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O23715

- PSA3_ARATH

UniProt

O23715 - PSA3_ARATH

Protein

Proteasome subunit alpha type-3

Gene

PAG1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (08 Dec 2000)
      Previous versions | rss
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    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

    1. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. response to cadmium ion Source: TAIR
    2. response to cold Source: TAIR
    3. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciARA:AT2G27020-MONOMER.
    ReactomeiREACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_107429. Orc1 removal from chromatin.
    REACT_185297. Separation of Sister Chromatids.
    REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_187719. ER-Phagosome pathway.
    REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_190947. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

    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: Chromosome 2

    Organism-specific databases

    TAIRiAT2G27020.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. cytosol Source: TAIR
    3. nucleus Source: TAIR
    4. proteasome complex Source: TAIR
    5. proteasome core complex, alpha-subunit complex Source: InterPro
    6. vacuolar membrane Source: TAIR
    7. vacuole Source: TAIR

    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

    Gene expression databases

    GenevestigatoriO23715.

    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.

    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

    MSSIGTGYDL SVTTFSPDGR VFQIEYAAKA VDNSGTVVGI KCKDGIVMGV    50
    EKLIASKMML PGSNRRIHSV HRHAGMAVAG LAADGRQIVA RAKSEARSYE 100
    SVYGDAVPVK ELSERVASYV HLCTLYWWLR PFGCGVILGG YDRDGPQLYM 150
    IEPSGISYRY FGAAIGKGKQ AAKTEIEKLN LSEMTCKEGV IEVAKIIYKL 200
    HDEAKDKAFE LEMSWICEES KREHQKVPDD LLEEAKTAAK TALEEMDAD 249
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi G84667.
    RefSeqi NP_180270.1. NM_128260.4.
    UniGenei At.22596.

    3D structure databases

    ProteinModelPortali O23715.
    SMRi O23715. Positions 2-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 2596. 1 interaction.
    IntActi O23715. 2 interactions.

    Proteomic databases

    PaxDbi O23715.
    PRIDEi O23715.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G27020.1 ; AT2G27020.1 ; AT2G27020 .
    GeneIDi 817244.
    KEGGi ath:AT2G27020.

    Organism-specific databases

    TAIRi AT2G27020.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091086.
    InParanoidi O23715.
    KOi K02727.
    OMAi VPDGRHF.
    PhylomeDBi O23715.

    Enzyme and pathway databases

    BioCyci ARA:AT2G27020-MONOMER.
    Reactomei REACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_107429. Orc1 removal from chromatin.
    REACT_185297. Separation of Sister Chromatids.
    REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_187719. ER-Phagosome pathway.
    REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_190947. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

    Miscellaneous databases

    PROi O23715.

    Gene expression databases

    Genevestigatori O23715.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SMARTi SM00948. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 118 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