ID   PSD7A_ARATH             Reviewed;         308 AA.
AC   O24412; Q6EMB3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 7 homolog A;
DE   AltName: Full=26S proteasome regulatory subunit RPN8a;
DE            Short=AtRPN8a;
DE   AltName: Full=Protein ASYMMETRIC LEAVES ENHANCER 3;
DE   AltName: Full=Protein MOV34;
DE            Short=AtMOV34;
GN   Name=RPN8A; Synonyms=AE3, MOV34; OrderedLocusNames=At5g05780;
GN   ORFNames=MJJ3.19;
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].
RX   PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
RA   Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
RA   Hinnebusch A.G., Hershey J.W.B.;
RT   "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits.
RT   Possible roles in RNA binding and macromolecular assembly.";
RL   J. Biol. Chem. 272:27042-27052(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=17028202; DOI=10.1105/tpc.106.045013;
RA   Huang W., Pi L., Liang W., Xu B., Wang H., Cai R., Huang H.;
RT   "The proteolytic function of the Arabidopsis 26S proteasome is required for
RT   specifying leaf adaxial identity.";
RL   Plant Cell 18:2479-2492(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP   COMPLEX, SUBUNIT, AND ACETYLATION AT MET-1.
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, AND DISRUPTION PHENOTYPE.
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).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins (By
CC       similarity). Required for innate immunity. {ECO:0000250,
CC       ECO:0000269|PubMed:22577987}.
CC   -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) lid
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. {ECO:0000269|PubMed:14623884,
CC       ECO:0000269|PubMed:20516081}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O24412-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC       {ECO:0000269|PubMed:14623884, ECO:0000269|PubMed:17028202}.
CC   -!- DISRUPTION PHENOTYPE: Slightly dwarfish, with long and narrow rosette
CC       leaves. Exhibits a delayed flowering time. Mutant displays enhanced
CC       susceptibility to the fungal pathogen G. cichoracearum.
CC       {ECO:0000269|PubMed:17028202, ECO:0000269|PubMed:22577987}.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR   EMBL; U54560; AAD03464.1; -; mRNA.
DR   EMBL; AY230839; AAP86666.1; -; mRNA.
DR   EMBL; AY230840; AAP86667.1; -; mRNA.
DR   EMBL; AB005237; BAB09672.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90923.1; -; Genomic_DNA.
DR   EMBL; AF378878; AAK55681.1; -; mRNA.
DR   EMBL; BT002610; AAO11526.1; -; mRNA.
DR   EMBL; AY087393; AAM64942.1; -; mRNA.
DR   RefSeq; NP_196197.1; NM_120660.4. [O24412-1]
DR   AlphaFoldDB; O24412; -.
DR   SMR; O24412; -.
DR   BioGRID; 15742; 91.
DR   IntAct; O24412; 3.
DR   STRING; 3702.AT5G05780.1; -.
DR   MEROPS; M67.973; -.
DR   iPTMnet; O24412; -.
DR   PaxDb; O24412; -.
DR   PRIDE; O24412; -.
DR   ProteomicsDB; 224825; -. [O24412-1]
DR   EnsemblPlants; AT5G05780.1; AT5G05780.1; AT5G05780. [O24412-1]
DR   GeneID; 830463; -.
DR   Gramene; AT5G05780.1; AT5G05780.1; AT5G05780. [O24412-1]
DR   KEGG; ath:AT5G05780; -.
DR   Araport; AT5G05780; -.
DR   TAIR; locus:2166449; AT5G05780.
DR   eggNOG; KOG1556; Eukaryota.
DR   HOGENOM; CLU_027018_3_0_1; -.
DR   InParanoid; O24412; -.
DR   OMA; HAMSIKT; -.
DR   OrthoDB; 1275837at2759; -.
DR   PhylomeDB; O24412; -.
DR   PRO; PR:O24412; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O24412; baseline and differential.
DR   Genevisible; O24412; AT.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR   GO; GO:0005838; C:proteasome regulatory particle; IEA:InterPro.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR   GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd08062; MPN_RPN7_8; 1.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR033858; MPN_RPN7_8.
DR   InterPro; IPR024969; Rpn11/EIF3F_C.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF13012; MitMem_reg; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Immunity; Innate immunity; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..308
FT                   /note="26S proteasome non-ATPase regulatory subunit 7
FT                   homolog A"
FT                   /id="PRO_0000213946"
FT   DOMAIN          17..154
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:20516081"
SQ   SEQUENCE   308 AA;  34728 MW;  49026E713D4A41C3 CRC64;
     MDVIKTQQIS ARTIEKVVVH PLVLLSIVDH YNRVAKDSSK RVVGVLLGSS SRGVVDVTNS
     YAVPFEEDDK DPSIWFLDHN YHESMFHMFK RINAKEHVVG WYSTGPKLRE NDLDVHALFN
     GYVPNPVLVI IDVQPKELGI PTKAYYAVEE VKENATQKSQ KVFVHVSTEI AAHEVEEIGV
     EHLLRDVKDT TISTLATEVT AKLTALKGLD ARLREIRSYL DLVIEGKLPL NHEILYHLQD
     VFNLLPNLNV NELVKAFSVK TNDMMLVIYL SSLIRSVIAL HNLINNKLLN KEHEKAEDSK
     PVAIPATS