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P22769

- PSA71_DROME

UniProt

P22769 - PSA71_DROME

Protein

Proteasome subunit alpha type-7-1

Gene

Prosalpha4

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (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. cellular response to DNA damage stimulus Source: FlyBase
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-7-1 (EC:3.4.25.1)
    Alternative name(s):
    PROS-Dm28.1
    Proteasome 28 kDa subunit 1
    Gene namesi
    Name:Prosalpha4
    Synonyms:PROS-28.1, Pros28.1
    ORF Names:CG3422
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0004066. Prosalpha4.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule associated complex Source: FlyBase
    3. nucleus Source: UniProtKB-SubCell
    4. proteasome core complex Source: FlyBase
    5. proteasome core complex, alpha-subunit complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 249249Proteasome subunit alpha type-7-1PRO_0000124153Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei177 – 1771Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP22769.
    PRIDEiP22769.

    Expressioni

    Gene expression databases

    BgeeiP22769.

    Interactioni

    Subunit structurei

    The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. 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 By similarity. Interacts with PI31; this interaction is reduced by PI31 ADP-ribosylation.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi58925. 52 interactions.
    DIPiDIP-17376N.
    IntActiP22769. 5 interactions.
    MINTiMINT-994729.
    STRINGi7227.FBpp0073989.

    Structurei

    3D structure databases

    ProteinModelPortaliP22769.
    SMRiP22769. Positions 5-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074753.
    HOGENOMiHOG000072912.
    InParanoidiP22769.
    KOiK02731.
    OMAiPLKMLDR.
    OrthoDBiEOG71VSTG.
    PhylomeDBiP22769.

    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.

    P22769-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSRYDRAVT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKK    50
    SVAQLQEDRK VRKICMLDNH VVMAFAGLTA DARIMINRAQ VECQSHRLNV 100
    EDPVTLEYIT RFIAQLKQKY TQSNGRRPFG ISCLIGGFDA DGSAHLFQTE 150
    PSGIFYEYKA NATGRSAKVV REFFEKSYRE EEVANEHGAV KLAIRALLEV 200
    AQSGQNNLEV AIMENGKPLK MLDTDVITDY VKIIEKEKEE ELEKKKQKK 249
    Length:249
    Mass (Da):27,973
    Last modified:December 8, 2000 - v2
    Checksum:i56987932DADD02B3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti224 – 2241T → N in AAA62768. (PubMed:2169443)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57712 mRNA. Translation: AAA62768.1.
    X62286 Genomic DNA. Translation: CAA44174.1.
    AY542383 Genomic DNA. Translation: AAS86210.1.
    AY542384 Genomic DNA. Translation: AAS86211.1.
    AY542385 Genomic DNA. Translation: AAS86212.1.
    AY542386 Genomic DNA. Translation: AAS86213.1.
    AY542387 Genomic DNA. Translation: AAS86214.1.
    AY542388 Genomic DNA. Translation: AAS86215.1.
    AY542389 Genomic DNA. Translation: AAS86216.1.
    AE014298 Genomic DNA. Translation: AAF48573.1.
    AY071241 mRNA. Translation: AAL48863.1.
    PIRiJQ0681.
    S23451.
    RefSeqiNP_525092.1. NM_080353.4.
    UniGeneiDm.1671.

    Genome annotation databases

    EnsemblMetazoaiFBtr0074210; FBpp0073989; FBgn0004066.
    GeneIDi32584.
    KEGGidme:Dmel_CG3422.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57712 mRNA. Translation: AAA62768.1 .
    X62286 Genomic DNA. Translation: CAA44174.1 .
    AY542383 Genomic DNA. Translation: AAS86210.1 .
    AY542384 Genomic DNA. Translation: AAS86211.1 .
    AY542385 Genomic DNA. Translation: AAS86212.1 .
    AY542386 Genomic DNA. Translation: AAS86213.1 .
    AY542387 Genomic DNA. Translation: AAS86214.1 .
    AY542388 Genomic DNA. Translation: AAS86215.1 .
    AY542389 Genomic DNA. Translation: AAS86216.1 .
    AE014298 Genomic DNA. Translation: AAF48573.1 .
    AY071241 mRNA. Translation: AAL48863.1 .
    PIRi JQ0681.
    S23451.
    RefSeqi NP_525092.1. NM_080353.4.
    UniGenei Dm.1671.

    3D structure databases

    ProteinModelPortali P22769.
    SMRi P22769. Positions 5-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58925. 52 interactions.
    DIPi DIP-17376N.
    IntActi P22769. 5 interactions.
    MINTi MINT-994729.
    STRINGi 7227.FBpp0073989.

    Proteomic databases

    PaxDbi P22769.
    PRIDEi P22769.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0074210 ; FBpp0073989 ; FBgn0004066 .
    GeneIDi 32584.
    KEGGi dme:Dmel_CG3422.

    Organism-specific databases

    CTDi 32584.
    FlyBasei FBgn0004066. Prosalpha4.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074753.
    HOGENOMi HOG000072912.
    InParanoidi P22769.
    KOi K02731.
    OMAi PLKMLDR.
    OrthoDBi EOG71VSTG.
    PhylomeDBi P22769.

    Miscellaneous databases

    GenomeRNAii 32584.
    NextBioi 779280.

    Gene expression databases

    Bgeei P22769.

    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 Drosophila PROS-28.1 gene is a member of the proteasome gene family."
      Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.
      Gene 90:235-241(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular characterization of the genomic regions of the Drosophila alpha-type subunit proteasome genes PROS-Dm28.1 and PROS-Dm35."
      Frentzel S., Troxell M., Haass C., Pesold-Hurt B., Glaetzer K.H., Kloetzel P.-M.
      Eur. J. Biochem. 205:1043-1051(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Oregon-R.
    3. "Rapid evolution through gene duplication and subfunctionalization of the testes-specific alpha4 proteasome subunits in Drosophila."
      Torgerson D.G., Singh R.S.
      Genetics 168:1421-1432(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: b pr tk, CPA-129, CPA-46, Z(H)-12, Z(H)-16 and Z(H)-34.
    4. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.
    8. "Proteasome regulation by ADP-ribosylation."
      Cho-Park P.F., Steller H.
      Cell 153:614-627(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PI31.

    Entry informationi

    Entry nameiPSA71_DROME
    AccessioniPrimary (citable) accession number: P22769
    Secondary accession number(s): Q9VXI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3