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26S proteasome regulatory subunit 6B homolog (26S protease subunit 6B homolog) (26S proteasome AAA-ATPase subunit RPT3) (Protein BMAA insensitive morphology 409) (Regulatory particle triple-A ATPase subunit 3)

 PRS6B_ARATH             Reviewed;         408 AA.
Q9SEI4; Q5PNS4;
22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 129.
RecName: Full=26S proteasome regulatory subunit 6B homolog;
AltName: Full=26S protease subunit 6B homolog;
AltName: Full=26S proteasome AAA-ATPase subunit RPT3;
AltName: Full=Protein BMAA insensitive morphology 409;
AltName: Full=Regulatory particle triple-A ATPase subunit 3;
Name=RPT3; Synonyms=BIM409; OrderedLocusNames=At5g58290;
ORFNames=MCK7.16;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[8]
MUTAGENESIS OF GLY-158, AND FUNCTION.
PubMed=19412571; DOI=10.1007/s11103-009-9489-7;
Brenner E.D., Feinberg P., Runko S., Coruzzi G.M.;
"A mutation in the proteosomal regulatory particle AAA-ATPase-3 in
Arabidopsis impairs the light-specific hypocotyl elongation response
elicited by a glutamate receptor agonist, BMAA.";
Plant Mol. Biol. 70:523-533(2009).
[9]
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).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- 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:19412571}.
-!- 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}.
-!- TISSUE SPECIFICITY: Expressed in dark-grown etiolated seedlings,
roots, leaves, stems and flowers.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF123392; AAF22523.1; -; mRNA.
EMBL; AB019228; BAA96920.1; -; Genomic_DNA.
EMBL; CP002688; AED97029.1; -; Genomic_DNA.
EMBL; AY070466; AAL49932.1; -; mRNA.
EMBL; BT020373; AAV85728.1; -; mRNA.
RefSeq; NP_200637.1; NM_125214.6.
UniGene; At.45955; -.
ProteinModelPortal; Q9SEI4; -.
SMR; Q9SEI4; -.
BioGrid; 21185; 8.
IntAct; Q9SEI4; 7.
STRING; 3702.AT5G58290.1; -.
iPTMnet; Q9SEI4; -.
PaxDb; Q9SEI4; -.
PRIDE; Q9SEI4; -.
EnsemblPlants; AT5G58290.1; AT5G58290.1; AT5G58290.
GeneID; 835941; -.
Gramene; AT5G58290.1; AT5G58290.1; AT5G58290.
KEGG; ath:AT5G58290; -.
Araport; AT5G58290; -.
TAIR; locus:2161258; AT5G58290.
eggNOG; KOG0727; Eukaryota.
eggNOG; COG1222; LUCA.
HOGENOM; HOG000225143; -.
KO; K03063; -.
OMA; LIIRNDP; -.
OrthoDB; EOG09360AE8; -.
PhylomeDB; Q9SEI4; -.
BRENDA; 3.6.4.8; 399.
Reactome; R-ATH-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-ATH-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-ATH-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-ATH-382556; ABC-family proteins mediated transport.
Reactome; R-ATH-4641258; Degradation of DVL.
Reactome; R-ATH-5632684; Hedgehog 'on' state.
Reactome; R-ATH-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-ATH-5689603; UCH proteinases.
Reactome; R-ATH-5689880; Ub-specific processing proteases.
Reactome; R-ATH-68949; Orc1 removal from chromatin.
Reactome; R-ATH-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:Q9SEI4; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9SEI4; baseline and differential.
Genevisible; Q9SEI4; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; TAS:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0000502; C:proteasome complex; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central.
GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
InterPro; IPR005937; 26S_Psome_P45-like.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR035256; PSMC4.
PANTHER; PTHR23073:SF8; PTHR23073:SF8; 1.
Pfam; PF00004; AAA; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01242; 26Sp45; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Coiled coil; Complete proteome; Cytoplasm;
Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 408 26S proteasome regulatory subunit 6B
homolog.
/FTId=PRO_0000084692.
NP_BIND 196 203 ATP. {ECO:0000255}.
COILED 28 75 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:19245862}.
MUTAGEN 158 158 G->E: Impairs the light-specific
hypocotyl elongation response elicited by
a glutamate receptor agonist, BMAA.
{ECO:0000269|PubMed:19412571}.
SEQUENCE 408 AA; 45751 MW; A1045D85BF3BBEE4 CRC64;
MASAAVASMV LDPKASPALM DLSTADEEDL YGRLKSLERQ LEFTDIQEEY VKDEQKNLKR
ELLRAQEEVK RIQSVPLVIG QFMEMVDQNN GIVGSTTGSN YYVRILSTIN RELLKPSASV
ALHRHSNALV DVLPPEADSS ISLLSQSEKP DVSYNDIGGC DIQKQEIREA VELPLTHHEL
YKQIGIDPPR GVLLYGPPGT GKTMLAKAVA NHTTAAFIRV VGSEFVQKYL GEGPRMVRDV
FRLAKENAPA IIFIDEVDAI ATARFDAQTG ADREVQRILM ELLNQMDGFD QTVNVKVIMA
TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLVFQVCTS KMNLSDEVDL EDYVSRPDKI
SAAEIAAICQ EAGMHAVRKN RYVILPKDFE KGYRANVKKP DTDFEFYK


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