ID   PSA2A_ARATH             Reviewed;         235 AA.
AC   O23708; B9DGA9; Q94EI0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Proteasome subunit alpha type-2-A;
DE   AltName: Full=20S proteasome alpha subunit B-1;
DE   AltName: Full=Proteasome component 3;
GN   Name=PAB1; Synonyms=PRC3; OrderedLocusNames=At1g16470;
GN   ORFNames=F3O9.27;
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] (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=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   [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] (ISOFORMS 1 AND 2).
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).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [7]
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   [8]
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   [9]
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   [10]
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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O23708-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O23708-2; Sequence=VSP_016142;
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; Y13176; CAA73619.1; -; mRNA.
DR   EMBL; AF043520; AAC32056.1; -; mRNA.
DR   EMBL; AC006341; AAD34699.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29457.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29458.1; -; Genomic_DNA.
DR   EMBL; AF332467; AAG48830.1; -; mRNA.
DR   EMBL; AF410305; AAK95291.1; -; mRNA.
DR   EMBL; BT000520; AAN18089.1; -; mRNA.
DR   EMBL; AK317085; BAH19776.1; -; mRNA.
DR   EMBL; AK317410; BAH20079.1; -; mRNA.
DR   EMBL; AY088628; AAM66950.1; -; mRNA.
DR   PIR; T51968; T51968.
DR   RefSeq; NP_001031057.1; NM_001035980.1. [O23708-1]
DR   RefSeq; NP_173096.1; NM_101512.4. [O23708-1]
DR   AlphaFoldDB; O23708; -.
DR   SMR; O23708; -.
DR   BioGRID; 23457; 74.
DR   STRING; 3702.O23708; -.
DR   MEROPS; T01.972; -.
DR   MetOSite; O23708; -.
DR   PaxDb; 3702-AT1G16470-2; -.
DR   ProteomicsDB; 226484; -. [O23708-1]
DR   EnsemblPlants; AT1G16470.1; AT1G16470.1; AT1G16470. [O23708-1]
DR   EnsemblPlants; AT1G16470.2; AT1G16470.2; AT1G16470. [O23708-1]
DR   GeneID; 838217; -.
DR   Gramene; AT1G16470.1; AT1G16470.1; AT1G16470. [O23708-1]
DR   Gramene; AT1G16470.2; AT1G16470.2; AT1G16470. [O23708-1]
DR   KEGG; ath:AT1G16470; -.
DR   Araport; AT1G16470; -.
DR   TAIR; AT1G16470; PAB1.
DR   eggNOG; KOG0181; Eukaryota.
DR   HOGENOM; CLU_035750_4_1_1; -.
DR   InParanoid; O23708; -.
DR   OMA; YQEQIPT; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; O23708; -.
DR   PRO; PR:O23708; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O23708; 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; HDA:TAIR.
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:0010043; P:response to zinc ion; IEP:TAIR.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03750; proteasome_alpha_type_2; 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; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF16; PROTEASOME SUBUNIT ALPHA TYPE-2; 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; O23708; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus; Proteasome;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..235
FT                   /note="Proteasome subunit alpha type-2-A"
FT                   /id="PRO_0000124085"
FT   CROSSLNK        64
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:O81149"
FT   VAR_SEQ         1..148
FT                   /note="MGDSQYSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKL
FT                   PSILVDEASVQKIQHLTPNIGVVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLV
FT                   RETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQ -> MIIPVRCFTCGK (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_016142"
SQ   SEQUENCE   235 AA;  25701 MW;  E9A676F750C85B96 CRC64;
     MGDSQYSFSL TTFSPSGKLV QIEHALTAVG SGQTSLGIKA SNGVVIATEK KLPSILVDEA
     SVQKIQHLTP NIGVVYSGMG PDFRVLVRKS RKQAEQYLRL YKEPIPVTQL VRETATVMQE
     FTQSGGVRPF GVSLLVAGYD DKGPQLYQVD PSGSYFSWKA SAMGKNVSNA KTFLEKRYTE
     DMELDDAIHT AILTLKEGFE GEISSKNIEI GKIGADKVFR VLTPAEIDDY LAEVE
//