PSA5B_ARATH
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 25-MAY-2022, entry version 171.
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; 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}.
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; 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.AT3G14290.1; -.
DR MEROPS; T01.995; -.
DR iPTMnet; Q42134; -.
DR PaxDb; Q42134; -.
DR PRIDE; Q42134; -.
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; locus:2091065; AT3G14290.
DR eggNOG; KOG0176; Eukaryota.
DR HOGENOM; CLU_035750_4_2_1; -.
DR OMA; FQVEYAR; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; Q42134; -.
DR PRO; PR:Q42134; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42134; baseline and differential.
DR Genevisible; Q42134; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
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; cd03753; proteasome_alpha_type_5; 1.
DR Gene3D; 3.60.20.10; -; 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 Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
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
