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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_RABIT               Reviewed;         750 AA.
P08049;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 142.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Kidney;
PubMed=2440677;
Devault A., Lazure C., Nault C., le Moual H., Seidah N.G.,
Chretien M., Kahn P., Powell J., Mallet J., Beaumont A., Roques B.P.,
Crine P., Boileau G.;
"Amino acid sequence of rabbit kidney neutral endopeptidase 24.11
(enkephalinase) deduced from a complementary DNA.";
EMBO J. 6:1317-1322(1987).
[2]
ERRATUM.
Devault A., Lazure C., Nault C., le Moual H., Seidah N.G.,
Chretien M., Kahn P., Powell J., Mallet J., Beaumont A., Roques B.P.,
Crine P., Boileau G.;
EMBO J. 6:2506-2506(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 206-274.
PubMed=3297057; DOI=10.1016/0006-291X(87)91347-7;
Kahn P.H., Powell J.F., Beaumont A., Roques B.P., Mallet J.J.;
"An antibody purified with a lambda GT11 fusion protein precipitates
enkephalinase activity.";
Biochem. Biophys. Res. Commun. 145:488-493(1987).
[4]
MUTAGENESIS.
PubMed=3162886; DOI=10.1016/0014-5793(88)80701-4;
Devault A., Sales V., Nault C., Beaumont A., Roques B., Crine P.,
Boileau G.;
"Exploration of the catalytic site of endopeptidase 24.11 by site-
directed mutagenesis. Histidine residues 583 and 587 are essential for
catalysis.";
FEBS Lett. 231:54-58(1988).
-!- 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:
Reaction=Preferential cleavage of polypeptides between hydrophobic
residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11;
Evidence={ECO:0000250|UniProtKB:P08473};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein.
-!- 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; X05338; CAA28950.1; -; mRNA.
EMBL; M16593; AAA53694.1; -; mRNA.
PIR; A29451; HYRBN.
RefSeq; NP_001095155.1; NM_001101685.1.
UniGene; Ocu.2011; -.
PDB; 4XBH; X-ray; 2.11 A; A/B=55-750.
PDB; 4ZR5; X-ray; 2.80 A; A/B=55-750.
PDB; 5V48; X-ray; 3.00 A; A/B=55-750.
PDBsum; 4XBH; -.
PDBsum; 4ZR5; -.
PDBsum; 5V48; -.
ProteinModelPortal; P08049; -.
SMR; P08049; -.
STRING; 9986.ENSOCUP00000021723; -.
BindingDB; P08049; -.
ChEMBL; CHEMBL3768; -.
MEROPS; M13.001; -.
PRIDE; P08049; -.
GeneID; 100009251; -.
KEGG; ocu:100009251; -.
CTD; 4311; -.
eggNOG; KOG3624; Eukaryota.
eggNOG; COG3590; LUCA.
HOGENOM; HOG000245574; -.
HOVERGEN; HBG005554; -.
InParanoid; P08049; -.
KO; K01389; -.
PRO; PR:P08049; -.
Proteomes; UP000001811; Unplaced.
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: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; -; 1.
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.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; 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.
CHAIN 2 750 Neprilysin.
/FTId=PRO_0000078216.
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.
METAL 588 588 Zinc; catalytic.
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:0000250}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
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}.
HELIX 60 72 {ECO:0000244|PDB:4XBH}.
TURN 79 81 {ECO:0000244|PDB:4XBH}.
HELIX 83 94 {ECO:0000244|PDB:4XBH}.
STRAND 102 105 {ECO:0000244|PDB:4XBH}.
HELIX 106 122 {ECO:0000244|PDB:4XBH}.
HELIX 131 144 {ECO:0000244|PDB:4XBH}.
HELIX 146 150 {ECO:0000244|PDB:4XBH}.
TURN 151 154 {ECO:0000244|PDB:4XBH}.
HELIX 155 160 {ECO:0000244|PDB:4XBH}.
HELIX 161 164 {ECO:0000244|PDB:4XBH}.
HELIX 168 170 {ECO:0000244|PDB:4XBH}.
STRAND 171 173 {ECO:0000244|PDB:4XBH}.
HELIX 174 177 {ECO:0000244|PDB:4XBH}.
TURN 178 181 {ECO:0000244|PDB:4XBH}.
HELIX 184 195 {ECO:0000244|PDB:4XBH}.
STRAND 200 208 {ECO:0000244|PDB:4XBH}.
STRAND 211 220 {ECO:0000244|PDB:4XBH}.
STRAND 225 228 {ECO:0000244|PDB:4XBH}.
HELIX 229 233 {ECO:0000244|PDB:4XBH}.
HELIX 236 238 {ECO:0000244|PDB:4XBH}.
HELIX 239 259 {ECO:0000244|PDB:4XBH}.
HELIX 266 286 {ECO:0000244|PDB:4XBH}.
HELIX 290 293 {ECO:0000244|PDB:4XBH}.
HELIX 296 299 {ECO:0000244|PDB:4XBH}.
STRAND 302 304 {ECO:0000244|PDB:4XBH}.
HELIX 305 311 {ECO:0000244|PDB:4XBH}.
HELIX 323 331 {ECO:0000244|PDB:4XBH}.
HELIX 332 334 {ECO:0000244|PDB:4XBH}.
STRAND 343 347 {ECO:0000244|PDB:4XBH}.
HELIX 349 359 {ECO:0000244|PDB:4XBH}.
HELIX 364 376 {ECO:0000244|PDB:4XBH}.
TURN 377 379 {ECO:0000244|PDB:4XBH}.
HELIX 380 382 {ECO:0000244|PDB:4XBH}.
HELIX 385 389 {ECO:0000244|PDB:4XBH}.
HELIX 392 399 {ECO:0000244|PDB:4XBH}.
HELIX 407 418 {ECO:0000244|PDB:4XBH}.
HELIX 420 431 {ECO:0000244|PDB:4XBH}.
HELIX 436 454 {ECO:0000244|PDB:4XBH}.
TURN 455 457 {ECO:0000244|PDB:4XBH}.
STRAND 459 461 {ECO:0000244|PDB:5V48}.
HELIX 463 475 {ECO:0000244|PDB:4XBH}.
STRAND 477 481 {ECO:0000244|PDB:4XBH}.
HELIX 485 488 {ECO:0000244|PDB:4XBH}.
HELIX 490 496 {ECO:0000244|PDB:4XBH}.
TURN 497 499 {ECO:0000244|PDB:4XBH}.
HELIX 507 523 {ECO:0000244|PDB:4XBH}.
HELIX 524 527 {ECO:0000244|PDB:4XBH}.
STRAND 545 547 {ECO:0000244|PDB:4XBH}.
TURN 548 551 {ECO:0000244|PDB:4XBH}.
STRAND 552 556 {ECO:0000244|PDB:4XBH}.
HELIX 557 559 {ECO:0000244|PDB:4XBH}.
TURN 562 564 {ECO:0000244|PDB:4XBH}.
HELIX 571 576 {ECO:0000244|PDB:4XBH}.
HELIX 578 588 {ECO:0000244|PDB:4XBH}.
HELIX 594 596 {ECO:0000244|PDB:4XBH}.
HELIX 609 627 {ECO:0000244|PDB:4XBH}.
HELIX 632 634 {ECO:0000244|PDB:4XBH}.
TURN 641 644 {ECO:0000244|PDB:4XBH}.
HELIX 645 669 {ECO:0000244|PDB:4XBH}.
HELIX 682 693 {ECO:0000244|PDB:4XBH}.
STRAND 696 698 {ECO:0000244|PDB:4XBH}.
HELIX 700 709 {ECO:0000244|PDB:4XBH}.
HELIX 715 724 {ECO:0000244|PDB:4XBH}.
HELIX 727 732 {ECO:0000244|PDB:4XBH}.
SEQUENCE 750 AA; 85582 MW; 0F26AF7316BB9D12 CRC64;
MGRSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTV IAVTMIALYA TYDDGICKSS
DCIKSAARLI QNMDATAEPC TDFFKYACGG WLKRNVIPET SSRYSNFDIL RDELEVILKD
VLQEPKTEDI VAVQKAKTLY RSCVNETAID SRGGQPLLKL LPDVYGWPVA TQNWEQTYGT
SWSAEKSIAQ LNSNYGKKVL INFFVGTDDK NSMNHIIHID QPRLGLPSRD YYECTGIYKE
ACTAYVDFMI AVAKLIRQEE GLPIDENQIS VEMNKVMELE KEIANATTKS EDRNDPMLLY
NKMTLAQIQN NFSLEINGKP FSWSNFTNEI MSTVNINIPN EEDVVVYAPE YLIKLKPILT
KYFPRDFQNL FSWRFIMDLV SSLSRTYKDS RNAFRKALYG TTSESATWRR CANYVNGNME
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKKAE EKALAIKERI
GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWITGAA
IVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
GDLVDWWTQQ SANNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGIGQAYR
AYQNYVKKNG EEKLLPGIDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
GSLQNSVEFS EAFQCPKNSY MNPEKKCRVW


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