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Protein

Proteasome subunit alpha type-3

Gene

PAG1

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

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciARA:AT2G27020-MONOMER.
ReactomeiREACT_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit G-1
DiDi 17A-2a
Proteasome component 8
Proteasome subunit alpha type-7
Gene namesi
Name:PAG1
Synonyms:PRC8
Ordered Locus Names:At2g27020
ORF Names:T20P8.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G27020.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • cytoplasm Source: GO_Central
  • cytosol Source: TAIR
  • nucleus Source: TAIR
  • proteasome complex Source: TAIR
  • proteasome core complex, alpha-subunit complex Source: InterPro
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

Lethal due to defect in male gametogenesis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 249248Proteasome subunit alpha type-3PRO_0000124098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei214 – 2141N-acetylserine1 Publication
Modified residuei220 – 2201N-acetylserine1 Publication
Cross-linki221 – 221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiO23715.
PRIDEiO23715.

Expressioni

Tissue specificityi

Ubiquitous low levels.2 Publications

Inductioni

Induced by the endoparasitic nematode M.incognita. Levels increase after infection in both giants cells and endodermal cells of galls. Later confined to giant cells at high levels.1 Publication

Interactioni

Subunit structurei

Component of the 20S core complex 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 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.3 Publications

Protein-protein interaction databases

BioGridi2596. 1 interaction.
IntActiO23715. 2 interactions.
STRINGi3702.AT2G27020.1.

Structurei

3D structure databases

ProteinModelPortaliO23715.
SMRiO23715. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091086.
InParanoidiO23715.
KOiK02727.
OMAiVPDGRHF.
PhylomeDBiO23715.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O23715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIGTGYDL SVTTFSPDGR VFQIEYAAKA VDNSGTVVGI KCKDGIVMGV
60 70 80 90 100
EKLIASKMML PGSNRRIHSV HRHAGMAVAG LAADGRQIVA RAKSEARSYE
110 120 130 140 150
SVYGDAVPVK ELSERVASYV HLCTLYWWLR PFGCGVILGG YDRDGPQLYM
160 170 180 190 200
IEPSGISYRY FGAAIGKGKQ AAKTEIEKLN LSEMTCKEGV IEVAKIIYKL
210 220 230 240
HDEAKDKAFE LEMSWICEES KREHQKVPDD LLEEAKTAAK TALEEMDAD
Length:249
Mass (Da):27,377
Last modified:December 8, 2000 - v2
Checksum:iFB5BAA07AC45A25D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201R → G in CAA74027 (PubMed:9373170).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13693 mRNA. Translation: CAA74027.1.
AF043528 mRNA. Translation: AAC32064.1.
AC005623 Genomic DNA. Translation: AAC77860.1.
CP002685 Genomic DNA. Translation: AEC07923.1.
AF375455 mRNA. Translation: AAK53039.1.
AY124806 mRNA. Translation: AAM70515.1.
AY088609 mRNA. Translation: AAM66932.1.
AK175942 mRNA. Translation: BAD43705.1.
AK175949 mRNA. Translation: BAD43712.1.
AJ286351 mRNA. Translation: CAB71015.1.
PIRiG84667.
RefSeqiNP_180270.1. NM_128260.4.
UniGeneiAt.22596.

Genome annotation databases

EnsemblPlantsiAT2G27020.1; AT2G27020.1; AT2G27020.
GeneIDi817244.
KEGGiath:AT2G27020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13693 mRNA. Translation: CAA74027.1.
AF043528 mRNA. Translation: AAC32064.1.
AC005623 Genomic DNA. Translation: AAC77860.1.
CP002685 Genomic DNA. Translation: AEC07923.1.
AF375455 mRNA. Translation: AAK53039.1.
AY124806 mRNA. Translation: AAM70515.1.
AY088609 mRNA. Translation: AAM66932.1.
AK175942 mRNA. Translation: BAD43705.1.
AK175949 mRNA. Translation: BAD43712.1.
AJ286351 mRNA. Translation: CAB71015.1.
PIRiG84667.
RefSeqiNP_180270.1. NM_128260.4.
UniGeneiAt.22596.

3D structure databases

ProteinModelPortaliO23715.
SMRiO23715. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2596. 1 interaction.
IntActiO23715. 2 interactions.
STRINGi3702.AT2G27020.1.

Proteomic databases

PaxDbiO23715.
PRIDEiO23715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G27020.1; AT2G27020.1; AT2G27020.
GeneIDi817244.
KEGGiath:AT2G27020.

Organism-specific databases

TAIRiAT2G27020.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091086.
InParanoidiO23715.
KOiK02727.
OMAiVPDGRHF.
PhylomeDBiO23715.

Enzyme and pathway databases

BioCyciARA:AT2G27020-MONOMER.
ReactomeiREACT_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

Miscellaneous databases

PROiO23715.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 20S proteasome gene family in Arabidopsis thaliana."
    Parmentier Y., Bouchez D., Fleck J., Genschik P.
    FEBS Lett. 416:281-285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana."
    Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.
    Genetics 149:677-692(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-249.
    Strain: cv. Columbia.
  8. "Arabidopsis thaliana genes expressed in the early compatible interaction with root-knot nematodes."
    Vercauteren I., van der Schueren E., Van Montagu M., Gheysen G.
    Mol. Plant Microbe Interact. 14:288-299(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 219-249, TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
    Tissue: Root.
  9. "Structure and functional analyses of the 26S proteasome subunits from plants."
    Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M., Finley D., Vierstra R.D.
    Mol. Biol. Rep. 26:137-146(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "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.
  11. "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, DISRUPTION PHENOTYPE, ACETYLATION AT SER-214 AND SER-220, UBIQUITINATION AT LYS-221.
  12. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSA3_ARATH
AccessioniPrimary (citable) accession number: O23715
Secondary accession number(s): O81151, Q680B8, Q9M3S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 8, 2000
Last modified: July 22, 2015
This is version 124 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.