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Q9V5C6

- PSA3_DROME

UniProt

Q9V5C6 - PSA3_DROME

Protein

Proteasome subunit alpha type-3

Gene

Prosalpha7

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 May 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 By similarity.By similarity

    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

    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-3 (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome subunit alpha-7
    Gene namesi
    Name:Prosalpha7
    ORF Names:CG1519
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0023175. Prosalpha7.

    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 – 253253Proteasome subunit alpha type-3PRO_0000124097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei248 – 2481Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9V5C6.
    PRIDEiQ9V5C6.

    Expressioni

    Gene expression databases

    BgeeiQ9V5C6.

    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 ntc.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi61847. 46 interactions.
    DIPiDIP-22157N.
    IntActiQ9V5C6. 8 interactions.
    MINTiMINT-950398.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9V5C6.
    SMRiQ9V5C6. Positions 2-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074912.
    InParanoidiQ9V5C6.
    KOiK02727.
    OMAiVPDGRHF.
    OrthoDBiEOG73JKW6.
    PhylomeDBiQ9V5C6.

    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.

    Q9V5C6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTIGTGYDL SASQFSPDGR VFQIDYASKA VEKSGTVIGI RGKDAVVLAV    50
    EKIITSKLYE PDAGGRIFTI EKNIGMAVAG LVADGNFVAD IARQEAANYR 100
    QQFEQAIPLK HLCHRVAGYV HAYTLYSAVR PFGLSIILAS WDEVEGPQLY 150
    KIEPSGSSFG YFACASGKAK QLAKTEMEKL KMDMRTDELV ESAGEIIYKV 200
    HDELKDKDFR FEMGLVGRVT GGLHLINPSE LTEKARKAGD AANKDEDSDN 250
    ETH 253
    Length:253
    Mass (Da):27,675
    Last modified:May 1, 2000 - v1
    Checksum:i7B19D8DA350E2B7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171P → A in AAB82572. 1 PublicationCurated
    Sequence conflicti30 – 301Missing in AAB82572. 1 PublicationCurated
    Sequence conflicti62 – 621D → H in AAB82572. 1 PublicationCurated
    Sequence conflicti140 – 15718Missing in AAT27293. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti167 – 1671Missing in AAB82572. 1 PublicationCurated
    Sequence conflicti182 – 1821M → T in AAB82572. 1 PublicationCurated
    Sequence conflicti235 – 25319ARKAG…DNETH → DEDTACGQQDEGRRQRQ in AAB82572. 1 PublicationCuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF025793 Genomic DNA. Translation: AAB82572.1.
    AE013599 Genomic DNA. Translation: AAF58889.1.
    AY069616 mRNA. Translation: AAL39761.1.
    BT014669 mRNA. Translation: AAT27293.1.
    RefSeqiNP_724834.1. NM_165703.3.
    UniGeneiDm.2041.

    Genome annotation databases

    EnsemblMetazoaiFBtr0089998; FBpp0089041; FBgn0023175.
    GeneIDi36018.
    KEGGidme:Dmel_CG1519.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF025793 Genomic DNA. Translation: AAB82572.1 .
    AE013599 Genomic DNA. Translation: AAF58889.1 .
    AY069616 mRNA. Translation: AAL39761.1 .
    BT014669 mRNA. Translation: AAT27293.1 .
    RefSeqi NP_724834.1. NM_165703.3.
    UniGenei Dm.2041.

    3D structure databases

    ProteinModelPortali Q9V5C6.
    SMRi Q9V5C6. Positions 2-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61847. 46 interactions.
    DIPi DIP-22157N.
    IntActi Q9V5C6. 8 interactions.
    MINTi MINT-950398.

    Proteomic databases

    PaxDbi Q9V5C6.
    PRIDEi Q9V5C6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0089998 ; FBpp0089041 ; FBgn0023175 .
    GeneIDi 36018.
    KEGGi dme:Dmel_CG1519.

    Organism-specific databases

    CTDi 36018.
    FlyBasei FBgn0023175. Prosalpha7.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074912.
    InParanoidi Q9V5C6.
    KOi K02727.
    OMAi VPDGRHF.
    OrthoDBi EOG73JKW6.
    PhylomeDBi Q9V5C6.

    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 36018.
    NextBioi 796366.
    PROi Q9V5C6.

    Gene expression databases

    Bgeei Q9V5C6.

    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. "Cloning of the Drosophila melanogaster alpha7 proteasome subunit gene."
      Belote J.M., Smyth K.A., Katz E., Miller M.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      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.
    5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Testis.
    6. "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-248, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.
    7. "A conserved F box regulatory complex controls proteasome activity in Drosophila."
      Bader M., Benjamin S., Wapinski O.L., Smith D.M., Goldberg A.L., Steller H.
      Cell 145:371-382(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NTC.

    Entry informationi

    Entry nameiPSA3_DROME
    AccessioniPrimary (citable) accession number: Q9V5C6
    Secondary accession number(s): O17313, Q8MKU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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