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P19621

- NEP_PIG

UniProt

P19621 - NEP_PIG

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Protein

Neprilysin

Gene

MME

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.

Cofactori

Binds 1 zinc ion per subunit.

GO - Molecular functioni

  1. metallopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:MME
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›26›26NeprilysinPRO_0000078215Add
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M13 family.Curated

Keywords - Domaini

Transmembrane

Sequencei

Sequence statusi: Fragment.

P19621-1 [UniParc]FASTAAdd to Basket

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        10         20
PKPKKKQRWT PLEISLEVLV LVLVXI
Length:26
Mass (Da):3,039
Last modified:February 1, 1991 - v1
Checksum:i3848804A9DDF7DEF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei26 – 261

Sequence databases

PIRiA26070.

Cross-referencesi

Sequence databases

PIRi A26070.

3D structure databases

ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL6107.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Kidney.

Entry informationi

Entry nameiNEP_PIG
AccessioniPrimary (citable) accession number: P19621
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 77 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