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O23715 (PSA3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PAG1
Synonyms:PRC8
Ordered Locus Names:At2g27020
ORF Names:T20P8.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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. Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Ubiquitous low levels. Ref.2 Ref.8

Induction

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. Ref.8

Disruption phenotype

Lethal due to defect in male gametogenesis. Ref.11

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 249248Proteasome subunit alpha type-3
PRO_0000124098

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue2141N-acetylserine Ref.11
Modified residue2201N-acetylserine Ref.11
Cross-link221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Experimental info

Sequence conflict201R → G in CAA74027. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O23715 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: FB5BAA07AC45A25D

FASTA24927,377
        10         20         30         40         50         60 
MSSIGTGYDL SVTTFSPDGR VFQIEYAAKA VDNSGTVVGI KCKDGIVMGV EKLIASKMML 

        70         80         90        100        110        120 
PGSNRRIHSV HRHAGMAVAG LAADGRQIVA RAKSEARSYE SVYGDAVPVK ELSERVASYV 

       130        140        150        160        170        180 
HLCTLYWWLR PFGCGVILGG YDRDGPQLYM IEPSGISYRY FGAAIGKGKQ AAKTEIEKLN 

       190        200        210        220        230        240 
LSEMTCKEGV IEVAKIIYKL HDEAKDKAFE LEMSWICEES KREHQKVPDD LLEEAKTAAK 


TALEEMDAD 

« Hide

References

« Hide 'large scale' references
[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]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRG84667.
RefSeqNP_180270.1. NM_128260.4.
UniGeneAt.22596.

3D structure databases

ProteinModelPortalO23715.
SMRO23715. Positions 2-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid2596. 1 interaction.
IntActO23715. 2 interactions.

Proteomic databases

PaxDbO23715.
PRIDEO23715.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G27020.1; AT2G27020.1; AT2G27020.
GeneID817244.
KEGGath:AT2G27020.

Organism-specific databases

TAIRAT2G27020.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091086.
InParanoidO23715.
KOK02727.
OMAVPDGRHF.
PhylomeDBO23715.

Enzyme and pathway databases

BioCycARA:AT2G27020-MONOMER.

Gene expression databases

GenevestigatorO23715.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROO23715.

Entry information

Entry namePSA3_ARATH
AccessionPrimary (citable) accession number: O23715
Secondary accession number(s): O81151, Q680B8, Q9M3S3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 8, 2000
Last modified: June 11, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names