PRS8B_ARATH
ID PRS8B_ARATH Reviewed; 419 AA.
AC Q94BQ2;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=26S proteasome regulatory subunit 8 homolog B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT6b;
DE AltName: Full=26S proteasome subunit 8 homolog B;
DE AltName: Full=Regulatory particle triple-A ATPase subunit 6b;
GN Name=RPT6B; Synonyms=SUG1; OrderedLocusNames=At5g20000;
GN ORFNames=F28I16.150;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, 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).
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.
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 -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92778.1; -; Genomic_DNA.
DR EMBL; AY039965; AAK64142.1; -; mRNA.
DR EMBL; AY079403; AAL85134.1; -; mRNA.
DR EMBL; AK226206; BAE98371.1; -; mRNA.
DR EMBL; AY087503; AAM65046.1; -; mRNA.
DR RefSeq; NP_197500.1; NM_122007.4.
DR AlphaFoldDB; Q94BQ2; -.
DR SMR; Q94BQ2; -.
DR BioGRID; 17398; 83.
DR IntAct; Q94BQ2; 2.
DR STRING; 3702.AT5G20000.1; -.
DR PaxDb; Q94BQ2; -.
DR PRIDE; Q94BQ2; -.
DR ProteomicsDB; 226221; -.
DR EnsemblPlants; AT5G20000.1; AT5G20000.1; AT5G20000.
DR GeneID; 832122; -.
DR Gramene; AT5G20000.1; AT5G20000.1; AT5G20000.
DR KEGG; ath:AT5G20000; -.
DR Araport; AT5G20000; -.
DR TAIR; locus:2147685; AT5G20000.
DR eggNOG; KOG0728; Eukaryota.
DR HOGENOM; CLU_000688_2_1_1; -.
DR InParanoid; Q94BQ2; -.
DR OMA; ICSAKAT; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; Q94BQ2; -.
DR PRO; PR:Q94BQ2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BQ2; baseline and differential.
DR Genevisible; Q94BQ2; AT.
DR GO; GO:0005634; C:nucleus; TAS:TAIR.
DR GO; GO:0009536; C:plastid; 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; IPR035261; PSMC5.
DR PANTHER; PTHR23073:SF102; PTHR23073:SF102; 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 ATP-binding; Cytoplasm; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Proteasome; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:20516081"
FT CHAIN 2..419
FT /note="26S proteasome regulatory subunit 8 homolog B"
FT /id="PRO_0000391488"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI2"
SQ SEQUENCE 419 AA; 47157 MW; B464FB8131048F1F CRC64;
MAAVGVEARP PVTAMEETCN VKGAAAKQGE GLNKYYLQHL DELQRLQREK SYNLNRLEAQ
RNELNSRVRM LREELQLLQE PGSYVGEVVK VMGKNKVLVK VHPEGKYVVD IDKSIDITKL
TPSTRVALRN DSYVLHLVLP SKVDPLVNLM KVEKVPDSTY DMIGGLDQQI KEIKEVIELP
IKHPELFESL GIAQPKGVLL YGPPGTGKTL LARAVAHHTD CTFIRVSGSE LVQKYIGEGS
RMVRELFVMA REHAPSIIFM DEIDSIGSAR MESGSGNGDS EVQRTMLELL NQLDGFEASN
KIKVLMATNR IDILDQALLR PGRIDRKIEF PNPNEESRFD ILKIHSRKMN LMRGIDLKKI
AEKMNGASGA ELKAVCTEAG MFALRERRVH VTQEDFEMAV AKVMKKDTEK NMSLRKLWK
