P19621 (NEP_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neprilysin
EC=3.4.24.11

Alternative name(s):
Atriopeptidase
Enkephalinase
Neutral endopeptidase 24.11
Short name=NEP
Short name=Neutral endopeptidase
Skin fibroblast elastase
Short name=SFE
CD_antigen=CD10

Gene names

Name:

MME

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	26 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 By similarity. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers By similarity.
Catalytic activity	Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
Cofactor	Binds 1 zinc ion per subunit.
Subcellular location	Cell membrane; Single-pass type II membrane protein.
Sequence similarities	Belongs to the peptidase M13 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Lipoprotein Myristate
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metallopeptidase activity 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 – ›26	›26	Neprilysin		PRO_0000078215
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	26	1

Sequences

	Sequence		Length	Mass (Da)
	P19621 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 3848804A9DDF7DEF	FASTA	26	3,039
	10 20 PKPKKKQRWT PLEISLEVLV LVLVXI

References

[1]	"The N-terminal amino acid sequence of pig kidney endopeptidase-24.11 shows homology with pro-sucrase-isomaltase." Fulcher I.S., Pappin D.J.C., Kenny A.J. Biochem. J. 240:305-308(1986) [PubMed: 3548708] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Kidney.

Cross-references

Sequence databases
PIR	A26070.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M13.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00142. ZINC_PROTEASE. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NEP_PIG

Accession

Primary (citable) accession number: P19621

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program