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Protein

26S protease regulatory subunit 6B homolog

Gene

RPT3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 26S protease 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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2038ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.8. 399.
ReactomeiR-ATH-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-ATH-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-ATH-5632684. Hedgehog 'on' state.
R-ATH-68949. Orc1 removal from chromatin.
R-ATH-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-ATH-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 6B homolog
Alternative name(s):
26S protease subunit 6B homolog
26S proteasome AAA-ATPase subunit RPT3
Protein BMAA insensitive morphology 409
Regulatory particle triple-A ATPase subunit 3
Gene namesi
Name:RPT3
Synonyms:BIM409
Ordered Locus Names:At5g58290
ORF Names:MCK7.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G58290.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • nucleus Source: TAIR
  • plasmodesma Source: TAIR
  • proteasome complex Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581G → E: Impairs the light-specific hypocotyl elongation response elicited by a glutamate receptor agonist, BMAA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 40840726S protease regulatory subunit 6B homologPRO_0000084692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei16 – 161PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9SEI4.
PRIDEiQ9SEI4.

PTM databases

iPTMnetiQ9SEI4.

Expressioni

Tissue specificityi

Expressed in dark-grown etiolated seedlings, roots, leaves, stems and flowers.

Gene expression databases

GenevisibleiQ9SEI4. AT.

Interactioni

Subunit structurei

Component of the 19S regulatory particule (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.2 Publications

Protein-protein interaction databases

BioGridi21185. 7 interactions.
IntActiQ9SEI4. 7 interactions.
STRINGi3702.AT5G58290.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SEI4.
SMRiQ9SEI4. Positions 31-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili28 – 7548Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0727. Eukaryota.
COG1222. LUCA.
HOGENOMiHOG000225143.
KOiK03063.
OMAiICRTETH.
PhylomeDBiQ9SEI4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SEI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAAVASMV LDPKASPALM DLSTADEEDL YGRLKSLERQ LEFTDIQEEY
60 70 80 90 100
VKDEQKNLKR ELLRAQEEVK RIQSVPLVIG QFMEMVDQNN GIVGSTTGSN
110 120 130 140 150
YYVRILSTIN RELLKPSASV ALHRHSNALV DVLPPEADSS ISLLSQSEKP
160 170 180 190 200
DVSYNDIGGC DIQKQEIREA VELPLTHHEL YKQIGIDPPR GVLLYGPPGT
210 220 230 240 250
GKTMLAKAVA NHTTAAFIRV VGSEFVQKYL GEGPRMVRDV FRLAKENAPA
260 270 280 290 300
IIFIDEVDAI ATARFDAQTG ADREVQRILM ELLNQMDGFD QTVNVKVIMA
310 320 330 340 350
TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLVFQVCTS KMNLSDEVDL
360 370 380 390 400
EDYVSRPDKI SAAEIAAICQ EAGMHAVRKN RYVILPKDFE KGYRANVKKP

DTDFEFYK
Length:408
Mass (Da):45,751
Last modified:May 1, 2000 - v1
Checksum:iA1045D85BF3BBEE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF123392 mRNA. Translation: AAF22523.1.
AB019228 Genomic DNA. Translation: BAA96920.1.
CP002688 Genomic DNA. Translation: AED97029.1.
AY070466 mRNA. Translation: AAL49932.1.
BT020373 mRNA. Translation: AAV85728.1.
RefSeqiNP_200637.1. NM_125214.5.
UniGeneiAt.45955.

Genome annotation databases

EnsemblPlantsiAT5G58290.1; AT5G58290.1; AT5G58290.
GeneIDi835941.
GrameneiAT5G58290.1; AT5G58290.1; AT5G58290.
KEGGiath:AT5G58290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF123392 mRNA. Translation: AAF22523.1.
AB019228 Genomic DNA. Translation: BAA96920.1.
CP002688 Genomic DNA. Translation: AED97029.1.
AY070466 mRNA. Translation: AAL49932.1.
BT020373 mRNA. Translation: AAV85728.1.
RefSeqiNP_200637.1. NM_125214.5.
UniGeneiAt.45955.

3D structure databases

ProteinModelPortaliQ9SEI4.
SMRiQ9SEI4. Positions 31-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21185. 7 interactions.
IntActiQ9SEI4. 7 interactions.
STRINGi3702.AT5G58290.1.

PTM databases

iPTMnetiQ9SEI4.

Proteomic databases

PaxDbiQ9SEI4.
PRIDEiQ9SEI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G58290.1; AT5G58290.1; AT5G58290.
GeneIDi835941.
GrameneiAT5G58290.1; AT5G58290.1; AT5G58290.
KEGGiath:AT5G58290.

Organism-specific databases

TAIRiAT5G58290.

Phylogenomic databases

eggNOGiKOG0727. Eukaryota.
COG1222. LUCA.
HOGENOMiHOG000225143.
KOiK03063.
OMAiICRTETH.
PhylomeDBiQ9SEI4.

Enzyme and pathway databases

BRENDAi3.6.4.8. 399.
ReactomeiR-ATH-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-ATH-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-ATH-5632684. Hedgehog 'on' state.
R-ATH-68949. Orc1 removal from chromatin.
R-ATH-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-ATH-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ9SEI4.

Gene expression databases

GenevisibleiQ9SEI4. AT.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and functional analysis of the six regulatory particle triple-A ATPase subunits from the Arabidopsis 26S proteasome."
    Fu H., Doelling J.H., Rubin D.M., Vierstra R.D.
    Plant J. 18:529-539(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  2. "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."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms."
    Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.
    J. Biol. Chem. 279:6401-6413(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  8. "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."
    Brenner E.D., Feinberg P., Runko S., Coruzzi G.M.
    Plant Mol. Biol. 70:523-533(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-158, FUNCTION.
  9. "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes."
    Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.
    J. Biol. Chem. 285:25554-25569(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT.
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRS6B_ARATH
AccessioniPrimary (citable) accession number: Q9SEI4
Secondary accession number(s): Q5PNS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.