P28839 (AMPL_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

LAP3

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	36 AA.
Sequence status	Fragment.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›36	›36	Cytosol aminopeptidase		PRO_0000165827
Experimental info
	Non-terminal residue	36	1

Sequences

	Sequence		Length	Mass (Da)
	P28839 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 2C0CECD973FAB49C	FASTA	36	4,015
	10 20 30 TKGLVLGIYS KEKEDDAPQF TSAGENFDKW VSGKLR

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: 1908238] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Intestine and Kidney.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases
PIR	PT0430.
3D structure databases
ProteinModelPortal	P28839.
SMR	P28839. Positions 1-36.
ModBase	Search...
Protein family/group databases
MEROPS	M17.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00631. CYTOSOL_AP. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPL_PIG

Accession

Primary (citable) accession number: P28839

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	November 16, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program