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Reviewed, UniProtKB/Swiss-Prot Q5RE69 (NEP_PONAB)

Last modified November 3, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Neprilysin
    EC=3.4.24.11
Alternative name(s):
    Neutral endopeptidase 24.11
      Short name=Neutral endopeptidase
      Short name=NEP
    Enkephalinase
    Atriopeptidase
    CD_antigen=CD10
Gene names
Name: MME
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

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 By similarity. Involved in the degradation of atrial natriuretic factor (ANF) By similarity.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cell membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the peptidase M13 family.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal-anchor
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 750749Neprilysin
PRO_0000319885

Regions

Topological domain2 – 2827Cytoplasmic Potential
Transmembrane29 – 5123Signal-anchor for type II membrane protein Potential
Topological domain52 – 750699Extracellular Potential
Motif16 – 238Stop-transfer sequence Potential

Sites

Active site5851 By similarity
Active site6511Proton donor By similarity
Metal binding5841Zinc; catalytic By similarity
Metal binding5881Zinc; catalytic By similarity
Metal binding6471Zinc; catalytic By similarity
Binding site1031Substrate carboxyl By similarity

Amino acid modifications

Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation6281N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 62 By similarity
Disulfide bond80 ↔ 735 By similarity
Disulfide bond88 ↔ 695 By similarity
Disulfide bond143 ↔ 411 By similarity
Disulfide bond234 ↔ 242 By similarity
Disulfide bond621 ↔ 747 By similarity

Experimental info

Sequence conflict1151E → G in CAH89405. Ref.1
Sequence conflict1751E → K in CAH89405. Ref.1
Sequence conflict5231L → P in CAH89938. Ref.1
Sequence conflict6811N → S in CAH92963. Ref.1
Sequence conflict7291F → C in CAH92963. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q5RE69-1 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: C4D1216E8361352F

FASTA75085,514
        10         20         30         40         50         60 
MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS 

        70         80         90        100        110        120 
DCIKSAARLI QNMDATAEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD 

       130        140        150        160        170        180 
VLQEPKTEDI VAVQKAKTLY RSCINESAID SRGGEPLLKL LPDVYGWPVA TENWEQKYGA 

       190        200        210        220        230        240 
SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE 

       250        260        270        280        290        300 
ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY 

       310        320        330        340        350        360 
KKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT 

       370        380        390        400        410        420 
KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME 

       430        440        450        460        470        480 
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI 

       490        500        510        520        530        540 
GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA 

       550        560        570        580        590        600 
VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD 

       610        620        630        640        650        660 
GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR 

       670        680        690        700        710        720 
AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII 

       730        740        750 
GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW

« Hide

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

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Cross-references

Sequence databases

CR857100 mRNA. Translation: CAH89405.1.
CR857668 mRNA. Translation: CAH89938.1.
CR860855 mRNA. Translation: CAH92963.1.
RefSeqNP_001126748.1.
UniGenePab.18628

3D structure databases

SMRQ5RE69. Positions 55-750.
ModBaseSearch...

Protein family/group databases

MEROPSM13.001.

Genome annotation databases

GeneID100173750.

Organism-specific databases

CTD100173750.

Phylogenomic databases

HOVERGENQ5RE69.
OMAGRNQIVF.

Enzyme and pathway databases

BRENDA3.4.24.11. 269192.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERPTHR11733. Peptidase_M13. 1 hit.
PfamPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSPR00786. NEPRILYSIN.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameNEP_PONAB
AccessionPrimary (citable) accession number: Q5RE69
Secondary accession number(s): Q5R5K3, Q5RFQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: November 3, 2009
This is version 27 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents