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P17220

- PSA2_RAT

UniProt

P17220 - PSA2_RAT

Protein

Proteasome subunit alpha type-2

Gene

Psma2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.

    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. response to virus Source: Ensembl
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Protein family/group databases

    MEROPSiT01.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-2 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C3
    Multicatalytic endopeptidase complex subunit C3
    Proteasome component C3
    Gene namesi
    Name:Psma2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 17

    Organism-specific databases

    RGDi61842. Psma2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. 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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi121 – 1211Y → F: Abolishes nuclear localization and phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 234233Proteasome subunit alpha type-2PRO_0000124079Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei70 – 701N6-acetyllysineBy similarity
    Modified residuei76 – 761PhosphotyrosineBy similarity
    Modified residuei121 – 1211Phosphotyrosine1 Publication
    Modified residuei171 – 1711N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues; which may be important for nuclear import.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP17220.

    2D gel databases

    World-2DPAGE0004:P17220.

    PTM databases

    PhosphoSiteiP17220.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    GenevestigatoriP17220.

    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

    BioGridi248290. 5 interactions.
    IntActiP17220. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP17220.
    SMRiP17220. Positions 2-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00550000074870.
    HOVERGENiHBG003005.
    KOiK02726.
    OMAiWKATALG.
    OrthoDBiEOG71VSTG.
    PhylomeDBiP17220.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17220-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK    50
    KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV 100
    YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD 150
    PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE DLELEDAIHT AILTLKESFE 200
    GQMTEDNIEV GICNEAGFRR LTPTEVRDYL AAIA 234
    Length:234
    Mass (Da):25,927
    Last modified:January 23, 2007 - v3
    Checksum:i4ECB56A233583821
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02897 mRNA. Translation: AAA40838.1.
    PIRiA34535. SNRTC3.
    RefSeqiNP_058975.1. NM_017279.1.
    UniGeneiRn.1617.

    Genome annotation databases

    EnsembliENSRNOT00000073834; ENSRNOP00000066950; ENSRNOG00000049920.
    GeneIDi29669.
    KEGGirno:29669.
    UCSCiRGD:61842. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02897 mRNA. Translation: AAA40838.1 .
    PIRi A34535. SNRTC3.
    RefSeqi NP_058975.1. NM_017279.1.
    UniGenei Rn.1617.

    3D structure databases

    ProteinModelPortali P17220.
    SMRi P17220. Positions 2-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248290. 5 interactions.
    IntActi P17220. 1 interaction.

    Protein family/group databases

    MEROPSi T01.972.

    PTM databases

    PhosphoSitei P17220.

    2D gel databases

    World-2DPAGE 0004:P17220.

    Proteomic databases

    PRIDEi P17220.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000073834 ; ENSRNOP00000066950 ; ENSRNOG00000049920 .
    GeneIDi 29669.
    KEGGi rno:29669.
    UCSCi RGD:61842. rat.

    Organism-specific databases

    CTDi 5683.
    RGDi 61842. Psma2.

    Phylogenomic databases

    GeneTreei ENSGT00550000074870.
    HOVERGENi HBG003005.
    KOi K02726.
    OMAi WKATALG.
    OrthoDBi EOG71VSTG.
    PhylomeDBi P17220.

    Miscellaneous databases

    NextBioi 609987.
    PROi P17220.

    Gene expression databases

    Genevestigatori P17220.

    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. "Molecular cloning of cDNA for proteasomes from rat liver: primary structure of component C3 with a possible tyrosine phosphorylation site."
      Tanaka K., Fujiwara T., Kumatori A., Shin S., Yoshimura T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S.
      Biochemistry 29:3777-3785(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Wistar.
      Tissue: Liver.
    2. "The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated."
      Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., Shimonishi Y.
      FEBS Lett. 263:373-375(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
      Tissue: Liver.
    3. Lubec G., Afjehi-Sadat L.
      Submitted (NOV-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 5-39 AND 71-84, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Spinal cord.
    4. "Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes."
      Benedict C.M., Clawson G.A.
      Biochemistry 35:11612-11621(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-121, PHOSPHORYLATION AT TYR-121.

    Entry informationi

    Entry nameiPSA2_RAT
    AccessioniPrimary (citable) accession number: P17220
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 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