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P28839

- AMPL_PIG

UniProt

P28839 - AMPL_PIG

Protein

Cytosol aminopeptidase

Gene

LAP3

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
    Release of N-terminal proline from a peptide.

    Cofactori

    Binds 2 zinc ions per subunit. One zinc ion is tightly bound and essential for enzyme activity, while the second metal coordination site can be occupied by zinc, magnesium or manganese to give enzymes of different activities By similarity.By similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM17.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosol aminopeptidase (EC:3.4.11.1)
    Alternative name(s):
    Leucine aminopeptidase 3
    Short name:
    LAP-3
    Leucyl aminopeptidase
    Proline aminopeptidase (EC:3.4.11.5)
    Prolyl aminopeptidase
    Gene namesi
    Name:LAP3
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›36›36Cytosol aminopeptidasePRO_0000165827Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylthreonineBy similarity
    Modified residuei13 – 131N6-succinyllysineBy similarity
    Modified residuei29 – 291N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    IntActiP28839. 1 interaction.
    MINTiMINT-8415208.

    Structurei

    3D structure databases

    ProteinModelPortaliP28839.
    SMRiP28839. Positions 1-36.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M17 family.Curated

    Sequencei

    Sequence statusi: Fragment.

    P28839-1 [UniParc]FASTAAdd to Basket

    « Hide

    TKGLVLGIYS KEKEDDAPQF TSAGENFDKW VSGKLR                  36
    Length:36
    Mass (Da):4,015
    Last modified:December 1, 1992 - v1
    Checksum:i2C0CECD973FAB49C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei36 – 361

    Sequence databases

    PIRiPT0430.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    PIRi PT0430.

    3D structure databases

    ProteinModelPortali P28839.
    SMRi P28839. Positions 1-36.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P28839. 1 interaction.
    MINTi MINT-8415208.

    Chemistry

    ChEMBLi CHEMBL5624.

    Protein family/group databases

    MEROPSi M17.003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase."
      Matsushima M., Takahashi T., Ichinose M., Miki K., Kurokawa K., Takahashi K.
      Biochem. Biophys. Res. Commun. 178:1459-1464(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Intestine and Kidney.

    Entry informationi

    Entry nameiAMPL_PIG
    AccessioniPrimary (citable) accession number: P28839
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 86 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