PSD2B_ARATH
ID PSD2B_ARATH Reviewed; 891 AA.
AC Q6XJG8; O49456;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 2 homolog B;
DE AltName: Full=26S proteasome regulatory subunit RPN1b;
DE Short=AtRPN1b;
DE AltName: Full=26S proteasome regulatory subunit S2 homolog B;
GN Name=RPN1B; OrderedLocusNames=At4g28470; ORFNames=F20O9.150;
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=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 [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 DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16169895; DOI=10.1105/tpc.105.034975;
RA Brukhin V., Gheyselinck J., Gagliardini V., Genschik P., Grossniklaus U.;
RT "The RPN1 subunit of the 26S proteasome in Arabidopsis is essential for
RT embryogenesis.";
RL Plant Cell 17:2723-2737(2005).
RN [5]
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).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Expressed in stems, leaves, buds, flowers, siliques
CC and developing seeds. {ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:16169895}.
CC -!- DEVELOPMENTAL STAGE: Detected in the entire flower with strong signals
CC in carpels, especially in differentiating ovules and the carpel wall.
CC Patchy localization with strong levels in particular cells. In anthers,
CC present at a high level in tetrads of microspores and the tapetum.
CC After fertilization, mostly observed in the embryo up to the heart
CC stage and in the chalazal endospem. Expressed at high levels in silique
CC wall at all stages of carpel development.
CC {ECO:0000269|PubMed:16169895}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Normal phenotype. {ECO:0000269|PubMed:16169895}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16886.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA16886.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB79649.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79649.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY230829; AAP86656.1; -; mRNA.
DR EMBL; AL021749; CAA16886.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161572; CAB79649.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85490.1; -; Genomic_DNA.
DR PIR; T04617; T04617.
DR RefSeq; NP_194576.5; NM_118989.6.
DR AlphaFoldDB; Q6XJG8; -.
DR SMR; Q6XJG8; -.
DR BioGRID; 14251; 138.
DR IntAct; Q6XJG8; 2.
DR STRING; 3702.AT4G28470.1; -.
DR iPTMnet; Q6XJG8; -.
DR MetOSite; Q6XJG8; -.
DR PaxDb; Q6XJG8; -.
DR PRIDE; Q6XJG8; -.
DR ProteomicsDB; 226006; -.
DR EnsemblPlants; AT4G28470.1; AT4G28470.1; AT4G28470.
DR GeneID; 828964; -.
DR Gramene; AT4G28470.1; AT4G28470.1; AT4G28470.
DR KEGG; ath:AT4G28470; -.
DR Araport; AT4G28470; -.
DR TAIR; locus:2121358; AT4G28470.
DR eggNOG; KOG2005; Eukaryota.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; Q6XJG8; -.
DR OMA; MAPPENP; -.
DR OrthoDB; 229956at2759; -.
DR PhylomeDB; Q6XJG8; -.
DR PRO; PR:Q6XJG8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6XJG8; baseline and differential.
DR Genevisible; Q6XJG8; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Proteasome; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..891
FT /note="26S proteasome non-ATPase regulatory subunit 2
FT homolog B"
FT /id="PRO_0000399922"
FT REPEAT 414..447
FT /note="PC 1"
FT REPEAT 448..484
FT /note="PC 2"
FT REPEAT 485..519
FT /note="PC 3"
FT REPEAT 522..556
FT /note="PC 4"
FT REPEAT 565..594
FT /note="PC 5"
FT REPEAT 674..705
FT /note="PC 6"
FT REPEAT 724..739
FT /note="PC 7"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 97954 MW; 8330D4146ED9F371 CRC64;
MAPVPDPNSV GGGAKRDEAT TKIPSKDSKK KDDKKEEDLS EEDLQLKQNL ELYVERVQDP
NPELQKIALE SMRKEIRDST SSMTSVPKPL KFLRPHYGVL KEFHAKMAES DLKKMLADIL
SVLALTMSAE GERESLNYRL NGSESDIGSW GHEYVRNLAG EIAKEYTIRQ GEESSIEDLM
DLVQQIVSFH MKHNAETEAV DLLMDVEDLD LLLEHVDNTN FRRTCNYLTS AAKYLPGPDD
MLVLDIAYMI YIKFAEYPNA LQIALFLDNM QYVKQVFTSC TDLVKKKQFC YMIARHGMTF
ELDQEMVAND EDKEALQDIV NNSKLSEGYL TLARDIEVME AKTPEDIYKA HLLDGRASSG
PSVDSARQNL SATFVNAFVN AGFGQDKLMT VPSDSTSGSA GNWLFKNKEH GKTSAVASLG
MIQLWDVETG LGHLDKYFHS NDNPVVAGAL LGVGIVNCGI KNDCDPAFAL LSGYIDNEDS
SVRIGAIMGL GIAYAGSQND QIKIRLSPIL NDANAPLDVI AFAALSLGMI YVGSCNEEVA
QSIIFALMDR SEAELGEALT RFLPLGLGLL YLGKQESVEA TAEVSKTFNE KIRKYCDMTL
LSCAYAGTGN VLKVQDLLAQ CGEHLVKGDI HQGPAVIGLA MVAMSEELGL DMEIRSLERV
LQYGEQNIRR AVPLALGLLC ISNPKVTVMD TLSRLSHDTD SEVAMAAIIS LGLIGAGTNN
ARIAGMLRNL SSYYYKDASL LFCVRIAQGF VHMGKGLLTL NPFHSERLLL SPTALAGIVT
LLHACLDMKS IILGKYHYVL YFLVLAMQPR MMLTVDQSLK PISVPVRVGQ AVDVVGQAGR
PKTITGFQTH STPVLLAAGE RAELATEKYI PLSPILEGFV ILKENPDYRE E
