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P90513

- PSA3_ACACA

UniProt

P90513 - PSA3_ACACA

Protein

Proteasome subunit alpha type-3

Gene
N/A
Organism
Acanthamoeba castellanii (Amoeba)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-3 (EC:3.4.25.1)
    OrganismiAcanthamoeba castellanii (Amoeba)
    Taxonomic identifieri5755 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaDiscoseaLongamoebiaCentramoebidaAcanthamoebidaeAcanthamoeba

    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, alpha-subunit complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 252›252Proteasome subunit alpha type-3PRO_0000124094Add
    BLAST

    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

    Structurei

    3D structure databases

    ProteinModelPortaliP90513.
    SMRiP90513. Positions 1-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    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: Fragment.

    P90513-1 [UniParc]FASTAAdd to Basket

    « Hide

    SIGTGYDLSS TTFSPDGRVF QVEYAAKAVD NSGTALGLRV KDGVVLAVEK    50
    LLVSKMLVPN TNRRIHTVDR HCGLAMSGLV ADGRQLVSRG RAEATSYREF 100
    YGTDISGKVL NERLSNFVQL YSLYGSVRPF GTSVILGCVD KNGPQLYMIE 150
    PSGISWGYFG VAIGKGARAA KTEIEKLKLS EMTAREAIKE AAKIIYSVHD 200
    DAKDKAFELE LSWVCEETGN LHKFVPKDLL EEAEKYAKQA LEEEEDMSEE 250
    ED 252
    Length:252
    Mass (Da):27,728
    Last modified:May 1, 1997 - v1
    Checksum:i71898276B50C2E79
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85398 mRNA. Translation: AAB41645.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85398 mRNA. Translation: AAB41645.1 .

    3D structure databases

    ProteinModelPortali P90513.
    SMRi P90513. Positions 1-243.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. Xu P., Zot H.G.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPSA3_ACACA
    AccessioniPrimary (citable) accession number: P90513
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3