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P08473 (NEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neprilysin

EC=3.4.24.11
Alternative name(s):
Atriopeptidase
Common acute lymphocytic leukemia antigen
Short name=CALLA
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
Synonyms:EPN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers. Ref.9 Ref.12 Ref.14

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit. Ref.18 Ref.19

Enzyme regulation

Inhibited in a dose dependent manner by opiorphin.

Subcellular location

Cell membrane; Single-pass type II membrane protein.

Post-translational modification

Myristoylation is a determinant of membrane targeting.

Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity.

Miscellaneous

Important cell surface marker in the diagnostic of human acute lymphocytic leukemia.

Sequence similarities

Belongs to the peptidase M13 family.

Biophysicochemical properties

Kinetic parameters:

KM=55.1 µM for angiotensin-1 Ref.12

KM=179 µM for angiotensin-2

KM=111.4 µM for angiotensin 1-9

Sequence caution

The sequence CAA30157.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Myristate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin maturation

Traceable author statement. Source: Reactome

beta-amyloid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to UV-A

Inferred from direct assay Ref.14. Source: UniProtKB

cellular response to UV-B

Inferred from direct assay Ref.14. Source: UniProtKB

cellular response to cytokine stimulus

Inferred from direct assay Ref.14. Source: UniProtKB

creatinine metabolic process

Inferred from mutant phenotype PubMed 22024547. Source: UniProtKB

kidney development

Inferred from expression pattern PubMed 22272689. Source: UniProtKB

peptide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from direct assay Ref.14Ref.10. Source: UniProtKB

replicative senescence

Inferred from expression pattern Ref.14. Source: UniProtKB

sensory perception of pain

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

brush border

Inferred from direct assay PubMed 22272689. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.14PubMed 22272689. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement PubMed 2521388. Source: UniProtKB

neuron projection terminus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.14PubMed 22272689. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionendopeptidase activity

Inferred from direct assay Ref.12Ref.14Ref.10. Source: UniProtKB

metalloendopeptidase activity

Inferred from mutant phenotype PubMed 2521388. Source: UniProtKB

peptide binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17342744PubMed 23289620. Source: IntAct

zinc ion binding

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 750749Neprilysin
PRO_0000078213

Regions

Topological domain2 – 2827Cytoplasmic Potential
Transmembrane29 – 5123Helical; Signal-anchor for type II membrane protein; Potential
Topological domain52 – 750699Extracellular Potential
Motif16 – 238Stop-transfer sequence Potential

Sites

Active site5911
Active site6511Proton donor Ref.10
Metal binding5841Zinc; catalytic
Metal binding5881Zinc; catalytic
Metal binding6471Zinc; catalytic
Binding site1031Substrate carboxyl By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Ref.15
Glycosylation1451N-linked (GlcNAc...) Ref.11 Ref.17 Ref.18 Ref.19
Glycosylation2851N-linked (GlcNAc...) Ref.11
Glycosylation3251N-linked (GlcNAc...) Ref.17 Ref.18 Ref.19
Glycosylation6281N-linked (GlcNAc...) Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond57 ↔ 62 Ref.18 Ref.19
Disulfide bond80 ↔ 735 Ref.18 Ref.19
Disulfide bond88 ↔ 695 Ref.18 Ref.19
Disulfide bond143 ↔ 411 Ref.18 Ref.19
Disulfide bond234 ↔ 242 Ref.18 Ref.19
Disulfide bond621 ↔ 747 Ref.18 Ref.19

Experimental info

Sequence conflict261P → R in AAA51915. Ref.4
Sequence conflict441T → R in AAA51915. Ref.4
Sequence conflict811T → R in AAA51915. Ref.4
Sequence conflict3041T → R in AAA51915. Ref.4

Secondary structure

.................................................................................................................... 750
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08473 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BCF3827C39898630

FASTA75085,514
        10         20         30         40         50         60 
MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS 

        70         80         90        100        110        120 
DCIKSAARLI QNMDATTEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD 

       130        140        150        160        170        180 
VLQEPKTEDI VAVQKAKALY RSCINESAID SRGGEPLLKL LPDIYGWPVA TENWEQKYGA 

       190        200        210        220        230        240 
SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE 

       250        260        270        280        290        300 
ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY 

       310        320        330        340        350        360 
NKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT 

       370        380        390        400        410        420 
KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME 

       430        440        450        460        470        480 
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI 

       490        500        510        520        530        540 
GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA 

       550        560        570        580        590        600 
VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD 

       610        620        630        640        650        660 
GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR 

       670        680        690        700        710        720 
AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII 

       730        740        750 
GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW 

« Hide

References

« Hide 'large scale' references
[1]"Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase."
Letarte M., Vera S., Tran R., Addis J.B.L., Onizuka R.J., Quackenbush E.J., Jongeneel C.V., McInnes R.R.
J. Exp. Med. 168:1247-1253(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Molecular cloning of the common acute lymphoblastic leukemia antigen (CALLA) identifies a type II integral membrane protein."
Shipp M.A., Richardson N.E., Sayre P.H., Brown N.R., Masteller E.L., Clayton L.K., Ritz J., Reinherz E.L.
Proc. Natl. Acad. Sci. U.S.A. 85:4819-4823(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24.11): multiple miniexons and separate 5' untranslated regions."
D'Adamio L., Shipp M.A., Masteller E.L., Reinherz E.L.
Proc. Natl. Acad. Sci. U.S.A. 86:7103-7107(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[8]"Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)."
Malfroy B., Kuang W.-J., Seeburg P.H., Mason A.J., Schofield P.R.
FEBS Lett. 229:206-210(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-750.
Tissue: Placenta.
[9]"Endopeptidase-24.11 in human plasma degrades atrial natriuretic factor (ANF) to ANF(99-105/106-126)."
Yandle T.G., Brennan S.O., Espiner E.A., Nicholls M.G., Richards A.M.
Peptides 10:891-894(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE DEGRADATION OF ANF.
[10]"Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11."
Le Moual H., Dion N., Roques B.P., Crine P., Boileau G.
Eur. J. Biochem. 221:475-480(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE ASP-651.
[11]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-145 AND ASN-285.
[12]"Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism."
Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M.
Biochem. J. 383:45-51(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOTENSIN PEPTIDE METABOLISM, BIOPHYSICOCHEMICAL PROPERTIES.
[13]"Human opiorphin, a natural antinociceptive modulator of opioid-dependent pathways."
Wisner A., Dufour E., Messaoudi M., Nejdi A., Marcel A., Ungeheuer M.-N., Rougeot C.
Proc. Natl. Acad. Sci. U.S.A. 103:17979-17984(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY OPIORPHIN.
[14]"Neprilysin is identical to skin fibroblast elastase: its role in skin aging and UV responses."
Morisaki N., Moriwaki S., Sugiyama-Nakagiri Y., Haketa K., Takema Y., Imokawa G.
J. Biol. Chem. 285:39819-39827(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS SKIN FIBROBLAST ELASTASE, FUNCTION.
[15]"Neutral endopeptidase is a myristoylated protein."
Zheng R., Horiguchi A., Iida K., Lee J., Shen R., Goodman O.B. Jr., Nanus D.M.
Mol. Cell. Biochem. 335:173-180(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[16]"The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity."
Sato B., Katagiri Y.U., Iijima K., Yamada H., Ito S., Kawasaki N., Okita H., Fujimoto J., Kiyokawa N.
Biochim. Biophys. Acta 1820:1715-1723(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-628.
[17]"Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon."
Oefner C., D'Arcy A., Hennig M., Winkler F.K., Dale G.E.
J. Mol. Biol. 296:341-349(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
[18]"Structural analysis of neprilysin with various specific and potent inhibitors."
Oefner C., Roques B.P., Fournie-Zaluski M.-C., Dale G.E.
Acta Crystallogr. D 60:392-396(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 55-750 IN COMPLEXES WITH ZINC IONS AND SYNTHETIC INHIBITORS, DISULFIDE BONDS, COFACTOR, GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
[19]"Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV."
Oefner C., Pierau S., Schulz H., Dale G.E.
Acta Crystallogr. D 63:975-981(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 55-750 IN COMPLEX WITH ZINC IONS AND THE SYNTHETIC INHIBITOR MCB3937, DISULFIDE BONDS, COFACTOR, GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00811 mRNA. Translation: CAA68752.1.
J03779 mRNA. Translation: AAA51915.1.
M26628 expand/collapse EMBL AC list , M26607, M26608, M26609, M26610, M26611, M26612, M26613, M26614, M26615, M26616, M26617, M26618, M26619, M26620, M26621, M26622, M26623, M26624, M26625, M26626, M26627 Genomic DNA. Translation: AAA52294.1.
AK291761 mRNA. Translation: BAF84450.1.
EU326307 Genomic DNA. Translation: ACA05913.1.
CH471052 Genomic DNA. Translation: EAW78754.1.
CH471052 Genomic DNA. Translation: EAW78755.1.
CH471052 Genomic DNA. Translation: EAW78756.1.
CH471052 Genomic DNA. Translation: EAW78757.1.
CH471052 Genomic DNA. Translation: EAW78758.1.
BC101632 mRNA. Translation: AAI01633.1.
BC101658 mRNA. Translation: AAI01659.1.
X07166 mRNA. Translation: CAA30157.1. Different initiation.
CCDSCCDS3172.1.
PIRHYHUN. A41387.
RefSeqNP_000893.2. NM_000902.3.
NP_009218.2. NM_007287.2.
NP_009219.2. NM_007288.2.
NP_009220.2. NM_007289.2.
XP_006713709.1. XM_006713646.1.
XP_006713710.1. XM_006713647.1.
UniGeneHs.307734.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DL9model-A508-750[»]
1DMTX-ray2.10A55-750[»]
1QVDmodel-A55-750[»]
1R1HX-ray1.95A55-750[»]
1R1IX-ray2.60A55-750[»]
1R1JX-ray2.35A55-750[»]
1Y8JX-ray2.25A55-750[»]
2QPJX-ray2.05A55-750[»]
2YB9X-ray2.40A55-750[»]
ProteinModelPortalP08473.
SMRP08473. Positions 55-750.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110455. 77 interactions.
IntActP08473. 80 interactions.
STRING9606.ENSP00000353679.

Chemistry

BindingDBP08473.
ChEMBLCHEMBL1944.
DrugBankDB00616. Candoxatril.
GuidetoPHARMACOLOGY1611.

Protein family/group databases

MEROPSM13.001.

PTM databases

PhosphoSiteP08473.

Polymorphism databases

DMDM128062.

Proteomic databases

MaxQBP08473.
PaxDbP08473.
PeptideAtlasP08473.
PRIDEP08473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360490; ENSP00000353679; ENSG00000196549.
ENST00000460393; ENSP00000418525; ENSG00000196549.
ENST00000462745; ENSP00000419653; ENSG00000196549.
ENST00000492661; ENSP00000420389; ENSG00000196549.
ENST00000493237; ENSP00000417079; ENSG00000196549.
GeneID4311.
KEGGhsa:4311.
UCSCuc003fab.1. human.

Organism-specific databases

CTD4311.
GeneCardsGC03P154741.
HGNCHGNC:7154. MME.
HPACAB000013.
MIM120520. gene.
neXtProtNX_P08473.
PharmGKBPA30864.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3590.
HOGENOMHOG000245574.
HOVERGENHBG005554.
InParanoidP08473.
KOK01389.
OMAVWCGTYR.
OrthoDBEOG7PZRWQ.
PhylomeDBP08473.
TreeFamTF315192.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP08473.
BgeeP08473.
CleanExHS_MME.
GenevestigatorP08473.

Family and domain databases

Gene3D3.40.390.10. 2 hits.
InterProIPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERPTHR11733. PTHR11733. 1 hit.
PfamPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSPR00786. NEPRILYSIN.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08473.
GeneWikiNeprilysin.
GenomeRNAi4311.
NextBio16959.
PROP08473.
SOURCESearch...

Entry information

Entry nameNEP_HUMAN
AccessionPrimary (citable) accession number: P08473
Secondary accession number(s): A8K6U6, D3DNJ9, Q3MIX4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries