PRS4B_ARATH
ID PRS4B_ARATH Reviewed; 443 AA.
AC Q9SL67; Q8LAV7; Q94JT0;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=26S proteasome regulatory subunit 4 homolog B {ECO:0000305};
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT2b {ECO:0000303|PubMed:10417703};
DE AltName: Full=26S proteasome subunit 4 homolog B {ECO:0000305};
DE AltName: Full=Regulatory particle triple-A ATPase subunit 2b {ECO:0000305};
GN Name=RPT2B {ECO:0000303|PubMed:10417703};
GN OrderedLocusNames=At2g20140 {ECO:0000312|Araport:AT2G20140};
GN ORFNames=T2G17.6 {ECO:0000312|EMBL:AAD24384.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
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 [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 TISSUE SPECIFICITY.
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP 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 [10]
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).
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). Acts redundantly with RPT2A in the regulation of
CC gametogenesis (PubMed:21784786, PubMed:22158466). With RPT2A plays a
CC critical role in 26S proteasome assembly (PubMed:22158466).
CC {ECO:0000269|PubMed:21784786, ECO:0000269|PubMed:22158466}.
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:22158466}. Nucleus
CC {ECO:0000269|PubMed:22158466}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the root and shoot
CC apical meristem. {ECO:0000269|PubMed:19500299}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:22158466). The double mutants rpt2a and rpt2b are
CC blocked in both male and female gametogenesis (PubMed:22158466,
CC 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; AC006081; AAD24384.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06970.1; -; Genomic_DNA.
DR EMBL; AF372977; AAK50114.1; -; mRNA.
DR EMBL; AY035072; AAK59577.1; -; mRNA.
DR EMBL; AY056335; AAL07184.1; -; mRNA.
DR EMBL; AY087584; AAM65126.1; -; mRNA.
DR PIR; E84585; E84585.
DR RefSeq; NP_179604.1; NM_127572.4.
DR AlphaFoldDB; Q9SL67; -.
DR SMR; Q9SL67; -.
DR BioGRID; 1887; 164.
DR IntAct; Q9SL67; 1.
DR STRING; 3702.AT2G20140.1; -.
DR iPTMnet; Q9SL67; -.
DR PaxDb; Q9SL67; -.
DR PRIDE; Q9SL67; -.
DR ProteomicsDB; 226222; -.
DR EnsemblPlants; AT2G20140.1; AT2G20140.1; AT2G20140.
DR GeneID; 816533; -.
DR Gramene; AT2G20140.1; AT2G20140.1; AT2G20140.
DR KEGG; ath:AT2G20140; -.
DR Araport; AT2G20140; -.
DR TAIR; locus:2061639; AT2G20140.
DR eggNOG; KOG0726; Eukaryota.
DR HOGENOM; CLU_000688_2_3_1; -.
DR InParanoid; Q9SL67; -.
DR OMA; ARCKLRY; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; Q9SL67; -.
DR PRO; PR:Q9SL67; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL67; baseline and differential.
DR Genevisible; Q9SL67; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0010078; P:maintenance of root meristem identity; IMP:TAIR.
DR GO; GO:0048232; P:male gamete generation; 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 ATP-binding; Cytoplasm; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..443
FT /note="26S proteasome regulatory subunit 4 homolog B"
FT /id="PRO_0000391484"
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 10
FT /note="N -> H (in Ref. 4; AAM65126)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="M -> V (in Ref. 3; AAK50114)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="V -> G (in Ref. 4; AAM65126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 49347 MW; EEA39B499CED5B99 CRC64;
MGQGPSGGLN RQGDRKPDGG EKKEKKFEPA 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
NSGGEREIQR TMLELLNQLD GFDSRGDVKV ILATNRIESL DPALLRPGRI DRKIEFPLPD
IKTRRRIFQI HTSKMTLAED VNLEEFVMTK DEFSGADIKA ICTEAGLLAL RERRMKVTHV
DFKKAKEKVM FKKKEGVPEG LYM
