ID   PSB7B_ARATH             Reviewed;         274 AA.
AC   Q7DLS1; O23709; Q8LAK8; Q8RWL9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Proteasome subunit beta type-7-B;
DE            EC=3.4.25.1;
DE   AltName: Full=20S proteasome beta subunit B-2;
DE   AltName: Full=Proteasome component FC;
DE   AltName: Full=Proteasome subunit beta type-2;
DE   Flags: Precursor;
GN   Name=PBB2; Synonyms=PRCFC; OrderedLocusNames=At5g40580;
GN   ORFNames=MNF13.10;
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], 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 57-274.
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   [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=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q7DLS1-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; AF043531; AAC32067.1; -; mRNA.
DR   EMBL; AB009052; BAB08528.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94567.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94568.1; -; Genomic_DNA.
DR   EMBL; AY093011; AAM13010.1; -; mRNA.
DR   EMBL; AY114591; AAM47910.1; -; mRNA.
DR   EMBL; AY087750; AAM65286.1; -; mRNA.
DR   EMBL; Y13177; CAA73620.1; -; mRNA.
DR   PIR; T51979; T51979.
DR   RefSeq; NP_198874.1; NM_123422.4. [Q7DLS1-1]
DR   RefSeq; NP_851108.1; NM_180777.3. [Q7DLS1-1]
DR   AlphaFoldDB; Q7DLS1; -.
DR   SMR; Q7DLS1; -.
DR   BioGRID; 19307; 61.
DR   IntAct; Q7DLS1; 1.
DR   STRING; 3702.Q7DLS1; -.
DR   MEROPS; T01.011; -.
DR   iPTMnet; Q7DLS1; -.
DR   PaxDb; 3702-AT5G40580-1; -.
DR   ProteomicsDB; 225994; -. [Q7DLS1-1]
DR   EnsemblPlants; AT5G40580.1; AT5G40580.1; AT5G40580. [Q7DLS1-1]
DR   EnsemblPlants; AT5G40580.2; AT5G40580.2; AT5G40580. [Q7DLS1-1]
DR   GeneID; 834056; -.
DR   Gramene; AT5G40580.1; AT5G40580.1; AT5G40580. [Q7DLS1-1]
DR   Gramene; AT5G40580.2; AT5G40580.2; AT5G40580. [Q7DLS1-1]
DR   KEGG; ath:AT5G40580; -.
DR   Araport; AT5G40580; -.
DR   TAIR; AT5G40580; PBB2.
DR   eggNOG; KOG0173; Eukaryota.
DR   InParanoid; Q7DLS1; -.
DR   OMA; VEKEFNC; -.
DR   OrthoDB; 5485745at2759; -.
DR   PhylomeDB; Q7DLS1; -.
DR   PRO; PR:Q7DLS1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q7DLS1; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   CDD; cd03763; proteasome_beta_type_7; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   PANTHER; PTHR32194:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
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; Q7DLS1; AT.
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_0000042832"
FT   CHAIN           38..274
FT                   /note="Proteasome subunit beta type-7-B"
FT                   /id="PRO_0000042833"
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P25043"
FT   CONFLICT        173
FT                   /note="A -> V (in Ref. 4; AAM13010/AAM47910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   274 AA;  29617 MW;  4AD31807A97D4C51 CRC64;
     MSQSSVDIPP KGGFSFDLCK RNDMLTQKGL KAPSFLKTGT TIVGLIFKDG VILGADTRAT
     EGPIVADKNC EKIHYMAPNI YCCGAGTAAD TEAVTDMVSS QLRLHRYQTG RDSRVVTALT
     LLKKHLFSYQ GHVSAALVLG GVDITGPHLH TIYPHGSTDT LPFATMGSGS LAAMSVFEAK
     YKEGLTRDEG IKLVAEAICS GIFNDLGSGS NVDICVITKG HKEYLRNYME PNPRTYVSSK
     GYSFTKKTEV LLTKITPLLE RVEIVEVAGE AMEE
//