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P28839 (AMPL_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LAP3
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length36 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Cofactor

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.

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Protease
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›36›36Cytosol aminopeptidase
PRO_0000165827

Amino acid modifications

Modified residue11N-acetylthreonine By similarity
Modified residue131N6-succinyllysine By similarity
Modified residue291N6-succinyllysine By similarity

Experimental info

Non-terminal residue361

Sequences

Sequence LengthMass (Da)Tools
P28839 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 2C0CECD973FAB49C

FASTA364,015
        10         20         30 
TKGLVLGIYS KEKEDDAPQF TSAGENFDKW VSGKLR 

« Hide

References

[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.

Cross-references

Sequence databases

PIRPT0430.

3D structure databases

ProteinModelPortalP28839.
SMRP28839. Positions 1-36.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28839. 1 interaction.
MINTMINT-8415208.

Chemistry

ChEMBLCHEMBL5624.

Protein family/group databases

MEROPSM17.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameAMPL_PIG
AccessionPrimary (citable) accession number: P28839
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 14, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries