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O81149

- PSA5A_ARATH

UniProt

O81149 - PSA5A_ARATH

Protein

Proteasome subunit alpha type-5-A

Gene

PAE1

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 114 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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. ribonuclease activity Source: TAIR
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. response to cadmium ion Source: TAIR
    2. RNA phosphodiester bond hydrolysis Source: GOC
    3. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciARA:AT1G53850-MONOMER.
    ARA:GQT-2342-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-5-A (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome alpha subunit E-1
    Gene namesi
    Name:PAE1
    Ordered Locus Names:At1g53850
    ORF Names:T18A20.8
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G53850.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. cytosol Source: TAIR
    3. cytosolic ribosome Source: TAIR
    4. nucleus Source: TAIR
    5. plasma membrane Source: TAIR
    6. proteasome complex Source: TAIR
    7. proteasome core complex, alpha-subunit complex Source: InterPro
    8. vacuolar membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 237237Proteasome subunit alpha type-5-APRO_0000124124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Cross-linki66 – 66Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiO81149.
    PRIDEiO81149.

    Expressioni

    Gene expression databases

    GenevestigatoriO81149.

    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

    IntActiO81149. 2 interactions.
    STRINGi3702.AT1G53850.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliO81149.
    SMRiO81149. Positions 8-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091085.
    InParanoidiO81149.
    KOiK02729.
    OMAiHYDEGMD.
    PhylomeDBiO81149.

    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.

    O81149-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKEGVVLAV    50
    EKRITSPLLE PSSVEKIMEI DDHIGCAMSG LIADARTLVE HARVETQNHR 100
    FSYGEPMTVE STTQALCDLA LRFGEGEEES MSRPFGVSLL IAGHDENGPS 150
    LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ EQFNKDLSLQ EAETIAVSIL 200
    KQVMEEKVTP NNVDIAKVAP AYHLYTPQEV EAVIARL 237
    Length:237
    Mass (Da):25,947
    Last modified:November 1, 1998 - v1
    Checksum:iB17DED1D6E2C9680
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211L → F in BAD94476. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043524 mRNA. Translation: AAC32060.1.
    AC009324 Genomic DNA. Translation: AAF02858.1.
    CP002684 Genomic DNA. Translation: AEE33009.1.
    CP002684 Genomic DNA. Translation: AEE33010.1.
    AY072371 mRNA. Translation: AAL62363.1.
    AY114616 mRNA. Translation: AAM47935.1.
    AY086045 mRNA. Translation: AAM63255.1.
    AK220949 mRNA. Translation: BAD94476.1.
    PIRiT51972.
    RefSeqiNP_001077717.1. NM_001084248.1.
    NP_175788.1. NM_104262.2.
    UniGeneiAt.23242.

    Genome annotation databases

    EnsemblPlantsiAT1G53850.1; AT1G53850.1; AT1G53850.
    AT1G53850.2; AT1G53850.2; AT1G53850.
    GeneIDi841822.
    KEGGiath:AT1G53850.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043524 mRNA. Translation: AAC32060.1 .
    AC009324 Genomic DNA. Translation: AAF02858.1 .
    CP002684 Genomic DNA. Translation: AEE33009.1 .
    CP002684 Genomic DNA. Translation: AEE33010.1 .
    AY072371 mRNA. Translation: AAL62363.1 .
    AY114616 mRNA. Translation: AAM47935.1 .
    AY086045 mRNA. Translation: AAM63255.1 .
    AK220949 mRNA. Translation: BAD94476.1 .
    PIRi T51972.
    RefSeqi NP_001077717.1. NM_001084248.1.
    NP_175788.1. NM_104262.2.
    UniGenei At.23242.

    3D structure databases

    ProteinModelPortali O81149.
    SMRi O81149. Positions 8-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O81149. 2 interactions.
    STRINGi 3702.AT1G53850.1-P.

    Proteomic databases

    PaxDbi O81149.
    PRIDEi O81149.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G53850.1 ; AT1G53850.1 ; AT1G53850 .
    AT1G53850.2 ; AT1G53850.2 ; AT1G53850 .
    GeneIDi 841822.
    KEGGi ath:AT1G53850.

    Organism-specific databases

    TAIRi AT1G53850.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091085.
    InParanoidi O81149.
    KOi K02729.
    OMAi HYDEGMD.
    PhylomeDBi O81149.

    Enzyme and pathway databases

    BioCyci ARA:AT1G53850-MONOMER.
    ARA:GQT-2342-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.

    Gene expression databases

    Genevestigatori O81149.

    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. "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], GENE FAMILY, NOMENCLATURE.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(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. "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].
    6. "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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-237.
      Strain: cv. Columbia.
    7. "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.
    8. "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.
    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, ACETYLATION AT MET-1, UBIQUITINATION AT LYS-66.

    Entry informationi

    Entry nameiPSA5A_ARATH
    AccessioniPrimary (citable) accession number: O81149
    Secondary accession number(s): Q56ZL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 114 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. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3