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P12881

- PSA1_DROME

UniProt

P12881 - PSA1_DROME

Protein

Proteasome subunit alpha type-1

Gene

Prosalpha6

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 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      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. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
    2. ventral furrow formation 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.

    Protein family/group databases

    MEROPSiT01.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-1 (EC:3.4.25.1)
    Alternative name(s):
    PROS-Dm35
    Proteasome 35 kDa subunit
    Gene namesi
    Name:Prosalpha6
    Synonyms:PROS-35, Pros35
    ORF Names:CG4904
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0250843. Prosalpha6.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. microtubule associated complex Source: FlyBase
    3. nucleus Source: FlyBase
    4. proteasome 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 – 279279Proteasome subunit alpha type-1PRO_0000124068Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei103 – 1031PhosphotyrosineSequence Analysis

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP12881.
    PRIDEiP12881.

    Expressioni

    Gene expression databases

    BgeeiP12881.

    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.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi60450. 51 interactions.
    DIPiDIP-22159N.
    IntActiP12881. 11 interactions.
    MINTiMINT-1759709.

    Structurei

    3D structure databases

    ProteinModelPortaliP12881.
    SMRiP12881. Positions 4-231.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074855.
    InParanoidiQ8SZ22.
    KOiK02725.
    OMAiFMKQQCL.
    OrthoDBiEOG7WQ7T1.
    PhylomeDBiP12881.

    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.

    P12881-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFRNQYDSDV TVWSPQGRLH QVEYAMEAVK LGTATVGLKN KDYAVLVALC    50
    KPTSELSDTQ RKIIPIDDHL GISIAGLTAD ARVLSRYLRS ECLNYKHSYD 100
    TTYPVSRLIT NLGNKMQTTT QRYDRRPYGV GLLVAGYDER GPHIYQVTPS 150
    ATFFNCKANS IGSRSQSART YLEKNLNKFL DSSKDEIIRH GIRAILGTLP 200
    TDEQGKDAGQ YDITVAIVGK DQPFTILSNK DSAKHVAIAK ENDNDTPRND 250
    DDDDRPSPPE EPAAGPRDPE VLVATEQRP 279
    Length:279
    Mass (Da):31,059
    Last modified:October 1, 1989 - v1
    Checksum:i1478BDC2C61EF3F1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti189 – 1891R → H in AAL48800. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15497 mRNA. Translation: CAA33520.1.
    X62285 Genomic DNA. Translation: CAA44173.1.
    AE014134 Genomic DNA. Translation: AAF52875.1.
    AY071178 mRNA. Translation: AAL48800.1.
    PIRiS23450. SNFF5K.
    RefSeqiNP_523532.1. NM_078808.3.
    UniGeneiDm.2599.

    Genome annotation databases

    EnsemblMetazoaiFBtr0079948; FBpp0079538; FBgn0250843.
    GeneIDi34359.
    KEGGidme:Dmel_CG4904.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15497 mRNA. Translation: CAA33520.1 .
    X62285 Genomic DNA. Translation: CAA44173.1 .
    AE014134 Genomic DNA. Translation: AAF52875.1 .
    AY071178 mRNA. Translation: AAL48800.1 .
    PIRi S23450. SNFF5K.
    RefSeqi NP_523532.1. NM_078808.3.
    UniGenei Dm.2599.

    3D structure databases

    ProteinModelPortali P12881.
    SMRi P12881. Positions 4-231.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60450. 51 interactions.
    DIPi DIP-22159N.
    IntActi P12881. 11 interactions.
    MINTi MINT-1759709.

    Protein family/group databases

    MEROPSi T01.976.

    Proteomic databases

    PaxDbi P12881.
    PRIDEi P12881.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0079948 ; FBpp0079538 ; FBgn0250843 .
    GeneIDi 34359.
    KEGGi dme:Dmel_CG4904.

    Organism-specific databases

    CTDi 34359.
    FlyBasei FBgn0250843. Prosalpha6.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074855.
    InParanoidi Q8SZ22.
    KOi K02725.
    OMAi FMKQQCL.
    OrthoDBi EOG7WQ7T1.
    PhylomeDBi P12881.

    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 34359.
    NextBioi 788106.

    Gene expression databases

    Bgeei P12881.

    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 PROS-35 gene encodes the 35 kd protein subunit of Drosophila melanogaster proteasome."
      Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.
      EMBO J. 8:2373-2379(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-18 AND 194-206.
      Strain: Oregon-R.
    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. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    6. "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 nameiPSA1_DROME
    AccessioniPrimary (citable) accession number: P12881
    Secondary accession number(s): Q8SZ22, Q9VL23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 139 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, Direct protein sequencing, 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