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Q95083

- PSA5_DROME

UniProt

Q95083 - PSA5_DROME

Protein

Proteasome subunit alpha type-5

Gene

Prosalpha5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 125 (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 process Source: FlyBase
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    ReactomeiREACT_180649. Activation of NF-kappaB in B cells.
    REACT_180655. ER-Phagosome pathway.
    REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_181662. Separation of Sister Chromatids.
    REACT_184330. Asymmetric localization of PCP proteins.
    REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_215026. degradation of AXIN.
    REACT_218589. Orc1 removal from chromatin.
    REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-5 (EC:3.4.25.1)
    Gene namesi
    Name:Prosalpha5
    Synonyms:ProsMA5
    ORF Names:CG10938
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0016697. Prosalpha5.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex Source: FlyBase
    4. 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 – 244244Proteasome subunit alpha type-5PRO_0000124121Add
    BLAST

    Proteomic databases

    PaxDbiQ95083.
    PRIDEiQ95083.

    Expressioni

    Gene expression databases

    BgeeiQ95083.

    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.By similarity

    Protein-protein interaction databases

    BioGridi62645. 37 interactions.
    DIPiDIP-19014N.
    IntActiQ95083. 2 interactions.
    MINTiMINT-966233.
    STRINGi7227.FBpp0086066.

    Structurei

    3D structure databases

    ProteinModelPortaliQ95083.
    SMRiQ95083. Positions 8-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074958.
    InParanoidiQ95083.
    KOiK02729.
    OMAiCAMSGLT.
    OrthoDBiEOG769ZKB.
    PhylomeDBiQ95083.

    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.

    Q95083-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI CTPEGVVLAV    50
    EKRITSPLMV PSTVEKIVEV DKHIGCATSG LMADARTLIE RARVECQNHW 100
    FVYNERMSIE SCAQAVSTLA IQFGDSGDSD GAAAMSRPFG VAILFAGIEA 150
    GQPQLWHMDP SGTFVRHGAK AIGSGSEGAQ QNLQDLFRPD LTLDEAIDIS 200
    LNTLKQVMEE KLNSTNVEVM TMTKEREFYM FTKEEVEQHI KNIA 244
    Length:244
    Mass (Da):26,884
    Last modified:December 8, 2000 - v2
    Checksum:iC58F3232A17FB711
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1661R → G in AAB93421. (PubMed:9409776)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U64721 Genomic DNA. Translation: AAB93421.1.
    AE013599 Genomic DNA. Translation: AAF57875.1.
    AY061404 mRNA. Translation: AAL28952.1.
    RefSeqiNP_477202.2. NM_057854.4.
    NP_725669.1. NM_166221.3.
    UniGeneiDm.3609.

    Genome annotation databases

    EnsemblMetazoaiFBtr0086910; FBpp0086066; FBgn0016697.
    FBtr0086911; FBpp0086067; FBgn0016697.
    GeneIDi36951.
    KEGGidme:Dmel_CG10938.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U64721 Genomic DNA. Translation: AAB93421.1 .
    AE013599 Genomic DNA. Translation: AAF57875.1 .
    AY061404 mRNA. Translation: AAL28952.1 .
    RefSeqi NP_477202.2. NM_057854.4.
    NP_725669.1. NM_166221.3.
    UniGenei Dm.3609.

    3D structure databases

    ProteinModelPortali Q95083.
    SMRi Q95083. Positions 8-243.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62645. 37 interactions.
    DIPi DIP-19014N.
    IntActi Q95083. 2 interactions.
    MINTi MINT-966233.
    STRINGi 7227.FBpp0086066.

    Proteomic databases

    PaxDbi Q95083.
    PRIDEi Q95083.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0086910 ; FBpp0086066 ; FBgn0016697 .
    FBtr0086911 ; FBpp0086067 ; FBgn0016697 .
    GeneIDi 36951.
    KEGGi dme:Dmel_CG10938.

    Organism-specific databases

    CTDi 36951.
    FlyBasei FBgn0016697. Prosalpha5.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074958.
    InParanoidi Q95083.
    KOi K02729.
    OMAi CAMSGLT.
    OrthoDBi EOG769ZKB.
    PhylomeDBi Q95083.

    Enzyme and pathway databases

    Reactomei REACT_180649. Activation of NF-kappaB in B cells.
    REACT_180655. ER-Phagosome pathway.
    REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_181662. Separation of Sister Chromatids.
    REACT_184330. Asymmetric localization of PCP proteins.
    REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_215026. degradation of AXIN.
    REACT_218589. Orc1 removal from chromatin.
    REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

    Miscellaneous databases

    GenomeRNAii 36951.
    NextBioi 801184.
    PROi Q95083.

    Gene expression databases

    Bgeei Q95083.

    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 cloning of the Drosophila melanogaster gene alpha5_dm encoding a 20S proteasome alpha-type subunit."
      Zaiss D., Belote J.M.
      Gene 201:99-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiPSA5_DROME
    AccessioniPrimary (citable) accession number: Q95083
    Secondary accession number(s): Q0E942, Q9V809
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 125 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