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P18420

- PSA1_RAT

UniProt

P18420 - PSA1_RAT

Protein

Proteasome subunit alpha type-1

Gene

Psma1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (01 Feb 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. Mediates the lipopolysaccharide-induced signal macrophage proteasome. Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells By similarity.By similarity

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

    GO - Molecular functioni

    1. lipopolysaccharide binding Source: Ensembl
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. immune system process Source: UniProtKB-KW
    2. negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
    3. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Immunity

    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

    MEROPSiT01.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-1 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C2
    Multicatalytic endopeptidase complex subunit C2
    Proteasome component C2
    Proteasome nu chain
    Gene namesi
    Name:Psma1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi61841. Psma1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    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 – 263263Proteasome subunit alpha type-1PRO_0000124064Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei14 – 141PhosphoserineBy similarity
    Glycosylationi110 – 1101O-linked (GlcNAc)By similarity
    Cross-linki115 – 115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Proteolytically cleaved from a C-terminal extension in the course of the conversion of the proteasome from its latent form into its active form.

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP18420.
    PRIDEiP18420.

    2D gel databases

    World-2DPAGE0004:P18420.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    GenevestigatoriP18420.

    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. Interacts with NOTCH3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi248289. 1 interaction.
    IntActiP18420. 1 interaction.
    STRINGi10116.ENSRNOP00000015946.

    Structurei

    3D structure databases

    ProteinModelPortaliP18420.
    SMRiP18420. Positions 4-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074855.
    HOGENOMiHOG000091080.
    HOVERGENiHBG105373.
    InParanoidiP18420.
    KOiK02725.
    OMAiFMKQQCL.
    OrthoDBiEOG7WQ7T1.
    PhylomeDBiP18420.
    TreeFamiTF106206.

    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.

    P18420-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK    50
    RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD 100
    RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHVFQTCPS 150
    ANYFDCRAMS IGARSQSART YLERHMSEFM QCNLDELVKH GLRALRETLP 200
    AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP QRKAQPSQAA 250
    DEPAEKADEP MEH 263
    Length:263
    Mass (Da):29,518
    Last modified:February 1, 1991 - v2
    Checksum:i68660696B43A4051
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29859 mRNA. Translation: AAA41943.1.
    D90265 mRNA. Translation: BAA14312.1.
    BC062233 mRNA. Translation: AAH62233.1.
    PIRiA32968. SNRTC2.
    RefSeqiNP_058974.1. NM_017278.1.
    UniGeneiRn.2668.

    Genome annotation databases

    EnsembliENSRNOT00000015946; ENSRNOP00000015946; ENSRNOG00000011745.
    GeneIDi29668.
    KEGGirno:29668.
    UCSCiRGD:61841. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29859 mRNA. Translation: AAA41943.1 .
    D90265 mRNA. Translation: BAA14312.1 .
    BC062233 mRNA. Translation: AAH62233.1 .
    PIRi A32968. SNRTC2.
    RefSeqi NP_058974.1. NM_017278.1.
    UniGenei Rn.2668.

    3D structure databases

    ProteinModelPortali P18420.
    SMRi P18420. Positions 4-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248289. 1 interaction.
    IntActi P18420. 1 interaction.
    STRINGi 10116.ENSRNOP00000015946.

    Protein family/group databases

    MEROPSi T01.976.

    2D gel databases

    World-2DPAGE 0004:P18420.

    Proteomic databases

    PaxDbi P18420.
    PRIDEi P18420.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000015946 ; ENSRNOP00000015946 ; ENSRNOG00000011745 .
    GeneIDi 29668.
    KEGGi rno:29668.
    UCSCi RGD:61841. rat.

    Organism-specific databases

    CTDi 5682.
    RGDi 61841. Psma1.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074855.
    HOGENOMi HOG000091080.
    HOVERGENi HBG105373.
    InParanoidi P18420.
    KOi K02725.
    OMAi FMKQQCL.
    OrthoDBi EOG7WQ7T1.
    PhylomeDBi P18420.
    TreeFami TF106206.

    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 609983.
    PROi P18420.

    Gene expression databases

    Genevestigatori P18420.

    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 (multicatalytic proteinase complexes) from rat liver: primary structure of the largest component (C2)."
      Fujiwara T., Tanaka K., Kumatori A., Shin S., Yoshimura T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S.
      Biochemistry 28:7332-7340(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pituitary.
    3. "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 1-30, ACETYLATION AT MET-1.
      Tissue: Liver.
    4. Lubec G., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 63-82 AND 97-107, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiPSA1_RAT
    AccessioniPrimary (citable) accession number: P18420
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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