ID   PSA5B_ARATH             Reviewed;         237 AA.
AC   Q42134;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Proteasome subunit alpha type-5-B;
DE   AltName: Full=20S proteasome alpha subunit E-2;
DE   AltName: Full=Proteasome component Z;
GN   Name=PAE2; Synonyms=PRCZ; OrderedLocusNames=At3g14290;
GN   ORFNames=MLN21.8;
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=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   [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] OF 181-237.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RX   PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA   Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA   Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA   Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA   Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA   Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA   Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT   a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
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   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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP   COMPLEX, SUBUNIT, ACETYLATION AT MET-1, AND UBIQUITINATION AT LYS-66 AND
RP   LYS-185.
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   -!- 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:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; AF043525; AAC32061.1; -; mRNA.
DR   EMBL; AB022220; BAB01035.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75498.1; -; Genomic_DNA.
DR   EMBL; AF370245; AAK44060.1; -; mRNA.
DR   EMBL; AY062970; AAL33816.1; -; mRNA.
DR   EMBL; Z26556; CAA81327.1; -; mRNA.
DR   PIR; T51973; T51973.
DR   RefSeq; NP_188046.1; NM_112287.4.
DR   AlphaFoldDB; Q42134; -.
DR   SMR; Q42134; -.
DR   BioGRID; 5983; 78.
DR   IntAct; Q42134; 1.
DR   STRING; 3702.Q42134; -.
DR   MEROPS; T01.995; -.
DR   iPTMnet; Q42134; -.
DR   PaxDb; 3702-AT3G14290-1; -.
DR   ProteomicsDB; 226344; -.
DR   EnsemblPlants; AT3G14290.1; AT3G14290.1; AT3G14290.
DR   GeneID; 820649; -.
DR   Gramene; AT3G14290.1; AT3G14290.1; AT3G14290.
DR   KEGG; ath:AT3G14290; -.
DR   Araport; AT3G14290; -.
DR   TAIR; AT3G14290; PAE2.
DR   eggNOG; KOG0176; Eukaryota.
DR   HOGENOM; CLU_035750_4_2_1; -.
DR   InParanoid; Q42134; -.
DR   OMA; FWFTYNR; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; Q42134; -.
DR   PRO; PR:Q42134; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q42134; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR   GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0004540; F:RNA nuclease activity; IDA:TAIR.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03753; proteasome_alpha_type_5; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR033812; Proteasome_alpha_type_5.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF14; PROTEASOME SUBUNIT ALPHA TYPE-5; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
DR   Genevisible; Q42134; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Proteasome;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..237
FT                   /note="Proteasome subunit alpha type-5-B"
FT                   /id="PRO_0000124125"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:20516081"
FT   CROSSLNK        43
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:O81148"
FT   CROSSLNK        66
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:20516081"
FT   CROSSLNK        185
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:20516081"
SQ   SEQUENCE   237 AA;  25977 MW;  B178A3A0DDA12680 CRC64;
     MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKEGVVLAV EKRITSPLLE
     PSSVEKIMEI DDHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQALCDLA
     LRFGEGEEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ
     EQFNKDITLQ EAETIAVSIL KQVMEEKVTP NNVDIAKVAP AYHLYTPQEV EAVISRL
//