PS6AA_ARATH
ID PS6AA_ARATH Reviewed; 424 AA.
AC Q9SEI2; Q8H195; Q9SWY7;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=26S proteasome regulatory subunit 6A homolog A {ECO:0000305};
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT5a {ECO:0000303|PubMed:10417703};
DE AltName: Full=Proteasome 26S subunit 6A homolog A {ECO:0000305};
DE AltName: Full=Regulatory particle triple-A ATPase subunit 5a {ECO:0000305};
DE AltName: Full=Tat-binding protein 1 homolog A;
DE Short=TBP-1 homolog A;
GN Name=RPT5A {ECO:0000303|PubMed:10417703};
GN Synonyms=ATS6A.2 {ECO:0000303|PubMed:9878390}, TBP1 {ECO:0000305};
GN OrderedLocusNames=At3g05530 {ECO:0000312|Araport:AT3G05530};
GN ORFNames=F22F7.1 {ECO:0000312|EMBL:AAF64530.1};
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=9878390; DOI=10.1006/jmbi.1998.2315;
RA Kwok S.F., Staub J.M., Deng X.-W.;
RT "Characterization of two subunits of Arabidopsis 19S proteasome regulatory
RT complex and its possible interaction with the COP9 complex.";
RL J. Mol. Biol. 285:85-95(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=19223514; DOI=10.1105/tpc.108.062372;
RA Gallois J.-L., Guyon-Debast A., Lecureuil A., Vezon D., Carpentier V.,
RA Bonhomme S., Guerche P.;
RT "The Arabidopsis proteasome RPT5 subunits are essential for gametophyte
RT development and show accession-dependent redundancy.";
RL Plant Cell 21:442-459(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, ACETYLATION AT THR-278, UBIQUITINATION AT LYS-279 AND
RP LYS-416, AND CLEAVAGE OF INITIATOR METHIONINE.
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.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
RN [11]
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).
CC -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex (Probable). Interacts with transit peptides of proteins
CC targeted to the chloroplast, and may be involved in the degradation of
CC unimported plastid protein precursors (PubMed:24846764). Plays a
CC essential role in the gametophyte development (PubMed:19223514).
CC Involved in tolerance to zinc deficiency, possibly through alleviation
CC of oxidative stresses or processing of poly-ubiquitinated proteins
CC (PubMed:21389614). {ECO:0000269|PubMed:19223514,
CC ECO:0000269|PubMed:21389614, ECO:0000269|PubMed:24846764, ECO:0000305}.
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. {ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9878390}. Nucleus
CC {ECO:0000269|PubMed:9878390}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9878390}.
CC -!- DISRUPTION PHENOTYPE: Displays a severe male gametophyte development
CC defects in cv. Wassilewskija but not in cv. Columbia due to the
CC complementation by RPT5B. {ECO:0000269|PubMed:19223514}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF081573; AAD46145.1; -; mRNA.
DR EMBL; AF123394; AAF22525.1; -; mRNA.
DR EMBL; AC009606; AAF64530.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74254.1; -; Genomic_DNA.
DR EMBL; AY062705; AAL32783.1; -; mRNA.
DR EMBL; BT000140; AAN15459.1; -; mRNA.
DR RefSeq; NP_187204.1; NM_111426.4.
DR AlphaFoldDB; Q9SEI2; -.
DR SMR; Q9SEI2; -.
DR BioGRID; 5053; 94.
DR IntAct; Q9SEI2; 5.
DR STRING; 3702.AT3G05530.1; -.
DR iPTMnet; Q9SEI2; -.
DR PaxDb; Q9SEI2; -.
DR PRIDE; Q9SEI2; -.
DR ProteomicsDB; 226384; -.
DR EnsemblPlants; AT3G05530.1; AT3G05530.1; AT3G05530.
DR GeneID; 819718; -.
DR Gramene; AT3G05530.1; AT3G05530.1; AT3G05530.
DR KEGG; ath:AT3G05530; -.
DR Araport; AT3G05530; -.
DR TAIR; locus:2079742; AT3G05530.
DR eggNOG; KOG0652; Eukaryota.
DR HOGENOM; CLU_000688_2_4_1; -.
DR InParanoid; Q9SEI2; -.
DR OMA; HEANCSF; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; Q9SEI2; -.
DR PRO; PR:Q9SEI2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SEI2; baseline and differential.
DR Genevisible; Q9SEI2; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0009553; P:embryo sac development; IGI:TAIR.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IGI:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 Acetylation; ATP-binding; Cytoplasm; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Proteasome; Reference proteome; Stress response;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20516081,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..424
FT /note="26S proteasome regulatory subunit 6A homolog A"
FT /id="PRO_0000391485"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI4"
FT MOD_RES 278
FT /note="O-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI3"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CONFLICT 271
FT /note="D -> Y (in Ref. 5; AAN15459)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="N -> H (in Ref. 1; AAD46145)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="N -> H (in Ref. 1; AAD46145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47480 MW; 99E7F04505E713B7 CRC64;
MATPMVEDTS SFEEDQLASM STEDITRATR LLDNEIRILK EDAQRTNLEC DSYKEKIKEN
QEKIKLNKQL PYLVGNIVEI LEMNPEDDAE EDGANIDLDS QRKGKCVVLK TSTRQTIFLP
VVGLVDPDSL KPGDLVGVNK DSYLILDTLP SEYDSRVKAM EVDEKPTEDY NDIGGLEKQI
QELVEAIVLP MTHKERFEKL GVRPPKGVLL YGPPGTGKTL MARACAAQTN ATFLKLAGPQ
LVQMFIGDGA KLVRDAFQLA KEKAPCIIFI DEIDAIGTKR FDSEVSGDRE VQRTMLELLN
QLDGFSSDER IKVIAATNRA DILDPALMRS GRLDRKIEFP HPTEEARARI LQIHSRKMNV
HPDVNFEELA RSTDDFNGAQ LKAVCVEAGM LALRRDATEV NHEDFNEGII QVQAKKKASL
NYYA
