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Protein

Cytosol aminopeptidase

Gene

LAP3

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

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

Note: 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

GO - Molecular functioni

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

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
Complete GO annotation...

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

        10         20         30 
TKGLVLGIYS KEKEDDAPQF TSAGENFDKW VSGKLR
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

PIRiPT0430.

3D structure databases

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

Protein-protein interaction databases

IntActiP28839. 1 interaction.
MINTiMINT-8415208.

Chemistry

ChEMBLiCHEMBL5624.

Protein family/group databases

MEROPSiM17.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

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: January 7, 2015
This is version 89 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.