PSD2A_ARATH
ID PSD2A_ARATH Reviewed; 891 AA.
AC Q9SIV2; Q56ZR0; Q9C5J1;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 2 homolog A {ECO:0000303|PubMed:14623884};
DE AltName: Full=26S proteasome regulatory subunit RPN1a {ECO:0000303|PubMed:14623884};
DE Short=AtRPN1a {ECO:0000303|PubMed:14623884};
DE AltName: Full=26S proteasome regulatory subunit S2 homolog A {ECO:0000303|PubMed:14623884};
GN Name=RPN1A {ECO:0000303|PubMed:14623884};
GN OrderedLocusNames=At2g20580 {ECO:0000312|Araport:AT2G20580};
GN ORFNames=F23N11.10 {ECO:0000312|EMBL:AAD21708.2};
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], SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [2]
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 [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 643-891.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16169895; DOI=10.1105/tpc.105.034975;
RA Brukhin V., Gheyselinck J., Gagliardini V., Genschik P., Grossniklaus U.;
RT "The RPN1 subunit of the 26S proteasome in Arabidopsis is essential for
RT embryogenesis.";
RL Plant Cell 17:2723-2737(2005).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19605416; DOI=10.1093/pcp/pcp105;
RA Wang S., Kurepa J., Smalle J.A.;
RT "The Arabidopsis 26S proteasome subunit RPN1a is required for optimal plant
RT growth and stress responses.";
RL Plant Cell Physiol. 50:1721-1725(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, ACETYLATION AT THR-219, AND UBIQUITINATION AT LYS-218.
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION BY
RP SALICYLIC ACID.
RX PubMed=22577987; DOI=10.1111/j.1365-313x.2012.05048.x;
RA Yao C., Wu Y., Nie H., Tang D.;
RT "RPN1a, a 26S proteasome subunit, is required for innate immunity in
RT Arabidopsis.";
RL Plant J. 71:1015-1028(2012).
RN [10]
RP FUNCTION, INTERACTION WITH JMJ27, AND REPRESSION BY DROUGHT.
RC STRAIN=cv. Columbia;
RX PubMed=34197643; DOI=10.1111/nph.17593;
RA Wang Q., Liu P., Jing H., Zhou X.F., Zhao B., Li Y., Jin J.B.;
RT "JMJ27-mediated histone H3K9 demethylation positively regulates drought-
RT stress responses in Arabidopsis.";
RL New Phytol. 232:221-236(2021).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins (By
CC similarity). Required during embryogenesis (PubMed:16169895). Required
CC for optimal plant growth and stress responses (PubMed:19605416).
CC Required for innate immunity (PubMed:22577987). Prevents JMJ27
CC accumulation in non-drought conditions (PubMed:34197643). {ECO:0000250,
CC ECO:0000269|PubMed:16169895, ECO:0000269|PubMed:19605416,
CC ECO:0000269|PubMed:22577987, ECO:0000269|PubMed:34197643}.
CC -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) base
CC subcomplex of the 26S proteasome. The 26S proteasome is composed of a
CC core protease (CP), known as the 20S proteasome, capped at one or both
CC ends by the 19S regulatory particle (RP/PA700). The RP/PA700 complex is
CC composed of at least 17 different subunits in two subcomplexes, the
CC base and the lid, which form the portions proximal and distal to the
CC 20S proteolytic core, respectively. Interacts with JMJ27
CC (PubMed:34197643). {ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081, ECO:0000269|PubMed:34197643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:22577987}. Cytoplasm {ECO:0000269|PubMed:22577987}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, buds, flowers, siliques
CC and developing seeds. {ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:16169895}.
CC -!- DEVELOPMENTAL STAGE: Detected in the floral meristem and primordia of
CC floral organs. During early stages of flower development, expressed in
CC the whole floral meristem, especially in emerging primordia. Later
CC present in developing carpels, particularly in emerging ovule
CC primordia. After fertilization, observed in the embryo and the chalazal
CC endosperm. High levels at the early embryogenesis stages that fade out
CC later. Also present in the developing seed coat, the septum, and the
CC silique wall. In the stamens, detected at high levels in the anthers.
CC Observed in sporogenous cells and then in tetrads of microspores.
CC {ECO:0000269|PubMed:16169895}.
CC -!- INDUCTION: By salicylic acid (SA) (PubMed:22577987). Repressed by
CC drought (PubMed:34197643). {ECO:0000269|PubMed:22577987,
CC ECO:0000269|PubMed:34197643}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality due to development arrest at the
CC globular stage with defects in the formation of the embryonic root, the
CC protoderm, and procambium (PubMed:16169895). Increased cell sizes,
CC anthocyanin accumulation, reduced growth rate, reduced fertility,
CC decreased heat shock tolerance, increased oxidative stress tolerance
CC (PubMed:19605416). Mutant displays enhanced susceptibility to the
CC fungal pathogen G. cichoracearum and to virulent and avirulent
CC bacterial Pto DC3000 strains, which indicated defects in basal defense
CC and resistance (R) protein-mediated defense (PubMed:22577987).
CC {ECO:0000269|PubMed:16169895, ECO:0000269|PubMed:19605416,
CC ECO:0000269|PubMed:22577987}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
CC -!- CAUTION: The embryo lethal disruption phenotype (PubMed:16169895) could
CC be confirmed (PubMed:19605416). {ECO:0000305|PubMed:16169895,
CC ECO:0000305|PubMed:19605416}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94334.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY230828; AAP86655.1; -; mRNA.
DR EMBL; AC007048; AAD21708.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07032.1; -; Genomic_DNA.
DR EMBL; AF360216; AAK25926.1; -; mRNA.
DR EMBL; AY040061; AAK64119.1; -; mRNA.
DR EMBL; AK220903; BAD94334.1; ALT_INIT; mRNA.
DR PIR; A84591; A84591.
DR RefSeq; NP_565477.1; NM_127618.4.
DR AlphaFoldDB; Q9SIV2; -.
DR SMR; Q9SIV2; -.
DR BioGRID; 1933; 147.
DR IntAct; Q9SIV2; 28.
DR STRING; 3702.AT2G20580.1; -.
DR iPTMnet; Q9SIV2; -.
DR MetOSite; Q9SIV2; -.
DR SwissPalm; Q9SIV2; -.
DR PaxDb; Q9SIV2; -.
DR PRIDE; Q9SIV2; -.
DR ProteomicsDB; 225998; -.
DR EnsemblPlants; AT2G20580.1; AT2G20580.1; AT2G20580.
DR GeneID; 816580; -.
DR Gramene; AT2G20580.1; AT2G20580.1; AT2G20580.
DR KEGG; ath:AT2G20580; -.
DR Araport; AT2G20580; -.
DR TAIR; locus:2046016; AT2G20580.
DR eggNOG; KOG2005; Eukaryota.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; Q9SIV2; -.
DR OMA; KTVYKHM; -.
DR OrthoDB; 229956at2759; -.
DR PhylomeDB; Q9SIV2; -.
DR PRO; PR:Q9SIV2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIV2; baseline and differential.
DR Genevisible; Q9SIV2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:TAIR.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR Pfam; PF01851; PC_rep; 1.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Immunity; Innate immunity; Isopeptide bond;
KW Nucleus; Proteasome; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..891
FT /note="26S proteasome non-ATPase regulatory subunit 2
FT homolog A"
FT /id="PRO_0000399921"
FT REPEAT 414..447
FT /note="PC 1"
FT /evidence="ECO:0000255"
FT REPEAT 448..484
FT /note="PC 2"
FT /evidence="ECO:0000255"
FT REPEAT 485..519
FT /note="PC 3"
FT /evidence="ECO:0000255"
FT REPEAT 522..556
FT /note="PC 4"
FT /evidence="ECO:0000255"
FT REPEAT 565..594
FT /note="PC 5"
FT /evidence="ECO:0000255"
FT REPEAT 674..705
FT /note="PC 6"
FT /evidence="ECO:0000255"
FT REPEAT 724..739
FT /note="PC 7"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..21
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 19..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 219
FT /note="O-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
SQ SEQUENCE 891 AA; 98144 MW; 68C0B94F83F21955 CRC64;
MAPTQDPNSV GGGAKKDEAT LKVPSKDPKK KDEKKDEDLS EEDLELKQNL ELYVERVQDP
NPELQKAALE SMRQEIRAST SSMTSVPKPL KFLRPHYGTL KAFHETMADS DLKKYLSDIL
SVLALTMSAD GERESLRFRL IGTEGDIGSW GHEYVRNLAG EIAQEYTKRQ SEEASIDDLM
ELVQQIVAFH MKHNAETEAV DLLMDVEDLD LLLEHVDKTN FKRTCNYLTS AARYLPGPDD
MLVLDISYMI YMKFEEYPNA LQIALFLDNT QYVKQVFTSC TDLLKKKQFC YMIARHGITF
ELDDEMVADD DDREALQDIV NNTKLSEGYL TLARDIEVME AKTPEDIYKA HLLDGRASSG
ASVDSARQNL AATFVNAFVN AGFGQDKLMT VPSDSTTGSS GNWLFKNKEH GKTSAAASLG
MIQLWDVDSG LSQLDKYFHS NDNPIIAGAL LGVGIVNCGI KNDCDPALAL LGDYIDKEDS
SVRIGAIMGL GISYAGSQND QIRNKLSPIL NDAKAPLDVI AFASLSLGMI YVGSCNEEVA
QSIIFALMDR SEAELGDALT RFLPLGLGLL YLGKQESVEA TAEVSKTFNE KIRKYCDMTL
LSCAYAGTGN VLKVQDLLAQ CGEHLEKGDI HQGPAVLGLA MVAMSEELGV DMEIRSLERM
LQYGEQNIRR AVPLALGLLC ISNPKVTVMD TLSRLSHDTD SEVAMSAIIS LGLIGAGTNN
ARIAGMLRNL SSYYYKDMSL LFCVRIAQGL VHMGKGLLTL SPFHSERFLL SPTALAGIVT
LLHACLDMKP IILGKYHYVL YFLVLAMQPR MMLTVDENLK PLSVPVRVGQ AVDVVGQAGR
PKTITGFQTH STPVLLAAGE RAELATDKYI PLSPILEGFI ILKENPDYRE E
