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P08473

- NEP_HUMAN

UniProt

P08473 - NEP_HUMAN

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Protein

Neprilysin

Gene

MME

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.3 Publications

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.2 Publications

Enzyme regulationi

Inhibited in a dose dependent manner by opiorphin.

Kineticsi

  1. KM=55.1 µM for angiotensin-11 Publication
  2. KM=179 µM for angiotensin-21 Publication
  3. KM=111.4 µM for angiotensin 1-91 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031Substrate carboxylBy similarity
Metal bindingi584 – 5841Zinc; catalytic
Metal bindingi588 – 5881Zinc; catalytic
Active sitei591 – 5911
Metal bindingi647 – 6471Zinc; catalytic
Active sitei651 – 6511Proton donor1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. endopeptidase activity Source: UniProtKB
  2. metalloendopeptidase activity Source: UniProtKB
  3. peptide binding Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. angiotensin maturation Source: Reactome
  2. beta-amyloid metabolic process Source: UniProtKB
  3. cellular protein metabolic process Source: Reactome
  4. cellular response to cytokine stimulus Source: UniProtKB
  5. cellular response to UV-A Source: UniProtKB
  6. cellular response to UV-B Source: UniProtKB
  7. creatinine metabolic process Source: UniProtKB
  8. kidney development Source: UniProtKB
  9. peptide metabolic process Source: UniProtKB
  10. proteolysis Source: UniProtKB
  11. replicative senescence Source: UniProtKB
  12. sensory perception of pain Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

Protein family/group databases

MEROPSiM13.001.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MME
Synonyms:EPN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7154. MME.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. brush border Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. dendrite Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. integral component of membrane Source: UniProtKB
  8. integral component of plasma membrane Source: UniProtKB
  9. neuron projection terminus Source: UniProtKB
  10. plasma membrane Source: UniProtKB
  11. synapse Source: UniProtKB
  12. synaptic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30864.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 750749NeprilysinPRO_0000078213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Disulfide bondi57 ↔ 62
Disulfide bondi80 ↔ 735
Disulfide bondi88 ↔ 695
Disulfide bondi143 ↔ 411
Glycosylationi145 – 1451N-linked (GlcNAc...)4 Publications
Disulfide bondi234 ↔ 242
Glycosylationi285 – 2851N-linked (GlcNAc...)1 Publication
Glycosylationi325 – 3251N-linked (GlcNAc...)3 Publications
Disulfide bondi621 ↔ 747
Glycosylationi628 – 6281N-linked (GlcNAc...)4 Publications

Post-translational modificationi

Myristoylation is a determinant of membrane targeting.1 Publication
Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate

Proteomic databases

MaxQBiP08473.
PaxDbiP08473.
PeptideAtlasiP08473.
PRIDEiP08473.

PTM databases

PhosphoSiteiP08473.

Expressioni

Gene expression databases

BgeeiP08473.
CleanExiHS_MME.
ExpressionAtlasiP08473. baseline and differential.
GenevestigatoriP08473.

Organism-specific databases

HPAiCAB000013.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CD9P219266EBI-353759,EBI-4280101
HSPA1BP081073EBI-353759,EBI-629985
HSPB1P047924EBI-353759,EBI-352682

Protein-protein interaction databases

BioGridi110455. 77 interactions.
IntActiP08473. 80 interactions.
STRINGi9606.ENSP00000353679.

Structurei

Secondary structure

1
750
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi60 – 7213
Turni79 – 813
Helixi83 – 9412
Beta strandi102 – 1054
Helixi106 – 12217
Helixi131 – 14414
Helixi146 – 1516
Turni152 – 1543
Helixi155 – 1584
Helixi161 – 1644
Helixi168 – 1703
Beta strandi171 – 1733
Helixi174 – 1774
Turni178 – 1814
Helixi184 – 19512
Beta strandi200 – 2089
Beta strandi211 – 22010
Beta strandi225 – 2284
Helixi229 – 2335
Helixi236 – 2383
Helixi239 – 25921
Helixi266 – 28621
Helixi290 – 2923
Helixi296 – 2994
Beta strandi302 – 3043
Helixi305 – 3117
Beta strandi316 – 3194
Helixi323 – 3319
Helixi332 – 3343
Beta strandi343 – 3475
Helixi349 – 35911
Helixi364 – 37916
Helixi380 – 3823
Helixi385 – 3895
Helixi392 – 3998
Helixi407 – 41812
Helixi420 – 43112
Helixi436 – 45419
Helixi455 – 4573
Beta strandi459 – 4613
Helixi463 – 47412
Beta strandi477 – 4815
Helixi485 – 4884
Helixi490 – 4967
Turni497 – 4993
Helixi507 – 52317
Turni524 – 5274
Beta strandi545 – 5473
Turni548 – 5514
Beta strandi552 – 5565
Helixi557 – 5593
Turni562 – 5643
Beta strandi567 – 5693
Helixi571 – 5766
Helixi578 – 58710
Helixi588 – 5903
Turni592 – 5954
Helixi609 – 62719
Helixi632 – 6343
Beta strandi636 – 6383
Turni641 – 6444
Helixi645 – 66925
Helixi682 – 69211
Beta strandi696 – 6983
Helixi700 – 70910
Helixi715 – 72410
Helixi727 – 7326

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4CTHX-ray2.15A52-750[»]
ProteinModelPortaliP08473.
SMRiP08473. Positions 55-750.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08473.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2827CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini52 – 750699ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 5123Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 238Stop-transfer sequenceSequence Analysis

Sequence similaritiesi

Belongs to the peptidase M13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3590.
GeneTreeiENSGT00760000119162.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiP08473.
KOiK01389.
OMAiVWCGTYR.
OrthoDBiEOG7PZRWQ.
PhylomeDBiP08473.
TreeFamiTF315192.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR024079. MetalloPept_cat_dom.
IPR029727. MME/CD10/NEP.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF114. PTHR11733:SF114. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08473-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA
60 70 80 90 100
TYDDGICKSS DCIKSAARLI QNMDATTEPC TDFFKYACGG WLKRNVIPET
110 120 130 140 150
SSRYGNFDIL RDELEVVLKD VLQEPKTEDI VAVQKAKALY RSCINESAID
160 170 180 190 200
SRGGEPLLKL LPDIYGWPVA TENWEQKYGA SWTAEKAIAQ LNSKYGKKVL
210 220 230 240 250
INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE ACTAYVDFMI
260 270 280 290 300
SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY
310 320 330 340 350
NKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE
360 370 380 390 400
YLTKLKPILT KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG
410 420 430 440 450
TTSETATWRR CANYVNGNME NAVGRLYVEA AFAGESKHVV EDLIAQIREV
460 470 480 490 500
FIQTLDDLTW MDAETKKRAE EKALAIKERI GYPDDIVSND NKLNNEYLEL
510 520 530 540 550
NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA VVNAFYSSGR
560 570 580 590 600
NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
610 620 630 640 650
GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA
660 670 680 690 700
DNGGLGQAYR AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP
710 720 730 740 750
EYAVNSIKTD VHSPGNFRII GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW
Length:750
Mass (Da):85,514
Last modified:January 23, 2007 - v2
Checksum:iBCF3827C39898630
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261P → R in AAA51915. (PubMed:14702039)Curated
Sequence conflicti44 – 441T → R in AAA51915. (PubMed:14702039)Curated
Sequence conflicti81 – 811T → R in AAA51915. (PubMed:14702039)Curated
Sequence conflicti304 – 3041T → R in AAA51915. (PubMed:14702039)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00811 mRNA. Translation: CAA68752.1.
J03779 mRNA. Translation: AAA51915.1.
M26628
, 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.
CCDSiCCDS3172.1.
PIRiA41387. HYHUN.
RefSeqiNP_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.
UniGeneiHs.307734.

Genome annotation databases

EnsembliENST00000360490; ENSP00000353679; ENSG00000196549.
ENST00000460393; ENSP00000418525; ENSG00000196549.
ENST00000462745; ENSP00000419653; ENSG00000196549.
ENST00000492661; ENSP00000420389; ENSG00000196549.
ENST00000493237; ENSP00000417079; ENSG00000196549.
ENST00000615825; ENSP00000478173; ENSG00000196549.
GeneIDi4311.
KEGGihsa:4311.
UCSCiuc003fab.1. human.

Polymorphism databases

DMDMi128062.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00811 mRNA. Translation: CAA68752.1 .
J03779 mRNA. Translation: AAA51915.1 .
M26628
, 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.
CCDSi CCDS3172.1.
PIRi A41387. HYHUN.
RefSeqi NP_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.
UniGenei Hs.307734.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DL9 model - A 508-750 [» ]
1DMT X-ray 2.10 A 55-750 [» ]
1QVD model - A 55-750 [» ]
1R1H X-ray 1.95 A 55-750 [» ]
1R1I X-ray 2.60 A 55-750 [» ]
1R1J X-ray 2.35 A 55-750 [» ]
1Y8J X-ray 2.25 A 55-750 [» ]
2QPJ X-ray 2.05 A 55-750 [» ]
2YB9 X-ray 2.40 A 55-750 [» ]
4CTH X-ray 2.15 A 52-750 [» ]
ProteinModelPortali P08473.
SMRi P08473. Positions 55-750.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110455. 77 interactions.
IntActi P08473. 80 interactions.
STRINGi 9606.ENSP00000353679.

Chemistry

BindingDBi P08473.
ChEMBLi CHEMBL1944.
DrugBanki DB00616. Candoxatril.
DB06655. Liraglutide.
GuidetoPHARMACOLOGYi 1611.

Protein family/group databases

MEROPSi M13.001.

PTM databases

PhosphoSitei P08473.

Polymorphism databases

DMDMi 128062.

Proteomic databases

MaxQBi P08473.
PaxDbi P08473.
PeptideAtlasi P08473.
PRIDEi P08473.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360490 ; ENSP00000353679 ; ENSG00000196549 .
ENST00000460393 ; ENSP00000418525 ; ENSG00000196549 .
ENST00000462745 ; ENSP00000419653 ; ENSG00000196549 .
ENST00000492661 ; ENSP00000420389 ; ENSG00000196549 .
ENST00000493237 ; ENSP00000417079 ; ENSG00000196549 .
ENST00000615825 ; ENSP00000478173 ; ENSG00000196549 .
GeneIDi 4311.
KEGGi hsa:4311.
UCSCi uc003fab.1. human.

Organism-specific databases

CTDi 4311.
GeneCardsi GC03P154741.
HGNCi HGNC:7154. MME.
HPAi CAB000013.
MIMi 120520. gene.
neXtProti NX_P08473.
PharmGKBi PA30864.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3590.
GeneTreei ENSGT00760000119162.
HOGENOMi HOG000245574.
HOVERGENi HBG005554.
InParanoidi P08473.
KOi K01389.
OMAi VWCGTYR.
OrthoDBi EOG7PZRWQ.
PhylomeDBi P08473.
TreeFami TF315192.

Enzyme and pathway databases

Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.

Miscellaneous databases

EvolutionaryTracei P08473.
GeneWikii Neprilysin.
GenomeRNAii 4311.
NextBioi 16959.
PROi P08473.
SOURCEi Search...

Gene expression databases

Bgeei P08473.
CleanExi HS_MME.
ExpressionAtlasi P08473. baseline and differential.
Genevestigatori P08473.

Family and domain databases

Gene3Di 3.40.390.10. 2 hits.
InterProi IPR024079. MetalloPept_cat_dom.
IPR029727. MME/CD10/NEP.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view ]
PANTHERi PTHR11733. PTHR11733. 1 hit.
PTHR11733:SF114. PTHR11733:SF114. 1 hit.
Pfami PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view ]
PRINTSi PR00786. NEPRILYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiNEP_HUMAN
AccessioniPrimary (citable) accession number: P08473
Secondary accession number(s): A8K6U6, D3DNJ9, Q3MIX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3