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Q5RE69

- NEP_PONAB

UniProt

Q5RE69 - NEP_PONAB

Protein

Neprilysin

Gene

MME

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031Substrate carboxylBy similarity
    Metal bindingi584 – 5841Zinc; catalyticPROSITE-ProRule annotation
    Active sitei585 – 5851PROSITE-ProRule annotation
    Metal bindingi588 – 5881Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi647 – 6471Zinc; catalyticPROSITE-ProRule annotation
    Active sitei651 – 6511Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. beta-amyloid metabolic process Source: UniProtKB
    2. cellular response to cytokine stimulus Source: UniProtKB
    3. cellular response to UV-A Source: UniProtKB
    4. cellular response to UV-B 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

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Chromosome 3

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 750749NeprilysinPRO_0000319885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Disulfide bondi57 ↔ 62By similarity
    Disulfide bondi80 ↔ 735By similarity
    Disulfide bondi88 ↔ 695By similarity
    Disulfide bondi143 ↔ 411By similarity
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi234 ↔ 242By similarity
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi621 ↔ 747By similarity
    Glycosylationi628 – 6281N-linked (GlcNAc...)Sequence Analysis

    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

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RE69.
    SMRiQ5RE69. Positions 55-750.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    GeneTreeiENSGT00650000093248.
    HOGENOMiHOG000245574.
    HOVERGENiHBG005554.
    InParanoidiQ5R5K3.
    KOiK01389.
    OMAiVWCGTYR.
    OrthoDBiEOG7PZRWQ.
    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.

    Q5RE69-1 [UniParc]FASTAAdd to Basket

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    MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA    50
    TYDDGICKSS DCIKSAARLI QNMDATAEPC TDFFKYACGG WLKRNVIPET 100
    SSRYGNFDIL RDELEVVLKD VLQEPKTEDI VAVQKAKTLY RSCINESAID 150
    SRGGEPLLKL LPDVYGWPVA TENWEQKYGA SWTAEKAIAQ LNSKYGKKVL 200
    INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE ACTAYVDFMI 250
    SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY 300
    KKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE 350
    YLTKLKPILT KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG 400
    TTSETATWRR CANYVNGNME NAVGRLYVEA AFAGESKHVV EDLIAQIREV 450
    FIQTLDDLTW MDAETKKRAE EKALAIKERI GYPDDIVSND NKLNNEYLEL 500
    NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA VVNAFYSSGR 550
    NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD 600
    GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA 650
    DNGGLGQAYR AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP 700
    EYAVNSIKTD VHSPGNFRII GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW 750
    Length:750
    Mass (Da):85,514
    Last modified:February 26, 2008 - v2
    Checksum:iC4D1216E8361352F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151E → G in CAH89405. 1 PublicationCurated
    Sequence conflicti175 – 1751E → K in CAH89405. 1 PublicationCurated
    Sequence conflicti523 – 5231L → P in CAH89938. 1 PublicationCurated
    Sequence conflicti681 – 6811N → S in CAH92963. 1 PublicationCurated
    Sequence conflicti729 – 7291F → C in CAH92963. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857100 mRNA. Translation: CAH89405.1.
    CR857668 mRNA. Translation: CAH89938.1.
    CR860855 mRNA. Translation: CAH92963.1.
    RefSeqiNP_001126748.1. NM_001133276.1.

    Genome annotation databases

    EnsembliENSPPYT00000016535; ENSPPYP00000015904; ENSPPYG00000014224.
    GeneIDi100173750.
    KEGGipon:100173750.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857100 mRNA. Translation: CAH89405.1 .
    CR857668 mRNA. Translation: CAH89938.1 .
    CR860855 mRNA. Translation: CAH92963.1 .
    RefSeqi NP_001126748.1. NM_001133276.1.

    3D structure databases

    ProteinModelPortali Q5RE69.
    SMRi Q5RE69. Positions 55-750.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M13.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSPPYT00000016535 ; ENSPPYP00000015904 ; ENSPPYG00000014224 .
    GeneIDi 100173750.
    KEGGi pon:100173750.

    Organism-specific databases

    CTDi 4311.

    Phylogenomic databases

    GeneTreei ENSGT00650000093248.
    HOGENOMi HOG000245574.
    HOVERGENi HBG005554.
    InParanoidi Q5R5K3.
    KOi K01389.
    OMAi VWCGTYR.
    OrthoDBi EOG7PZRWQ.
    TreeFami TF315192.

    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

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

    Entry informationi

    Entry nameiNEP_PONAB
    AccessioniPrimary (citable) accession number: Q5RE69
    Secondary accession number(s): Q5R5K3, Q5RFQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 60 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3