PSD8A_ARATH
ID PSD8A_ARATH Reviewed; 267 AA.
AC Q9SGW3; Q6XJF4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 8 homolog A;
DE AltName: Full=26S proteasome regulatory subunit RPN12a {ECO:0000303|PubMed:14623884};
DE Short=AtRPN12a {ECO:0000303|PubMed:14623884};
DE AltName: Full=26S proteasome regulatory subunit S14 homolog A;
GN Name=RPN12A {ECO:0000303|PubMed:14623884};
GN OrderedLocusNames=At1g64520 {ECO:0000312|Araport:AT1G64520};
GN ORFNames=F1N19.9 {ECO:0000312|EMBL:AAF19671.1};
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=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 [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 FUNCTION, IDENTIFICATION IN THE 26S PROTEASOME, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11826296; DOI=10.1105/tpc.010381;
RA Smalle J., Kurepa J., Yang P., Babiychuk E., Kushnir S., Durski A.,
RA Vierstra R.D.;
RT "Cytokinin growth responses in Arabidopsis involve the 26S proteasome
RT subunit RPN12.";
RL Plant Cell 14:17-32(2002).
RN [6]
RP INTERACTION WITH PUB22 AND PUB23, AND UBIQUITINATION.
RX PubMed=18664614; DOI=10.1105/tpc.108.060699;
RA Cho S.K., Ryu M.Y., Song C., Kwak J.M., Kim W.T.;
RT "Arabidopsis PUB22 and PUB23 are homologous U-Box E3 ubiquitin ligases that
RT play combinatory roles in response to drought stress.";
RL Plant Cell 20:1899-1914(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17971041; DOI=10.1111/j.1365-313x.2007.03322.x;
RA Kurepa J., Toh-E A., Smalle J.A.;
RT "26S proteasome regulatory particle mutants have increased oxidative stress
RT tolerance.";
RL Plant J. 53:102-114(2008).
RN [8]
RP INTERACTION WITH TIF3E1.
RX PubMed=19704582; DOI=10.4161/psb.3.6.5434;
RA Paz-Aviram T., Yahalom A., Chamovitz D.A.;
RT "Arabidopsis eIF3e interacts with subunits of the ribosome, Cop9
RT signalosome and proteasome.";
RL Plant Signal. Behav. 3:409-411(2008).
RN [9]
RP FUNCTION.
RX PubMed=19812900; DOI=10.1007/s10059-009-0132-x;
RA Ryu M.Y., Cho S.K., Kim W.T.;
RT "RNAi suppression of RPN12a decreases the expression of type-A ARRs,
RT negative regulators of cytokinin signaling pathway, in Arabidopsis.";
RL Mol. Cells 28:375-382(2009).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19321709; DOI=10.1104/pp.109.135970;
RA Kurepa J., Wang S., Li Y., Zaitlin D., Pierce A.J., Smalle J.A.;
RT "Loss of 26S proteasome function leads to increased cell size and decreased
RT cell number in Arabidopsis shoot organs.";
RL Plant Physiol. 150:178-189(2009).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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).
RN [13]
RP INTERACTION WITH UCH1 AND UCH2.
RX PubMed=22951400; DOI=10.4161/psb.21899;
RA Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
RT "Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
RT associate with the 26S proteasome and the TREX-2 complex.";
RL Plant Signal. Behav. 7:1415-1419(2012).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC May help to control the degradation of one or more factors that repress
CC cytokinin signaling. Plays an important role for balancing cell
CC expansion with cell proliferation rates during shoot development.
CC {ECO:0000269|PubMed:11826296, ECO:0000269|PubMed:17971041,
CC ECO:0000269|PubMed:19321709, ECO:0000269|PubMed:19812900}.
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. Interacts with PUB22 and PUB23.
CC Binds to the translation initiation factors TIF3E1 (PubMed:19704582).
CC Interacts with UCH1 and UCH2 (PubMed:22951400).
CC {ECO:0000269|PubMed:11826296, ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:18664614, ECO:0000269|PubMed:19704582,
CC ECO:0000269|PubMed:20516081, ECO:0000269|PubMed:22951400}.
CC -!- INTERACTION:
CC Q9SGW3; P46639: KNAT1; NbExp=3; IntAct=EBI-594133, EBI-530486;
CC Q9SGW3; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-594133, EBI-15192297;
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
CC {ECO:0000269|PubMed:14623884}.
CC -!- INDUCTION: By cytokinins. {ECO:0000269|PubMed:11826296}.
CC -!- PTM: Ubiquitinated by PUB22 and PUB23. {ECO:0000269|PubMed:18664614}.
CC -!- DISRUPTION PHENOTYPE: Decreased rate of leaf formation, reduced root
CC elongation, delayed skotomorphogenesis and altered growth responses to
CC exogenous cytokinins. Increased sensitivity to heat shock and increased
CC tolerance to oxidative stress. Decreased 26S proteasome accumulation.
CC In flowers and cotyledons, epidermal cells were larger than those in
CC the wild type. {ECO:0000269|PubMed:11826296,
CC ECO:0000269|PubMed:17971041, ECO:0000269|PubMed:19321709}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S14 family.
CC {ECO:0000305}.
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DR EMBL; AY230846; AAP86673.1; -; mRNA.
DR EMBL; AY230847; AAP86674.1; -; mRNA.
DR EMBL; AC009519; AAF19671.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34249.1; -; Genomic_DNA.
DR EMBL; AF410265; AAK95251.1; -; mRNA.
DR EMBL; AY039857; AAK63961.1; -; mRNA.
DR EMBL; AY143888; AAN28827.1; -; mRNA.
DR PIR; H96668; H96668.
DR RefSeq; NP_176633.1; NM_105127.4.
DR AlphaFoldDB; Q9SGW3; -.
DR SMR; Q9SGW3; -.
DR BioGRID; 27981; 104.
DR IntAct; Q9SGW3; 8.
DR STRING; 3702.AT1G64520.1; -.
DR iPTMnet; Q9SGW3; -.
DR SwissPalm; Q9SGW3; -.
DR PaxDb; Q9SGW3; -.
DR PRIDE; Q9SGW3; -.
DR ProteomicsDB; 226351; -.
DR DNASU; 842760; -.
DR EnsemblPlants; AT1G64520.1; AT1G64520.1; AT1G64520.
DR GeneID; 842760; -.
DR Gramene; AT1G64520.1; AT1G64520.1; AT1G64520.
DR KEGG; ath:AT1G64520; -.
DR Araport; AT1G64520; -.
DR TAIR; locus:2019504; AT1G64520.
DR eggNOG; KOG3151; Eukaryota.
DR HOGENOM; CLU_046003_0_0_1; -.
DR InParanoid; Q9SGW3; -.
DR OMA; VYIRHPL; -.
DR OrthoDB; 1183195at2759; -.
DR PhylomeDB; Q9SGW3; -.
DR PRO; PR:Q9SGW3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGW3; baseline and differential.
DR Genevisible; Q9SGW3; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0048825; P:cotyledon development; IMP:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0048528; P:post-embryonic root development; IMP:TAIR.
DR GO; GO:0043248; P:proteasome assembly; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:TAIR.
DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR GO; GO:0031540; P:regulation of anthocyanin biosynthetic process; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0051788; P:response to misfolded protein; IMP:TAIR.
DR GO; GO:0009647; P:skotomorphogenesis; IMP:TAIR.
DR InterPro; IPR006746; 26S_Psome_Rpn12.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR12387; PTHR12387; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytokinin signaling pathway; Proteasome; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..267
FT /note="26S proteasome non-ATPase regulatory subunit 8
FT homolog A"
FT /id="PRO_0000397122"
FT DOMAIN 79..251
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:20516081,
FT ECO:0007744|PubMed:22223895"
FT CONFLICT 182
FT /note="T -> P (in Ref. 1; AAP86674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 30706 MW; D3EC626161AAA4E8 CRC64;
MDPQLTEVSQ QFERFKAAFA RKDYNTCSDL LSQLKVLLTK FTSLPPLFEN SPNAAKELTI
ARDIYEHAVV LSVKTEDQDA FERDFFQLKP YYVDARNRIP QSPQENLILG LNLLRLLVQN
RIAEFHTELE LLSSATLEDP CIKHAVELEQ SFMEGAYNRV LSARQTAPDA TYVYFMDLLA
KTIRDEIAGC SEKAYDYVSI SDARQMLLFS SDQELLTYVT DEHPEWEVKE GFVVFQKAKE
TAPCKEIPSL QLINQTLSYA RELERIV
