ID   PSB3B_ARATH             Reviewed;         204 AA.
AC   O81153; Q9CAR1; Q9SRH0;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Proteasome subunit beta type-3-B;
DE   AltName: Full=20S proteasome beta subunit C-2;
GN   Name=PBC2; OrderedLocusNames=At1g77440; ORFNames=T5M16.3;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   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   [6]
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   [7]
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   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51672.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF043533; AAC32069.1; -; mRNA.
DR   EMBL; AC010704; AAG51672.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE35977.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35978.1; -; Genomic_DNA.
DR   EMBL; AF385730; AAK60320.1; -; mRNA.
DR   EMBL; AY081735; AAL87388.1; -; mRNA.
DR   PIR; F96803; F96803.
DR   PIR; T51981; T51981.
DR   RefSeq; NP_001031294.1; NM_001036217.1.
DR   RefSeq; NP_565156.1; NM_106393.5.
DR   AlphaFoldDB; O81153; -.
DR   SMR; O81153; -.
DR   BioGRID; 29299; 39.
DR   IntAct; O81153; 1.
DR   STRING; 3702.AT1G77440.1; -.
DR   PaxDb; O81153; -.
DR   PRIDE; O81153; -.
DR   ProteomicsDB; 248888; -.
DR   EnsemblPlants; AT1G77440.1; AT1G77440.1; AT1G77440.
DR   EnsemblPlants; AT1G77440.2; AT1G77440.2; AT1G77440.
DR   GeneID; 844080; -.
DR   Gramene; AT1G77440.1; AT1G77440.1; AT1G77440.
DR   Gramene; AT1G77440.2; AT1G77440.2; AT1G77440.
DR   KEGG; ath:AT1G77440; -.
DR   Araport; AT1G77440; -.
DR   TAIR; locus:2204675; AT1G77440.
DR   eggNOG; KOG0180; Eukaryota.
DR   HOGENOM; CLU_035750_10_0_1; -.
DR   InParanoid; O81153; -.
DR   OrthoDB; 1170036at2759; -.
DR   PhylomeDB; O81153; -.
DR   PRO; PR:O81153; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O81153; baseline and differential.
DR   Genevisible; O81153; AT.
DR   GO; GO:0005739; C:mitochondrion; 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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03759; proteasome_beta_type_3; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR033811; Proteasome_beta_3.
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   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..204
FT                   /note="Proteasome subunit beta type-3-B"
FT                   /id="PRO_0000148066"
SQ   SEQUENCE   204 AA;  22759 MW;  AABEC113232EAFCF CRC64;
     MSIFEYNGSA VVAMVGKNCF AIASDRRLGV QLQTIATDFQ RISKIHDHLF IGLSGLATDV
     QTLYQRLVFR HKLYQLREER DMKPETFASL VSAILYEKRF GPFLCQPVIA GLGDDNKPFI
     CTMDSIGAKE LAKDFVVSGT ASESLYGACE AMFKPDMEAE ELFETISQAL LSSVDRDCLS
     GWGGHVYVVT PKEVKERILK GRMD