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P21670

- PSA4_RAT

UniProt

P21670 - PSA4_RAT

Protein

Proteasome subunit alpha type-4

Gene

Psma4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      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

    Enzyme and pathway databases

    ReactomeiREACT_194781. Separation of Sister Chromatids.
    REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_198391. Asymmetric localization of PCP proteins.
    REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_199197. ER-Phagosome pathway.
    REACT_199247. Activation of NF-kappaB in B cells.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_206488. degradation of DVL.
    REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
    REACT_211117. Orc1 removal from chromatin.
    REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_220232. Regulation of ornithine decarboxylase (ODC).
    REACT_227706. degradation of AXIN.

    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):
    Macropain subunit C9
    Multicatalytic endopeptidase complex subunit C9
    Proteasome component C9
    Proteasome subunit L
    Gene namesi
    Name:Psma4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi61846. Psma4.

    Subcellular locationi

    Cytoplasm. Nucleus. CytoplasmP-body By similarity
    Note: Colocalizes with TRIM5 in the cytoplasmic bodies.By similarity

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex Source: UniProtKB
    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 – 261261Proteasome subunit alpha type-4PRO_0000124106Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131PhosphoserineBy similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei127 – 1271N6-acetyllysineBy similarity
    Modified residuei176 – 1761N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP21670.
    PRIDEiP21670.

    2D gel databases

    World-2DPAGE0004:P21670.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    GenevestigatoriP21670.

    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.

    Protein-protein interaction databases

    IntActiP21670. 2 interactions.
    STRINGi10116.ENSRNOP00000018173.

    Structurei

    3D structure databases

    ProteinModelPortaliP21670.
    SMRiP21670. Positions 2-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074827.
    HOGENOMiHOG000091085.
    HOVERGENiHBG003005.
    InParanoidiP21670.
    KOiK02728.
    OMAiKQEYKDD.
    OrthoDBiEOG7F512J.
    PhylomeDBiP21670.
    TreeFamiTF106209.

    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.

    P21670-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR    50
    NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ 100
    YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS 150
    DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAVKVLNKT 200
    MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH EEEEAKAERE 250
    KKEKEQREKD K 261
    Length:261
    Mass (Da):29,498
    Last modified:May 1, 1991 - v1
    Checksum:iBB6742398E91E13B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53304 mRNA. Translation: CAA37390.1.
    X55986 mRNA. Translation: CAA39458.1.
    PIRiS10566. SNRTC9.
    RefSeqiNP_058977.1. NM_017281.1.
    XP_006243128.1. XM_006243066.1.
    UniGeneiRn.11076.

    Genome annotation databases

    EnsembliENSRNOT00000018173; ENSRNOP00000018173; ENSRNOG00000013493.
    GeneIDi29671.
    KEGGirno:29671.
    UCSCiRGD:61846. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53304 mRNA. Translation: CAA37390.1 .
    X55986 mRNA. Translation: CAA39458.1 .
    PIRi S10566. SNRTC9.
    RefSeqi NP_058977.1. NM_017281.1.
    XP_006243128.1. XM_006243066.1.
    UniGenei Rn.11076.

    3D structure databases

    ProteinModelPortali P21670.
    SMRi P21670. Positions 2-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21670. 2 interactions.
    STRINGi 10116.ENSRNOP00000018173.

    Protein family/group databases

    MEROPSi T01.973.

    2D gel databases

    World-2DPAGE 0004:P21670.

    Proteomic databases

    PaxDbi P21670.
    PRIDEi P21670.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000018173 ; ENSRNOP00000018173 ; ENSRNOG00000013493 .
    GeneIDi 29671.
    KEGGi rno:29671.
    UCSCi RGD:61846. rat.

    Organism-specific databases

    CTDi 5685.
    RGDi 61846. Psma4.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074827.
    HOGENOMi HOG000091085.
    HOVERGENi HBG003005.
    InParanoidi P21670.
    KOi K02728.
    OMAi KQEYKDD.
    OrthoDBi EOG7F512J.
    PhylomeDBi P21670.
    TreeFami TF106209.

    Enzyme and pathway databases

    Reactomei REACT_194781. Separation of Sister Chromatids.
    REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_198391. Asymmetric localization of PCP proteins.
    REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_199197. ER-Phagosome pathway.
    REACT_199247. Activation of NF-kappaB in B cells.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_206488. degradation of DVL.
    REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
    REACT_211117. Orc1 removal from chromatin.
    REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_220232. Regulation of ornithine decarboxylase (ODC).
    REACT_227706. degradation of AXIN.

    Miscellaneous databases

    NextBioi 609995.
    PROi P21670.

    Gene expression databases

    Genevestigatori P21670.

    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. "cDNA cloning and sequencing of component C9 of proteasomes from rat hepatoma cells."
      Kumatori A., Tanaka K., Tamura T., Fujiwara T., Ichihara A., Tokunaga F., Onikura A., Iwanaga S.
      FEBS Lett. 264:279-282(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. "Molecular cloning of cDNAs for two subunits of rat multicatalytic proteinase. Existence of N-terminal conserved and C-terminal diverged sequences among subunits."
      Sorimachi H., Tsukahara T., Kawasaki H., Ishiura S., Emori Y., Sugita H., Suzuki K.
      Eur. J. Biochem. 193:775-781(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.

    Entry informationi

    Entry nameiPSA4_RAT
    AccessioniPrimary (citable) accession number: P21670
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    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