PRS6B_ARATH
ID PRS6B_ARATH Reviewed; 408 AA.
AC Q9SEI4; Q5PNS4;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=26S proteasome regulatory subunit 6B homolog;
DE AltName: Full=26S protease subunit 6B homolog;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT3;
DE AltName: Full=Protein BMAA insensitive morphology 409;
DE AltName: Full=Regulatory particle triple-A ATPase subunit 3;
GN Name=RPT3; Synonyms=BIM409; OrderedLocusNames=At5g58290; ORFNames=MCK7.16;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP MUTAGENESIS OF GLY-158, AND FUNCTION.
RX PubMed=19412571; DOI=10.1007/s11103-009-9489-7;
RA Brenner E.D., Feinberg P., Runko S., Coruzzi G.M.;
RT "A mutation in the proteosomal regulatory particle AAA-ATPase-3 in
RT Arabidopsis impairs the light-specific hypocotyl elongation response
RT elicited by a glutamate receptor agonist, BMAA.";
RL Plant Mol. Biol. 70:523-533(2009).
RN [9]
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 [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).
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. {ECO:0000269|PubMed:19412571}.
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:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in dark-grown etiolated seedlings, roots,
CC leaves, stems and flowers.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF123392; AAF22523.1; -; mRNA.
DR EMBL; AB019228; BAA96920.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97029.1; -; Genomic_DNA.
DR EMBL; AY070466; AAL49932.1; -; mRNA.
DR EMBL; BT020373; AAV85728.1; -; mRNA.
DR RefSeq; NP_200637.1; NM_125214.6.
DR AlphaFoldDB; Q9SEI4; -.
DR SMR; Q9SEI4; -.
DR BioGRID; 21185; 173.
DR IntAct; Q9SEI4; 7.
DR STRING; 3702.AT5G58290.1; -.
DR iPTMnet; Q9SEI4; -.
DR MetOSite; Q9SEI4; -.
DR PaxDb; Q9SEI4; -.
DR PRIDE; Q9SEI4; -.
DR ProteomicsDB; 226295; -.
DR EnsemblPlants; AT5G58290.1; AT5G58290.1; AT5G58290.
DR GeneID; 835941; -.
DR Gramene; AT5G58290.1; AT5G58290.1; AT5G58290.
DR KEGG; ath:AT5G58290; -.
DR Araport; AT5G58290; -.
DR TAIR; locus:2161258; AT5G58290.
DR eggNOG; KOG0727; Eukaryota.
DR HOGENOM; CLU_000688_2_0_1; -.
DR OMA; AYAAQVK; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; Q9SEI4; -.
DR BRENDA; 5.6.1.5; 399.
DR PRO; PR:Q9SEI4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SEI4; baseline and differential.
DR Genevisible; Q9SEI4; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
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: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: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 InterPro; IPR035256; PSMC4.
DR PANTHER; PTHR23073:SF120; PTHR23073:SF120; 1.
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; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..408
FT /note="26S proteasome regulatory subunit 6B homolog"
FT /id="PRO_0000084692"
FT COILED 28..75
FT /evidence="ECO:0000255"
FT BINDING 196..203
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 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MUTAGEN 158
FT /note="G->E: Impairs the light-specific hypocotyl
FT elongation response elicited by a glutamate receptor
FT agonist, BMAA."
FT /evidence="ECO:0000269|PubMed:19412571"
SQ SEQUENCE 408 AA; 45751 MW; A1045D85BF3BBEE4 CRC64;
MASAAVASMV LDPKASPALM DLSTADEEDL YGRLKSLERQ LEFTDIQEEY VKDEQKNLKR
ELLRAQEEVK RIQSVPLVIG QFMEMVDQNN GIVGSTTGSN YYVRILSTIN RELLKPSASV
ALHRHSNALV DVLPPEADSS ISLLSQSEKP DVSYNDIGGC DIQKQEIREA VELPLTHHEL
YKQIGIDPPR GVLLYGPPGT GKTMLAKAVA NHTTAAFIRV VGSEFVQKYL GEGPRMVRDV
FRLAKENAPA IIFIDEVDAI ATARFDAQTG ADREVQRILM ELLNQMDGFD QTVNVKVIMA
TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLVFQVCTS KMNLSDEVDL EDYVSRPDKI
SAAEIAAICQ EAGMHAVRKN RYVILPKDFE KGYRANVKKP DTDFEFYK
