Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00708
Entry Name
UniProt Accession
Theoretical PI
5.54
Molecular Weight
85513.94
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Neprilysin
Protein Synonyms/Alias
3.4.24.11; Atriopeptidase; Common acute lymphocytic leukemia antigen; CALLA; Enkephalinase; Neutral endopeptidase 24.11; NEP; Neutral endopeptidase; Skin fibroblast elastase; SFE; CD10;
Gene Name
MME
Gene Synonyms/Alias
EPN;
Created Date
01-AUG-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGKSESQMD
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Zheng R, Horiguchi A, Iida K, Lee J, Shen R, Goodman OB Jr, Nanus DM. Neutral endopeptidase is a myristoylated protein. Mol Cell Biochem. 2010Feb;335(1-2):173-80. doi: 10.1007/s11010-009-0253-8. Epub 2009 Sep 15. PubMedPMID: 19756956.[PMID:19756956]
Functional Description
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.
Sequence Annotation
Topological domain: 2 28 Cytoplasmic.
Transmembrane: 29 51 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 52 750 Extracellular.
Motif: 16 23 Stop-transfer sequence.
Active site: 651 651 Proton donor.
Metal binding site: 584 584 Zinc; catalytic.
Metal binding site: 588 588 Zinc; catalytic.
Metal binding site: 647 647 Zinc; catalytic.
Binding site: 103 103 Substrate carboxyl.
Protein Length
750 AA.
Protein Sequence
(Canonical)
MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS  60
DCIKSAARLI QNMDATTEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD  120
VLQEPKTEDI VAVQKAKALY RSCINESAID SRGGEPLLKL LPDIYGWPVA TENWEQKYGA  180
SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE  240
ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY  300
NKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT  360
KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME  420
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI  480
GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA  540
VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD  600
GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR  660
AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII  720
GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW                                   750
FASTA
(Canonical)
>LipidDB-9606-00708|P08473
MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSS
DCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKD
VLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGA
SWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKE
ACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLY
NKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILT
KYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNME
NAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERI
GYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAA
VVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKD
GDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYR
AYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRII
GTLQNSAEFSEAFHCRKNSYMNPEKKCRVW
Gene Ontology
GO:0030424; C:axon; ISS:UniProtKB
GO:0005903; C:brush border; IDA:UniProtKB
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0030425; C:dendrite; ISS:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0016021; C:integral component of membrane; NAS:UniProtKB
GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB
GO:0044306; C:neuron projection terminus; ISS:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0045202; C:synapse; ISS:UniProtKB
GO:0008021; C:synaptic vesicle; ISS:UniProtKB
GO:0004175; F:endopeptidase activity; IDA:UniProtKB
GO:0004222; F:metalloendopeptidase activity; IMP:UniProtKB
GO:0042277; F:peptide binding; ISS:UniProtKB
GO:0008270; F:zinc ion binding; IDA:UniProtKB
GO:0002003; P:angiotensin maturation; TAS:Reactome
GO:0050435; P:beta-amyloid metabolic process; ISS:UniProtKB
GO:0044267; P:cellular protein metabolic process; TAS:Reactome
GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB
GO:0071492; P:cellular response to UV-A; IDA:UniProtKB
GO:0071493; P:cellular response to UV-B; IDA:UniProtKB
GO:0046449; P:creatinine metabolic process; IMP:UniProtKB
GO:0001822; P:kidney development; IEP:UniProtKB
GO:0006518; P:peptide metabolic process; ISS:UniProtKB
GO:0006508; P:proteolysis; IDA:UniProtKB
GO:0090399; P:replicative senescence; IEP:UniProtKB
GO:0019233; P:sensory perception of pain; ISS:UniProtKB
Interpro
InterPro; IPR024079; MetalloPept_cat_dom
InterPro; IPR029727; MME/CD10/NEP
InterPro; IPR000718; Peptidase_M13
InterPro; IPR018497; Peptidase_M13_C
InterPro; IPR008753; Peptidase_M13_N
Pfam
Pfam; PF01431; Peptidase_M13;
Pfam; PF05649; Peptidase_M13_N;
SMART
PROSITE
PROSITE; PS00142; ZINC_PROTEASE;
PRINTS
PRINTS; PR00786; NEPRILYSIN;