PSA3_ARATH
ID PSA3_ARATH Reviewed; 249 AA.
AC O23715; O81151; Q680B8; Q9M3S3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=Proteasome subunit alpha type-3;
DE AltName: Full=20S proteasome alpha subunit G-1;
DE AltName: Full=DiDi 17A-2a;
DE AltName: Full=Proteasome component 8;
DE AltName: Full=Proteasome subunit alpha type-7;
GN Name=PAG1; Synonyms=PRC8; OrderedLocusNames=At2g27020; ORFNames=T20P8.7;
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].
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], TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-249.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 219-249, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=11277426; DOI=10.1094/mpmi.2001.14.3.288;
RA Vercauteren I., van der Schueren E., Van Montagu M., Gheysen G.;
RT "Arabidopsis thaliana genes expressed in the early compatible interaction
RT with root-knot nematodes.";
RL Mol. Plant Microbe Interact. 14:288-299(2001).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, DISRUPTION PHENOTYPE, ACETYLATION AT SER-214 AND SER-220,
RP AND UBIQUITINATION AT LYS-221.
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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -!- INTERACTION:
CC O23715; O23160: MYB73; NbExp=3; IntAct=EBI-594343, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous low levels.
CC {ECO:0000269|PubMed:11277426, ECO:0000269|PubMed:9611183}.
CC -!- INDUCTION: Induced by the endoparasitic nematode M.incognita. Levels
CC increase after infection in both giants cells and endodermal cells of
CC galls. Later confined to giant cells at high levels.
CC {ECO:0000269|PubMed:11277426}.
CC -!- DISRUPTION PHENOTYPE: Lethal due to defect in male gametogenesis.
CC {ECO:0000269|PubMed:20516081}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; Y13693; CAA74027.1; -; mRNA.
DR EMBL; AF043528; AAC32064.1; -; mRNA.
DR EMBL; AC005623; AAC77860.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07923.1; -; Genomic_DNA.
DR EMBL; AF375455; AAK53039.1; -; mRNA.
DR EMBL; AY124806; AAM70515.1; -; mRNA.
DR EMBL; AY088609; AAM66932.1; -; mRNA.
DR EMBL; AK175942; BAD43705.1; -; mRNA.
DR EMBL; AK175949; BAD43712.1; -; mRNA.
DR EMBL; AJ286351; CAB71015.1; -; mRNA.
DR PIR; G84667; G84667.
DR RefSeq; NP_180270.1; NM_128260.5.
DR AlphaFoldDB; O23715; -.
DR SMR; O23715; -.
DR BioGRID; 2596; 76.
DR IntAct; O23715; 4.
DR STRING; 3702.AT2G27020.1; -.
DR iPTMnet; O23715; -.
DR MetOSite; O23715; -.
DR PaxDb; O23715; -.
DR PRIDE; O23715; -.
DR ProteomicsDB; 226304; -.
DR EnsemblPlants; AT2G27020.1; AT2G27020.1; AT2G27020.
DR GeneID; 817244; -.
DR Gramene; AT2G27020.1; AT2G27020.1; AT2G27020.
DR KEGG; ath:AT2G27020; -.
DR Araport; AT2G27020; -.
DR TAIR; locus:2059319; AT2G27020.
DR eggNOG; KOG0184; Eukaryota.
DR HOGENOM; CLU_035750_0_0_1; -.
DR InParanoid; O23715; -.
DR OMA; SMYMHAY; -.
DR PhylomeDB; O23715; -.
DR PRO; PR:O23715; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O23715; baseline and differential.
DR Genevisible; O23715; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.10; -; 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 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..249
FT /note="Proteasome subunit alpha type-3"
FT /id="PRO_0000124098"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 214
FT /note="O-acetylserine"
FT /evidence="ECO:0000269|PubMed:20516081"
FT MOD_RES 220
FT /note="O-acetylserine"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CONFLICT 20
FT /note="R -> G (in Ref. 1; CAA74027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27377 MW; FB5BAA07AC45A25D CRC64;
MSSIGTGYDL SVTTFSPDGR VFQIEYAAKA VDNSGTVVGI KCKDGIVMGV EKLIASKMML
PGSNRRIHSV HRHAGMAVAG LAADGRQIVA RAKSEARSYE SVYGDAVPVK ELSERVASYV
HLCTLYWWLR PFGCGVILGG YDRDGPQLYM IEPSGISYRY FGAAIGKGKQ AAKTEIEKLN
LSEMTCKEGV IEVAKIIYKL HDEAKDKAFE LEMSWICEES KREHQKVPDD LLEEAKTAAK
TALEEMDAD
