PRS4A_ARATH
ID PRS4A_ARATH Reviewed; 443 AA.
AC Q9SZD4; Q9SEI5;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=26S proteasome regulatory subunit 4 homolog A {ECO:0000305};
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT2a {ECO:0000303|PubMed:10417703};
DE AltName: Full=26S proteasome subunit 4 homolog A {ECO:0000305};
DE AltName: Full=Protein HALTED ROOT {ECO:0000303|PubMed:15073153};
DE AltName: Full=Regulatory particle triple-A ATPase subunit 2a {ECO:0000305};
GN Name=RPT2A {ECO:0000303|PubMed:10417703};
GN Synonyms=HLR {ECO:0000303|PubMed:15073153};
GN OrderedLocusNames=At4g29040 {ECO:0000312|Araport:AT4G29040};
GN ORFNames=F19B15.70 {ECO:0000312|EMBL:CAB43918.1}, F25O24.6;
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], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=10417703; DOI=10.1046/j.1365-313x.1999.00479.x;
RA Fu H., Doelling J.H., Rubin D.M., Vierstra R.D.;
RT "Structural and functional analysis of the six regulatory particle triple-A
RT ATPase subunits from the Arabidopsis 26S proteasome.";
RL Plant J. 18:529-539(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=15073153; DOI=10.1242/dev.01096;
RA Ueda M., Matsui K., Ishiguro S., Sano R., Wada T., Paponov I., Palme K.,
RA Okada K.;
RT "The HALTED ROOT gene encoding the 26S proteasome subunit RPT2a is
RT essential for the maintenance of Arabidopsis meristems.";
RL Development 131:2101-2111(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
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 DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19500299; DOI=10.1111/j.1365-313x.2009.03932.x;
RA Sonoda Y., Sako K., Maki Y., Yamazaki N., Yamamoto H., Ikeda A.,
RA Yamaguchi J.;
RT "Regulation of leaf organ size by the Arabidopsis RPT2a 19S proteasome
RT subunit.";
RL Plant J. 60:68-78(2009).
RN [9]
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 [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).
RN [11]
RP FUNCTION.
RX PubMed=20195883; DOI=10.1007/s10265-010-0321-x;
RA Sako K., Maki Y., Aoyama T., Goto D.B., Yamaguchi J.;
RT "Control of endoreduplication of trichome by RPT2a, a subunit of the 19S
RT proteasome in Arabidopsis.";
RL J. Plant Res. 123:701-706(2010).
RN [12]
RP FUNCTION.
RX PubMed=21389614; DOI=10.1271/bbb.100794;
RA Sakamoto T., Kamiya T., Sako K., Yamaguchi J., Yamagami M., Fujiwara T.;
RT "Arabidopsis thaliana 26S proteasome subunits RPT2a and RPT5a are crucial
RT for zinc deficiency-tolerance.";
RL Biosci. Biotechnol. Biochem. 75:561-567(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INDUCTION BY PROTEASOME
RP INHIBITOR MG132, AND DISRUPTION PHENOTYPE.
RX PubMed=22158466; DOI=10.1105/tpc.111.089482;
RA Lee K.H., Minami A., Marshall R.S., Book A.J., Farmer L.M., Walker J.M.,
RA Vierstra R.D.;
RT "The RPT2 subunit of the 26S proteasome directs complex assembly, histone
RT dynamics, and gametophyte and sporophyte development in Arabidopsis.";
RL Plant Cell 23:4298-4317(2011).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21784786; DOI=10.1093/pcp/pcr093;
RA Ueda M., Matsui K., Ishiguro S., Kato T., Tabata S., Kobayashi M., Seki M.,
RA Shinozaki K., Okada K.;
RT "Arabidopsis RPT2a encoding the 26S proteasome subunit is required for
RT various aspects of root meristem maintenance, and regulates gametogenesis
RT redundantly with its homolog, RPT2b.";
RL Plant Cell Physiol. 52:1628-1640(2011).
RN [15]
RP FUNCTION, AND INTERACTION WITH UNI.
RX PubMed=21791544; DOI=10.1093/pcp/pcr099;
RA Chung K., Tasaka M.;
RT "RPT2a, a 26S proteasome AAA-ATPase, is directly involved in Arabidopsis
RT CC-NBS-LRR protein uni-1D-induced signaling pathways.";
RL Plant Cell Physiol. 52:1657-1664(2011).
RN [16]
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).
RN [17]
RP FUNCTION.
RX PubMed=24846764; DOI=10.1021/pr401245g;
RA Sako K., Yanagawa Y., Kanai T., Sato T., Seki M., Fujiwara M., Fukao Y.,
RA Yamaguchi J.;
RT "Proteomic analysis of the 26S proteasome reveals its direct interaction
RT with transit peptides of plastid protein precursors for their
RT degradation.";
RL J. Proteome Res. 13:3223-3230(2014).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22615900; DOI=10.1371/journal.pone.0037086;
RA Sako K., Maki Y., Kanai T., Kato E., Maekawa S., Yasuda S., Sato T.,
RA Watahiki M.K., Yamaguchi J.;
RT "Arabidopsis RPT2a, 19S proteasome subunit, regulates gene silencing via
RT DNA methylation.";
RL PLoS ONE 7:E37086-E37086(2012).
CC -!- FUNCTION: The 26S protease is involved in the ATP-dependent degradation
CC of ubiquitinated proteins. The regulatory (or ATPase) complex confers
CC ATP dependency and substrate specificity to the 26S complex
CC (PubMed:22158466) (Probable). Interacts with transit peptides of
CC proteins targeted to the chloroplast, and may be involved in the
CC degradation of unimported plastid protein precursors (PubMed:24846764).
CC Is required for the maintenance of postembryonic root and shoot
CC meristems (PubMed:15073153, PubMed:21784786). Has a specific role in
CC the regulation of organs size (PubMed:19500299, PubMed:19321709). Acts
CC redundantly with RPT2B in the regulation of gametogenesis
CC (PubMed:21784786, PubMed:22158466). With RPT2B plays a critical role in
CC 26S proteasome assembly (PubMed:22158466). Acts as an upstream
CC signaling component for inducing both defense and morphological
CC phenotypes in the constitutive active uni-1D mutant (PubMed:21791544).
CC Acts as negative regulator of endoreduplication in trichome cells
CC (PubMed:20195883). May function after the completion of the third
CC endoreduplication step (8C to 16C) mediated by RHL1 (PubMed:20195883).
CC Acts as negative regulator of transcriptional gene silencing (TGS) at
CC specific endogenous genes through DNA methylation (PubMed:22615900).
CC Promotes post-transcriptional gene silencing (PTGS) by limiting the
CC degradation of transgene aberrant RNAs by the RNA quality control (RQC)
CC machinery, thus favoring their entry into cytoplasmic siRNA bodies
CC where they can trigger PTGS (PubMed:22615900). Involved in tolerance to
CC zinc deficiency, possibly through alleviation of oxidative stresses or
CC processing of poly-ubiquitinated proteins (PubMed:21389614). Required
CC for resistance to the fungal pathogen Golovinomyces cichoracearum
CC (PubMed:22577987). {ECO:0000269|PubMed:15073153,
CC ECO:0000269|PubMed:19321709, ECO:0000269|PubMed:19500299,
CC ECO:0000269|PubMed:20195883, ECO:0000269|PubMed:21389614,
CC ECO:0000269|PubMed:21784786, ECO:0000269|PubMed:21791544,
CC ECO:0000269|PubMed:22158466, ECO:0000269|PubMed:22577987,
CC ECO:0000269|PubMed:22615900, ECO:0000269|PubMed:24846764,
CC ECO:0000305|PubMed:17971041}.
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. Required for innate immunity
CC (PubMed:14623884, PubMed:20516081). Interacts with UNI
CC (PubMed:21791544). {ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081, ECO:0000269|PubMed:21791544}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:22615900}.
CC Nucleus {ECO:0000269|PubMed:22615900}. Note=Localizes to siRNA-bodies
CC in the cytoplasm. {ECO:0000269|PubMed:22615900}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the root and shoot
CC apical meristem. {ECO:0000269|PubMed:15073153,
CC ECO:0000269|PubMed:19500299}.
CC -!- INDUCTION: Induced by treatment with the proteasome inhibitor MG132.
CC {ECO:0000269|PubMed:22158466}.
CC -!- DISRUPTION PHENOTYPE: Displays disruption of cellular organization in
CC the postembryonic root and shoot apical meristems. Leads to decreased
CC 26SP accumulation, resulting in reduced rates of Ub-dependent
CC proteolysis. Shows hypersensitivity to heat shock and increased
CC oxidative stress tolerance. Displays enlarged leaves, stems, flowers,
CC fruits, seeds and embryos, caused by increased cell size and shows
CC increased branch number and nuclear size of trichomes, in correlation
CC with increased ploidy. Mutant displays enhanced susceptibility to the
CC fungal pathogen Golovinomyces cichoracearum. The double mutants rpt2a
CC and rpt2b are blocked in both male and female gametogenesis
CC (PubMed:22158466, PubMed:21784786). {ECO:0000269|PubMed:21784786,
CC ECO:0000269|PubMed:22158466}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF123391; AAF22522.1; -; mRNA.
DR EMBL; AB161192; BAD18016.1; -; mRNA.
DR EMBL; AL078469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078470; CAB43918.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79662.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85578.1; -; Genomic_DNA.
DR EMBL; AY034975; AAK59480.1; -; mRNA.
DR PIR; T08959; T08959.
DR RefSeq; NP_194633.1; NM_119048.4.
DR AlphaFoldDB; Q9SZD4; -.
DR SMR; Q9SZD4; -.
DR BioGRID; 14312; 305.
DR IntAct; Q9SZD4; 36.
DR STRING; 3702.AT4G29040.1; -.
DR PaxDb; Q9SZD4; -.
DR PRIDE; Q9SZD4; -.
DR ProteomicsDB; 226478; -.
DR EnsemblPlants; AT4G29040.1; AT4G29040.1; AT4G29040.
DR GeneID; 829025; -.
DR Gramene; AT4G29040.1; AT4G29040.1; AT4G29040.
DR KEGG; ath:AT4G29040; -.
DR Araport; AT4G29040; -.
DR TAIR; locus:2119926; AT4G29040.
DR eggNOG; KOG0726; Eukaryota.
DR HOGENOM; CLU_000688_2_3_1; -.
DR InParanoid; Q9SZD4; -.
DR OMA; YCPLHIT; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; Q9SZD4; -.
DR PRO; PR:Q9SZD4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZD4; baseline and differential.
DR Genevisible; Q9SZD4; AT.
DR GO; GO:0005634; C:nucleus; TAS:TAIR.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0007292; P:female gamete generation; IGI:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:TAIR.
DR GO; GO:0048232; P:male gamete generation; IGI:TAIR.
DR GO; GO:0035266; P:meristem growth; IMP:TAIR.
DR GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
DR GO; GO:0048827; P:phyllome 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:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0051788; P:response to misfolded protein; IMP:TAIR.
DR GO; GO:0048829; P:root cap development; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010015; P:root morphogenesis; IMP:TAIR.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Immunity; Innate immunity; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Proteasome; Reference proteome;
KW Stress response; Ubl conjugation.
FT CHAIN 1..443
FT /note="26S proteasome regulatory subunit 4 homolog A"
FT /id="PRO_0000391483"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 229..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI2"
FT CROSSLNK 433
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI2"
FT CONFLICT 37
FT /note="G -> V (in Ref. 1; AAF22522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 49370 MW; E2589DB0B59DC288 CRC64;
MGQGPSGGLN RQGDRKPDGG DKKEKKFEPA APPARVGRKQ RKQKGPEAAA RLPTVTPSTK
CKLRLLKLER IKDYLLMEEE FVANQERLKP QEEKAEEDRS KVDDLRGTPM SVGNLEELID
ENHAIVSSSV GPEYYVGILS FVDKDQLEPG CSILMHNKVL SVVGILQDEV DPMVSVMKVE
KAPLESYADI GGLEAQIQEI KEAVELPLTH PELYEDIGIK PPKGVILYGE PGTGKTLLAK
AVANSTSATF LRVVGSELIQ KYLGDGPKLV RELFRVADDL SPSIVFIDEI DAVGTKRYDA
HSGGEREIQR TMLELLNQLD GFDSRGDVKV ILATNRIESL DPALLRPGRI DRKIEFPLPD
IKTRRRIFQI HTSKMTLSED VNLEEFVMTK DEFSGADIKA ICTEAGLLAL RERRMKVTHP
DFKKAKEKVM FKKKEGVPEG LYM
