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Neprilysin (EC 3.4.24.11) (Atriopeptidase) (Enkephalinase) (Neutral endopeptidase 24.11) (NEP) (Neutral endopeptidase) (Skin fibroblast elastase) (SFE) (CD antigen CD10)

 NEP_PONAB               Reviewed;         750 AA.
Q5RE69; Q5R5K3; Q5RFQ2;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
23-MAY-2018, entry version 84.
RecName: Full=Neprilysin;
EC=3.4.24.11 {ECO:0000250|UniProtKB:P08473};
AltName: Full=Atriopeptidase;
AltName: Full=Enkephalinase;
AltName: Full=Neutral endopeptidase 24.11;
Short=NEP;
Short=Neutral endopeptidase;
AltName: Full=Skin fibroblast elastase;
Short=SFE;
AltName: CD_antigen=CD10;
Name=MME;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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. {ECO:0000250|UniProtKB:P08473}.
-!- CATALYTIC ACTIVITY: Preferential cleavage of polypeptides between
hydrophobic residues, particularly with Phe or Tyr at P1'.
{ECO:0000250|UniProtKB:P08473}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type II membrane protein {ECO:0000250}.
-!- PTM: Myristoylation is a determinant of membrane targeting.
{ECO:0000250}.
-!- PTM: Glycosylation at Asn-628 is necessary both for surface
expression and neutral endopeptidase activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CR857100; CAH89405.1; -; mRNA.
EMBL; CR857668; CAH89938.1; -; mRNA.
EMBL; CR860855; CAH92963.1; -; mRNA.
RefSeq; NP_001126748.1; NM_001133276.1.
ProteinModelPortal; Q5RE69; -.
SMR; Q5RE69; -.
STRING; 9601.ENSPPYP00000015904; -.
MEROPS; M13.001; -.
PRIDE; Q5RE69; -.
Ensembl; ENSPPYT00000016535; ENSPPYP00000015904; ENSPPYG00000014224.
GeneID; 100173750; -.
KEGG; pon:100173750; -.
CTD; 4311; -.
eggNOG; KOG3624; Eukaryota.
eggNOG; COG3590; LUCA.
GeneTree; ENSGT00760000119162; -.
HOGENOM; HOG000245574; -.
HOVERGEN; HBG005554; -.
InParanoid; Q5RE69; -.
KO; K01389; -.
OMA; TATWRRC; -.
OrthoDB; EOG091G025Y; -.
TreeFam; TF315192; -.
Proteomes; UP000001595; Chromosome 3.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005903; C:brush border; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044306; C:neuron projection terminus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
GO; GO:0008238; F:exopeptidase activity; IEA:Ensembl.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
GO; GO:0046449; P:creatinine metabolic process; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; ISS:UniProtKB.
GO; GO:0006518; P:peptide metabolic process; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0090399; P:replicative senescence; ISS:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
CDD; cd08662; M13; 1.
Gene3D; 3.40.390.10; -; 3.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR029727; MME/CD10/NEP.
InterPro; IPR000718; Peptidase_M13.
InterPro; IPR018497; Peptidase_M13_C.
InterPro; IPR008753; Peptidase_M13_N.
PANTHER; PTHR11733; PTHR11733; 1.
PANTHER; PTHR11733:SF114; PTHR11733:SF114; 1.
Pfam; PF01431; Peptidase_M13; 1.
Pfam; PF05649; Peptidase_M13_N; 1.
PRINTS; PR00786; NEPRILYSIN.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease;
Myristate; Phosphoprotein; Protease; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08473}.
CHAIN 2 750 Neprilysin.
/FTId=PRO_0000319885.
TOPO_DOM 2 28 Cytoplasmic. {ECO:0000255}.
TRANSMEM 29 51 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 52 750 Extracellular. {ECO:0000255}.
MOTIF 16 23 Stop-transfer sequence. {ECO:0000255}.
ACT_SITE 585 585 {ECO:0000255|PROSITE-ProRule:PRU10095}.
ACT_SITE 651 651 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 584 584 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 588 588 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 647 647 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
BINDING 103 103 Substrate carboxyl. {ECO:0000250}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:P08473}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:P08473}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 62 {ECO:0000250}.
DISULFID 80 735 {ECO:0000250}.
DISULFID 88 695 {ECO:0000250}.
DISULFID 143 411 {ECO:0000250}.
DISULFID 234 242 {ECO:0000250}.
DISULFID 621 747 {ECO:0000250}.
CONFLICT 115 115 E -> G (in Ref. 1; CAH89405).
{ECO:0000305}.
CONFLICT 175 175 E -> K (in Ref. 1; CAH89405).
{ECO:0000305}.
CONFLICT 523 523 L -> P (in Ref. 1; CAH89938).
{ECO:0000305}.
CONFLICT 681 681 N -> S (in Ref. 1; CAH92963).
{ECO:0000305}.
CONFLICT 729 729 F -> C (in Ref. 1; CAH92963).
{ECO:0000305}.
SEQUENCE 750 AA; 85514 MW; C4D1216E8361352F CRC64;
MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS
DCIKSAARLI QNMDATAEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD
VLQEPKTEDI VAVQKAKTLY RSCINESAID SRGGEPLLKL LPDVYGWPVA TENWEQKYGA
SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE
ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY
KKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT
KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI
GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA
VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR
AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW


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