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Q61391

- NEP_MOUSE

UniProt

Q61391 - NEP_MOUSE

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Protein
Neprilysin
Gene
Mme
Organism
Mus musculus (Mouse)
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 By similarity. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031Substrate carboxyl By similarity
Metal bindingi584 – 5841Zinc; catalytic By similarity
Active sitei585 – 5851 By similarity
Metal bindingi588 – 5881Zinc; catalytic By similarity
Metal bindingi647 – 6471Zinc; catalytic By similarity
Active sitei651 – 6511Proton donor By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: UniProtKB
  2. peptidase activity Source: MGI
  3. peptide binding Source: UniProtKB
  4. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. beta-amyloid metabolic process Source: MGI
  2. cellular response to UV-A Source: UniProtKB
  3. cellular response to UV-B Source: UniProtKB
  4. cellular response to cytokine stimulus Source: UniProtKB
  5. creatinine metabolic process Source: UniProtKB
  6. kidney development Source: UniProtKB
  7. peptide metabolic process Source: UniProtKB
  8. proteolysis Source: UniProtKB
  9. replicative senescence Source: UniProtKB
  10. 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_196539. 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
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:97004. Mme.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2827Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei29 – 5123Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini52 – 750699Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. axon Source: MGI
  2. brush border Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. dendrite Source: MGI
  5. integral component of membrane Source: UniProtKB-KW
  6. membrane Source: MGI
  7. neuron projection terminus Source: MGI
  8. plasma membrane Source: UniProtKB
  9. synapse Source: MGI
  10. synaptic vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 750749Neprilysin
PRO_0000078214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Disulfide bondi57 ↔ 62 By similarity
Disulfide bondi80 ↔ 735 By similarity
Disulfide bondi88 ↔ 695 By similarity
Disulfide bondi143 ↔ 411 By similarity
Glycosylationi145 – 1451N-linked (GlcNAc...)1 Publication
Glycosylationi211 – 2111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi234 ↔ 242 By similarity
Glycosylationi285 – 2851N-linked (GlcNAc...)1 Publication
Glycosylationi311 – 3111N-linked (GlcNAc...)1 Publication
Glycosylationi317 – 3171N-linked (GlcNAc...); atypical1 Publication
Glycosylationi325 – 3251N-linked (GlcNAc...) By similarity
Disulfide bondi621 ↔ 747 By similarity
Glycosylationi628 – 6281N-linked (GlcNAc...) By similarity

Post-translational modificationi

Myristoylation is a determinant of membrane targeting By similarity.
Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate

Proteomic databases

MaxQBiQ61391.
PaxDbiQ61391.
PRIDEiQ61391.

PTM databases

PhosphoSiteiQ61391.

Expressioni

Gene expression databases

ArrayExpressiQ61391.
BgeeiQ61391.
CleanExiMM_MME.
GenevestigatoriQ61391.

Interactioni

Protein-protein interaction databases

BioGridi201441. 2 interactions.
IntActiQ61391. 3 interactions.
MINTiMINT-4103332.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YVCX-ray3.20D/E/F2-23[»]
ProteinModelPortaliQ61391.
SMRiQ61391. Positions 55-750.

Miscellaneous databases

EvolutionaryTraceiQ61391.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 238Stop-transfer sequence Reviewed prediction

Sequence similaritiesi

Belongs to the peptidase M13 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3590.
GeneTreeiENSGT00650000093248.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiQ61391.
KOiK01389.
OMAiVWCGTYR.
OrthoDBiEOG7PZRWQ.
PhylomeDBiQ61391.
TreeFamiTF315192.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 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.

Q61391-1 [UniParc]FASTAAdd to Basket

« Hide

MGRSESQMDI TDINAPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA    50
TYDDGICKSS DCIKSAARLI QNMDASVEPC TDFFKYACGG WLKRNVIPET 100
SSRYSNFDIL RDELEVILKD VLQEPKTEDI VAVQKAKTLY RSCINESAID 150
SRGGQPLLKL LPDIYGWPVA SDNWDQTYGT SWTAEKSIAQ LNSKYGKKVL 200
INFFVGTDDK NSTQHIIHFD QPRLGLPSRD YYECTGIYKE ACTAYVDFMI 250
SVARLIRQEQ SLPIDENQLS LEMNKVMELE KEIANATTKP EDRNDPMLLY 300
NKMTLAKLQN NFSLEVNGKS FSWSNFTNEI MSTVNINIQN EEEVVVYAPE 350
YLTKLKPILT KYSPRDLQNL MSWRFIMDLV SSLSRNYKES RNAFRKALYG 400
TTSETATWRR CANYVNGNME NAVGRLYVEA AFAGESKHVV EDLIAQIREV 450
FIQTLDDLTW MDAETKKKAE EKALAIKERI GYPDDIISNE NKLNNEYLEL 500
NYREDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA VVNAFYSSGR 550
NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD 600
GDLVDWWTQQ SANNFKDQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA 650
DNGGIGQAYR AYQNYVKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP 700
EYAVNSIKTD VHSPGNFRII GTLQNSAEFA DAFHCRKNSY MNPERKCRVW 750
Length:750
Mass (Da):85,702
Last modified:January 23, 2007 - v3
Checksum:i1FC39A971D98F6FE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301D → G in AAA37386. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81591 mRNA. Translation: AAA37386.1.
AK031446 mRNA. Translation: BAC27410.1.
AK033824 mRNA. Translation: BAC28487.1.
BC034092 mRNA. Translation: AAH34092.1.
BC066840 mRNA. Translation: AAH66840.1.
CCDSiCCDS17381.1.
RefSeqiNP_001276391.1. NM_001289462.1.
NP_001276392.1. NM_001289463.1.
NP_032630.2. NM_008604.4.
XP_006501158.1. XM_006501095.1.
XP_006501161.1. XM_006501098.1.
XP_006501162.1. XM_006501099.1.
UniGeneiMm.296022.

Genome annotation databases

EnsembliENSMUST00000029400; ENSMUSP00000029400; ENSMUSG00000027820.
GeneIDi17380.
KEGGimmu:17380.
UCSCiuc008pjp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81591 mRNA. Translation: AAA37386.1 .
AK031446 mRNA. Translation: BAC27410.1 .
AK033824 mRNA. Translation: BAC28487.1 .
BC034092 mRNA. Translation: AAH34092.1 .
BC066840 mRNA. Translation: AAH66840.1 .
CCDSi CCDS17381.1.
RefSeqi NP_001276391.1. NM_001289462.1.
NP_001276392.1. NM_001289463.1.
NP_032630.2. NM_008604.4.
XP_006501158.1. XM_006501095.1.
XP_006501161.1. XM_006501098.1.
XP_006501162.1. XM_006501099.1.
UniGenei Mm.296022.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YVC X-ray 3.20 D/E/F 2-23 [» ]
ProteinModelPortali Q61391.
SMRi Q61391. Positions 55-750.
ModBasei Search...

Protein-protein interaction databases

BioGridi 201441. 2 interactions.
IntActi Q61391. 3 interactions.
MINTi MINT-4103332.

Chemistry

BindingDBi Q61391.
ChEMBLi CHEMBL2642.

Protein family/group databases

MEROPSi M13.001.

PTM databases

PhosphoSitei Q61391.

Proteomic databases

MaxQBi Q61391.
PaxDbi Q61391.
PRIDEi Q61391.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029400 ; ENSMUSP00000029400 ; ENSMUSG00000027820 .
GeneIDi 17380.
KEGGi mmu:17380.
UCSCi uc008pjp.1. mouse.

Organism-specific databases

CTDi 4311.
MGIi MGI:97004. Mme.

Phylogenomic databases

eggNOGi COG3590.
GeneTreei ENSGT00650000093248.
HOGENOMi HOG000245574.
HOVERGENi HBG005554.
InParanoidi Q61391.
KOi K01389.
OMAi VWCGTYR.
OrthoDBi EOG7PZRWQ.
PhylomeDBi Q61391.
TreeFami TF315192.

Enzyme and pathway databases

Reactomei REACT_196539. Metabolism of Angiotensinogen to Angiotensins.

Miscellaneous databases

EvolutionaryTracei Q61391.
NextBioi 291980.
PROi Q61391.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61391.
Bgeei Q61391.
CleanExi MM_MME.
Genevestigatori Q61391.

Family and domain databases

Gene3Di 3.40.390.10. 2 hits.
InterProi IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view ]
PANTHERi PTHR11733. PTHR11733. 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. "Murine common acute lymphoblastic leukemia antigen (CD10 neutral endopeptidase 24.11). Molecular characterization, chromosomal localization, and modeling of the active site."
    Chen C.Y., Salles G., Seldin M.F., Kister A.E., Reinher E.L., Shipp M.A.
    J. Immunol. 148:2817-2825(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Epididymis and Testis.
  3. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Embryonic germ cell and Mammary tumor.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 473-479, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145; ASN-285; ASN-311 AND ASN-317.
  6. "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.

Entry informationi

Entry nameiNEP_MOUSE
AccessioniPrimary (citable) accession number: Q61391
Secondary accession number(s): Q6NXX5, Q8K251
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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