26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B)

 PS6AB_ARATH             Reviewed;         423 AA.
 O04019; Q93V77;
 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
 09-FEB-2010, sequence version 3.
 23-FEB-2022, entry version 148.
 RecName: Full=26S proteasome regulatory subunit 6A homolog B;
 AltName: Full=26S proteasome AAA-ATPase subunit RPT5b;
 AltName: Full=Proteasome 26S subunit 6A homolog B;
 AltName: Full=Regulatory particle triple-A ATPase subunit 5b;
 AltName: Full=Tat-binding protein 1 homolog B;
          Short=TBP-1 homolog B;
 Name=RPT5B; Synonyms=TBP1; OrderedLocusNames=At1g09100; ORFNames=F7G19.2;
 Arabidopsis thaliana (Mouse-ear cress).
 Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
 Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
 rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
 NCBI_TaxID=3702;
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 STRAIN=cv. Wassilewskija;
 PubMed=19223514; DOI=10.1105/tpc.108.062372;
 Gallois J.-L., Guyon-Debast A., Lecureuil A., Vezon D., Carpentier V.,
 Bonhomme S., Guerche P.;
 "The Arabidopsis proteasome RPT5 subunits are essential for gametophyte
 development and show accession-dependent redundancy.";
 Plant Cell 21:442-459(2009).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=cv. Columbia;
 PubMed=11130712; DOI=10.1038/35048500;
 Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
 Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
 Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
 Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
 Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
 Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
 Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
 Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
 Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
 Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
 Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
 Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
 Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
 Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
 Yu G., Fraser C.M., Venter J.C., Davis R.W.;
 "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
 Nature 408:816-820(2000).
 [3]
 GENOME REANNOTATION.
 STRAIN=cv. Columbia;
 PubMed=27862469; DOI=10.1111/tpj.13415;
 Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
 Town C.D.;
 "Araport11: a complete reannotation of the Arabidopsis thaliana reference
 genome.";
 Plant J. 89:789-804(2017).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=cv. Columbia;
 PubMed=14593172; DOI=10.1126/science.1088305;
 Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
 Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
 Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
 Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
 Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
 Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
 Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
 Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
 Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
 Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
 Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
 Ecker J.R.;
 "Empirical analysis of transcriptional activity in the Arabidopsis
 genome.";
 Science 302:842-846(2003).
 [5]
 GENE FAMILY, AND NOMENCLATURE.
 PubMed=10417703; DOI=10.1046/j.1365-313x.1999.00479.x;
 Fu H., Doelling J.H., Rubin D.M., Vierstra R.D.;
 "Structural and functional analysis of the six regulatory particle triple-A
 ATPase subunits from the Arabidopsis 26S proteasome.";
 Plant J. 18:529-539(1999).
 [6]
 SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
 PubMed=14623884; DOI=10.1074/jbc.m311977200;
 Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.;
 "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular
 analyses revealed the presence of multiple isoforms.";
 J. Biol. Chem. 279:6401-6413(2004).
 [7]
 INTERACTION WITH HXK1, SUBCELLULAR LOCATION, AND FUNCTION.
 PubMed=17081979; DOI=10.1016/j.cell.2006.09.028;
 Cho Y.H., Yoo S.D., Sheen J.;
 "Regulatory functions of nuclear hexokinase1 complex in glucose
 signaling.";
 Cell 127:579-589(2006).
 [8]
 IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
 COMPLEX, AND SUBUNIT.
 PubMed=20516081; DOI=10.1074/jbc.m110.136622;
 Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.;
 "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse
 array of plant proteolytic complexes.";
 J. Biol. Chem. 285:25554-25569(2010).
 -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
     degradation of ubiquitinated proteins. The regulatory (or ATPase)
     complex confers ATP dependency and substrate specificity to the 26S
     complex. {ECO:0000269|PubMed:17081979}.
 -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) base
     subcomplex of the 26S proteasome. The 26S proteasome is composed of a
     core protease (CP), known as the 20S proteasome, capped at one or both
     ends by the 19S regulatory particle (RP/PA700). The RP/PA700 complex is
     composed of at least 17 different subunits in two subcomplexes, the
     base and the lid, which form the portions proximal and distal to the
     20S proteolytic core, respectively. {ECO:0000269|PubMed:14623884,
     ECO:0000269|PubMed:20516081}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
 -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAB70397.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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 EMBL; EU980096; ACJ66733.1; -; Genomic_DNA.
 EMBL; AC000106; AAB70397.1; ALT_INIT; Genomic_DNA.
 EMBL; CP002684; AEE28396.1; -; Genomic_DNA.
 EMBL; AY050423; AAK91439.1; -; mRNA.
 EMBL; AF412095; AAL06548.1; -; mRNA.
 EMBL; AY124813; AAM70522.1; -; mRNA.
 PIR; C86223; C86223.
 RefSeq; NP_172384.1; NM_100781.5.
 SMR; O04019; -.
 BioGRID; 22672; 91.
 IntAct; O04019; 5.
 STRING; 3702.AT1G09100.1; -.
 MoonProt; O04019; -.
 iPTMnet; O04019; -.
 MetOSite; O04019; -.
 PaxDb; O04019; -.
 PRIDE; O04019; -.
 ProteomicsDB; 226343; -.
 EnsemblPlants; AT1G09100.1; AT1G09100.1; AT1G09100.
 GeneID; 837431; -.
 Gramene; AT1G09100.1; AT1G09100.1; AT1G09100.
 KEGG; ath:AT1G09100; -.
 Araport; AT1G09100; -.
 TAIR; locus:2036099; AT1G09100.
 eggNOG; KOG0652; Eukaryota.
 HOGENOM; CLU_000688_2_4_1; -.
 InParanoid; O04019; -.
 OMA; KPTEQYT; -.
 OrthoDB; 571919at2759; -.
 PhylomeDB; O04019; -.
 PRO; PR:O04019; -.
 Proteomes; UP000006548; Chromosome 1.
 ExpressionAtlas; O04019; baseline and differential.
 Genevisible; O04019; AT.
 GO; GO:0005829; C:cytosol; HDA:TAIR.
 GO; GO:0005576; C:extracellular region; HDA:TAIR.
 GO; GO:0005634; C:nucleus; IDA:CAFA.
 GO; GO:0000502; C:proteasome complex; IDA:TAIR.
 GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
 GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
 GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
 GO; GO:0009553; P:embryo sac development; IGI:TAIR.
 GO; GO:0010255; P:glucose mediated signaling pathway; IMP:TAIR.
 GO; GO:0009555; P:pollen development; IGI:TAIR.
 GO; GO:0010498; P:proteasomal protein catabolic process; IGI:TAIR.
 GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CAFA.
 Gene3D; 3.40.50.300; -; 1.
 InterPro; IPR005937; 26S_Psome_P45-like.
 InterPro; IPR003593; AAA+_ATPase.
 InterPro; IPR041569; AAA_lid_3.
 InterPro; IPR003959; ATPase_AAA_core.
 InterPro; IPR003960; ATPase_AAA_CS.
 InterPro; IPR027417; P-loop_NTPase.
 InterPro; IPR032501; Prot_ATP_ID_OB.
 Pfam; PF00004; AAA; 1.
 Pfam; PF17862; AAA_lid_3; 1.
 Pfam; PF16450; Prot_ATP_ID_OB; 1.
 SMART; SM00382; AAA; 1.
 SUPFAM; SSF52540; SSF52540; 1.
 TIGRFAMs; TIGR01242; 26Sp45; 1.
 PROSITE; PS00674; AAA; 1.
 1: Evidence at protein level;
 ATP-binding; Cytoplasm; Isopeptide bond; Nucleotide-binding; Nucleus;
 Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
 CHAIN           1..423
                 /note="26S proteasome regulatory subunit 6A homolog B"
                 /id="PRO_0000084703"
 NP_BIND         211..218
                 /note="ATP"
                 /evidence="ECO:0000255"
 MOD_RES         18
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q9SEI4"
 CROSSLNK        234
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in ubiquitin)"
                 /evidence="ECO:0000250|UniProtKB:Q9SEI3"
 CROSSLNK        278
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in ubiquitin)"
                 /evidence="ECO:0000250|UniProtKB:Q9SEI2"
 CROSSLNK        415
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in ubiquitin)"
                 /evidence="ECO:0000250|UniProtKB:Q9SEI2"
 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

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