PS6AB_ARATH
ID PS6AB_ARATH Reviewed; 423 AA.
AC O04019; Q93V77;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=26S proteasome regulatory subunit 6A homolog B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT5b;
DE AltName: Full=Proteasome 26S subunit 6A homolog B;
DE AltName: Full=Regulatory particle triple-A ATPase subunit 5b;
DE AltName: Full=Tat-binding protein 1 homolog B;
DE Short=TBP-1 homolog B;
GN Name=RPT5B; Synonyms=TBP1; OrderedLocusNames=At1g09100; ORFNames=F7G19.2;
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 [GENOMIC DNA].
RC STRAIN=cv. Wassilewskija;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 INTERACTION WITH HXK1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17081979; DOI=10.1016/j.cell.2006.09.028;
RA Cho Y.H., Yoo S.D., Sheen J.;
RT "Regulatory functions of nuclear hexokinase1 complex in glucose
RT signaling.";
RL Cell 127:579-589(2006).
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).
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:17081979}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70397.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU980096; ACJ66733.1; -; Genomic_DNA.
DR EMBL; AC000106; AAB70397.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE28396.1; -; Genomic_DNA.
DR EMBL; AY050423; AAK91439.1; -; mRNA.
DR EMBL; AF412095; AAL06548.1; -; mRNA.
DR EMBL; AY124813; AAM70522.1; -; mRNA.
DR PIR; C86223; C86223.
DR RefSeq; NP_172384.1; NM_100781.5.
DR AlphaFoldDB; O04019; -.
DR SMR; O04019; -.
DR BioGRID; 22672; 91.
DR IntAct; O04019; 5.
DR STRING; 3702.AT1G09100.1; -.
DR MoonProt; O04019; -.
DR iPTMnet; O04019; -.
DR MetOSite; O04019; -.
DR PaxDb; O04019; -.
DR PRIDE; O04019; -.
DR ProteomicsDB; 226343; -.
DR EnsemblPlants; AT1G09100.1; AT1G09100.1; AT1G09100.
DR GeneID; 837431; -.
DR Gramene; AT1G09100.1; AT1G09100.1; AT1G09100.
DR KEGG; ath:AT1G09100; -.
DR Araport; AT1G09100; -.
DR TAIR; locus:2036099; AT1G09100.
DR eggNOG; KOG0652; Eukaryota.
DR HOGENOM; CLU_000688_2_4_1; -.
DR InParanoid; O04019; -.
DR OMA; HEKAAMG; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; O04019; -.
DR PRO; PR:O04019; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04019; baseline and differential.
DR Genevisible; O04019; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
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:0032991; C:protein-containing complex; IMP:CAFA.
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:0010255; P:glucose mediated signaling pathway; IMP: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 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CAFA.
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 Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..423
FT /note="26S proteasome regulatory subunit 6A homolog B"
FT /id="PRO_0000084703"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI4"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI3"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI2"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SEI2"
SQ SEQUENCE 423 AA; 47038 MW; E7236A9547CE1EA7 CRC64;
MATAMAEDTS FEGDQLASMT TDDIGRASRL LANEIRILKE ESQRTNLDLE SVKEKIKENQ
EKIKLNKQLP YLVGNIVEIL EMSPEDDAEE DGANIDLDSQ RKGKCVVLKT STRQTIFLPV
VGLVDPDTLK PGDLVGVNKD SYLILDTLPS EYDSRVKAME VDEKPTEDYN DIGGLEKQIQ
ELVEAIVLPM THKEQFEKLG IRPPKGVLLY GPPGTGKTLM ARACAAQTNA TFLKLAGPQL
VQMFIGDGAK LVRDAFLLAK EKSPCIIFID EIDAIGTKRF DSEVSGDREV QRTMLELLNQ
LDGFSSDDRI KVIAATNRAD ILDPALMRSG RLDRKIEFPH PTEEARGRIL QIHSRKMNVN
ADVNFEELAR STDDFNGAQL KAVCVEAGML ALRRDATEVN HEDFNEGIIQ VQAKKKASLN
YYA
