR eggNOG; KOG0173; Eukaryota.
DR InParanoid; O23710; -.
DR OMA; ESKYHEG; -.
DR PhylomeDB; O23710; -.
DR PRO; PR:O23710; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O23710; baseline and differential.
DR Genevisible; O23710; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
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; IPR000243; Pept_T1A_subB.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
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; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..37
FT /note="Removed in mature form"
FT /id="PRO_0000042830"
FT CHAIN 38..273
FT /note="Proteasome subunit beta type-7-A"
FT /id="PRO_0000042831"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25043"
FT VAR_SEQ 249..267
FT /note="EVLLTKITPLLERVEITEV -> GSSHQNHPIAGASRNHRSW (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018144"
FT VAR_SEQ 268..273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018145"
FT CONFLICT 27
FT /note="Q -> P (in Ref. 1; CAA73621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29555 MW; 4133891315E0915C CRC64;
MSQSTVDVPP KGGFSFDLCK RNDMLTQKGL KAPSFLKTGT TIVGLIFKDG VILGADTRAT
EGPIVADKNC EKIHYMAPNI YCCGAGTAAD TEAVTDMVSS QLRLHRYQTG RDSRVITALT
LLKKHLFSYQ GHVSAALVLG GVDITGPHLH TIYPHGSTDT LPFATMGSGS LAAMSVFEAK
YKEGLTRDEG IKLVAESICS GIFNDLGSGS NVDICVITKG NKEYLRNYME PNPRTYVSSK
GYSFTKKTEV LLTKITPLLE RVEITEVGEA MEE
