Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P18053

- PSA4_DROME

UniProt

P18053 - PSA4_DROME

Protein

Proteasome subunit alpha type-4

Gene

Prosalpha3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (08 Dec 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell proliferation Source: FlyBase
    2. mitotic spindle elongation Source: FlyBase
    3. mitotic spindle organization Source: FlyBase
    4. 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.

    Protein family/group databases

    MEROPSiT01.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-4 (EC:3.4.25.1)
    Alternative name(s):
    PROS-Dm29
    Proteasome 29 kDa subunit
    Gene namesi
    Name:Prosalpha3
    Synonyms:PROS-29, Pros29
    ORF Names:CG9327
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0261394. Prosalpha3.

    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 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 – 264264Proteasome subunit alpha type-4PRO_0000124109Add
    BLAST

    Proteomic databases

    PaxDbiP18053.
    PRIDEiP18053.

    Expressioni

    Gene expression databases

    BgeeiP18053.

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PI31Q9V6372EBI-138951,EBI-144377
    Prosalpha2P403013EBI-138951,EBI-98978

    Protein-protein interaction databases

    BioGridi63019. 41 interactions.
    DIPiDIP-19125N.
    IntActiP18053. 6 interactions.
    MINTiMINT-996465.
    STRINGi7227.FBpp0071451.

    Structurei

    3D structure databases

    ProteinModelPortaliP18053.
    SMRiP18053. Positions 2-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074827.
    InParanoidiP18053.
    KOiK02728.
    OMAiRNDKQAY.
    OrthoDBiEOG7F512J.
    PhylomeDBiP18053.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR016050. Proteasome_bsu_CS.
    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.

    P18053-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARRYDSRTT IFSPEGRLYQ VEYAMEAISH AGTCLGILAE DGILLAAECR    50
    STNKLLDSAI PSEKIYRLND NMVCSVAGIT SDANVLTSEL RLIAQRYQFS 100
    YGEVIPCEQL VSHLCDIKQA YTQYGGKRPF GVSLLYMGWD NKYGYQLYQS 150
    DPSGNYGGWK ATCIGNNFGA AISMLKQELA DKENVKLTLA DAKDLAIKVL 200
    SMTLDTTKLT PEKVEMATLQ RVDNKTVYSV LEKPDVEKLI EKYTKVQAEA 250
    EAAKKEKQAK QPTK 264
    Length:264
    Mass (Da):29,412
    Last modified:December 8, 2000 - v2
    Checksum:iE5209BC634008B8B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681L → R in CAA36555. (PubMed:2374736)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52319 mRNA. Translation: CAA36555.1.
    AE013599 Genomic DNA. Translation: AAF46651.1.
    AY084140 mRNA. Translation: AAL89878.1.
    PIRiS10318.
    RefSeqiNP_476691.1. NM_057343.5.
    UniGeneiDm.712.

    Genome annotation databases

    EnsemblMetazoaiFBtr0071522; FBpp0071451; FBgn0261394.
    GeneIDi37378.
    KEGGidme:Dmel_CG9327.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52319 mRNA. Translation: CAA36555.1 .
    AE013599 Genomic DNA. Translation: AAF46651.1 .
    AY084140 mRNA. Translation: AAL89878.1 .
    PIRi S10318.
    RefSeqi NP_476691.1. NM_057343.5.
    UniGenei Dm.712.

    3D structure databases

    ProteinModelPortali P18053.
    SMRi P18053. Positions 2-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63019. 41 interactions.
    DIPi DIP-19125N.
    IntActi P18053. 6 interactions.
    MINTi MINT-996465.
    STRINGi 7227.FBpp0071451.

    Protein family/group databases

    MEROPSi T01.973.

    Proteomic databases

    PaxDbi P18053.
    PRIDEi P18053.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0071522 ; FBpp0071451 ; FBgn0261394 .
    GeneIDi 37378.
    KEGGi dme:Dmel_CG9327.

    Organism-specific databases

    CTDi 37378.
    FlyBasei FBgn0261394. Prosalpha3.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074827.
    InParanoidi P18053.
    KOi K02728.
    OMAi RNDKQAY.
    OrthoDBi EOG7F512J.
    PhylomeDBi P18053.

    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

    ChiTaRSi Pros29. drosophila.
    GenomeRNAii 37378.
    NextBioi 803347.
    PROi P18053.

    Gene expression databases

    Bgeei P18053.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR016050. Proteasome_bsu_CS.
    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-29 gene is a new member of the PROS-gene family."
      Haass C., Pesold-Hurt B., Kloetzel P.-M.
      Nucleic Acids Res. 18:4018-4018(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Oregon-R.
    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. "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 nameiPSA4_DROME
    AccessioniPrimary (citable) accession number: P18053
    Secondary accession number(s): Q9W2N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 140 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