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Protein

Neprilysin

Gene

MME

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (PubMed:15283675, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675). Involved in the degradation of atrial natriuretic factor (ANF) (PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573).5 Publications

Catalytic activityi

Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.2 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Enzyme regulationi

Inhibited in a dose dependent manner by opiorphin.1 Publication

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)DescriptionActionsGraphical viewLength
    Binding sitei103Substrate carboxylBy similarity1
    Metal bindingi584Zinc; catalytic1
    Active sitei5851
    Metal bindingi588Zinc; catalytic1
    Metal bindingi647Zinc; catalytic1
    Active sitei651Proton donorPROSITE-ProRule annotation1 Publication1

    GO - Molecular functioni

    • endopeptidase activity Source: UniProtKB
    • exopeptidase activity Source: BHF-UCL
    • metalloendopeptidase activity Source: UniProtKB
    • metallopeptidase activity Source: Reactome
    • peptide binding Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • angiotensin maturation Source: Reactome
    • beta-amyloid metabolic process Source: UniProtKB
    • cellular response to cytokine stimulus Source: UniProtKB
    • cellular response to UV-A Source: UniProtKB
    • cellular response to UV-B Source: UniProtKB
    • creatinine metabolic process Source: UniProtKB
    • kidney development Source: UniProtKB
    • peptide metabolic process Source: UniProtKB
    • proteolysis Source: UniProtKB
    • replicative senescence Source: UniProtKB
    • sensory perception of pain Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciZFISH:HS03802-MONOMER.
    BRENDAi3.4.24.11. 2681.
    ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
    R-HSA-6798695. Neutrophil degranulation.
    SIGNORiP08473.

    Protein family/group databases

    MEROPSiM13.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neprilysin (EC:3.4.24.112 Publications)
    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:7154. MME.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini2 – 28CytoplasmicSequence analysisAdd BLAST27
    Transmembranei29 – 51Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
    Topological domaini52 – 750ExtracellularSequence analysisAdd BLAST699

    GO - Cellular componenti

    • axon Source: UniProtKB
    • brush border Source: UniProtKB
    • cytoplasm Source: UniProtKB
    • dendrite Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • focal adhesion Source: UniProtKB
    • integral component of membrane Source: UniProtKB
    • integral component of plasma membrane Source: UniProtKB
    • neuron projection terminus Source: UniProtKB
    • plasma membrane Source: UniProtKB
    • synapse Source: UniProtKB
    • synaptic vesicle Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi4311.
    MalaCardsiMME.
    OpenTargetsiENSG00000196549.
    PharmGKBiPA30864.

    Chemistry databases

    ChEMBLiCHEMBL1944.
    DrugBankiDB00616. Candoxatril.
    DB06655. Liraglutide.
    DB09292. Sacubitril.
    GuidetoPHARMACOLOGYi1611.

    Polymorphism and mutation databases

    BioMutaiMME.
    DMDMi128062.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00000782132 – 750NeprilysinAdd BLAST749

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Lipidationi2N-myristoyl glycine1 Publication1
    Modified residuei4PhosphoserineCombined sources1
    Modified residuei6PhosphoserineCombined sources1
    Disulfide bondi57 ↔ 62
    Disulfide bondi80 ↔ 735
    Disulfide bondi88 ↔ 695
    Disulfide bondi143 ↔ 411
    Glycosylationi145N-linked (GlcNAc...)4 Publications1
    Disulfide bondi234 ↔ 242
    Glycosylationi285N-linked (GlcNAc...)1 Publication1
    Glycosylationi325N-linked (GlcNAc...)3 Publications1
    Disulfide bondi621 ↔ 747
    Glycosylationi628N-linked (GlcNAc...)4 Publications1

    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, Phosphoprotein

    Proteomic databases

    EPDiP08473.
    MaxQBiP08473.
    PaxDbiP08473.
    PeptideAtlasiP08473.
    PRIDEiP08473.

    PTM databases

    iPTMnetiP08473.
    PhosphoSitePlusiP08473.

    Expressioni

    Gene expression databases

    BgeeiENSG00000196549.
    CleanExiHS_MME.
    ExpressionAtlasiP08473. baseline and differential.
    GenevisibleiP08473. HS.

    Organism-specific databases

    HPAiCAB000013.
    HPA052583.
    HPA056072.

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi110455. 96 interactors.
    IntActiP08473. 80 interactors.
    STRINGi9606.ENSP00000353679.

    Chemistry databases

    BindingDBiP08473.

    Structurei

    Secondary structure

    1750
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi60 – 72Combined sources13
    Turni79 – 81Combined sources3
    Helixi83 – 94Combined sources12
    Beta strandi102 – 105Combined sources4
    Helixi106 – 122Combined sources17
    Helixi131 – 144Combined sources14
    Helixi146 – 151Combined sources6
    Turni152 – 154Combined sources3
    Helixi155 – 158Combined sources4
    Helixi161 – 164Combined sources4
    Helixi168 – 170Combined sources3
    Beta strandi171 – 173Combined sources3
    Helixi174 – 177Combined sources4
    Turni178 – 181Combined sources4
    Helixi184 – 195Combined sources12
    Beta strandi200 – 208Combined sources9
    Beta strandi211 – 220Combined sources10
    Beta strandi225 – 228Combined sources4
    Helixi229 – 233Combined sources5
    Helixi236 – 238Combined sources3
    Helixi239 – 259Combined sources21
    Helixi266 – 286Combined sources21
    Helixi290 – 292Combined sources3
    Helixi296 – 299Combined sources4
    Beta strandi302 – 304Combined sources3
    Helixi305 – 311Combined sources7
    Beta strandi316 – 319Combined sources4
    Helixi323 – 331Combined sources9
    Helixi332 – 334Combined sources3
    Beta strandi343 – 347Combined sources5
    Helixi349 – 359Combined sources11
    Helixi364 – 379Combined sources16
    Helixi380 – 382Combined sources3
    Helixi385 – 389Combined sources5
    Helixi392 – 399Combined sources8
    Helixi407 – 418Combined sources12
    Helixi420 – 431Combined sources12
    Helixi436 – 454Combined sources19
    Helixi455 – 457Combined sources3
    Beta strandi459 – 461Combined sources3
    Helixi463 – 474Combined sources12
    Beta strandi477 – 481Combined sources5
    Helixi485 – 488Combined sources4
    Helixi490 – 496Combined sources7
    Turni497 – 499Combined sources3
    Helixi507 – 523Combined sources17
    Turni524 – 527Combined sources4
    Beta strandi545 – 547Combined sources3
    Turni548 – 551Combined sources4
    Beta strandi552 – 556Combined sources5
    Helixi557 – 559Combined sources3
    Turni562 – 564Combined sources3
    Beta strandi567 – 569Combined sources3
    Helixi571 – 576Combined sources6
    Helixi578 – 587Combined sources10
    Helixi588 – 590Combined sources3
    Turni592 – 595Combined sources4
    Helixi609 – 627Combined sources19
    Helixi632 – 634Combined sources3
    Beta strandi636 – 638Combined sources3
    Turni641 – 644Combined sources4
    Helixi645 – 669Combined sources25
    Helixi682 – 692Combined sources11
    Beta strandi696 – 698Combined sources3
    Helixi700 – 709Combined sources10
    Helixi715 – 724Combined sources10
    Helixi727 – 732Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5JMYX-ray2.00A/B53-750[»]
    ProteinModelPortaliP08473.
    SMRiP08473.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08473.

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi16 – 23Stop-transfer sequenceSequence analysis8

    Sequence similaritiesi

    Belongs to the peptidase M13 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG3624. Eukaryota.
    COG3590. LUCA.
    GeneTreeiENSGT00760000119162.
    HOGENOMiHOG000245574.
    HOVERGENiHBG005554.
    InParanoidiP08473.
    KOiK01389.
    OMAiKLSKFTY.
    OrthoDBiEOG091G025Y.
    PhylomeDBiP08473.
    TreeFamiTF315192.

    Family and domain databases

    CDDicd08662. M13. 1 hit.
    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 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti26P → R in AAA51915 (PubMed:14702039).Curated1
    Sequence conflicti44T → R in AAA51915 (PubMed:14702039).Curated1
    Sequence conflicti81T → R in AAA51915 (PubMed:14702039).Curated1
    Sequence conflicti304T → R in AAA51915 (PubMed:14702039).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_006713646.3.
    XP_006713710.1. XM_006713647.3.
    XP_011511157.1. XM_011512855.2.
    XP_011511158.1. XM_011512856.2.
    XP_011511159.1. XM_011512857.2.
    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.2. human.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_006713646.3.
    XP_006713710.1. XM_006713647.3.
    XP_011511157.1. XM_011512855.2.
    XP_011511158.1. XM_011512856.2.
    XP_011511159.1. XM_011512857.2.
    UniGeneiHs.307734.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5JMYX-ray2.00A/B53-750[»]
    ProteinModelPortaliP08473.
    SMRiP08473.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110455. 96 interactors.
    IntActiP08473. 80 interactors.
    STRINGi9606.ENSP00000353679.

    Chemistry databases

    BindingDBiP08473.
    ChEMBLiCHEMBL1944.
    DrugBankiDB00616. Candoxatril.
    DB06655. Liraglutide.
    DB09292. Sacubitril.
    GuidetoPHARMACOLOGYi1611.

    Protein family/group databases

    MEROPSiM13.001.

    PTM databases

    iPTMnetiP08473.
    PhosphoSitePlusiP08473.

    Polymorphism and mutation databases

    BioMutaiMME.
    DMDMi128062.

    Proteomic databases

    EPDiP08473.
    MaxQBiP08473.
    PaxDbiP08473.
    PeptideAtlasiP08473.
    PRIDEiP08473.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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.2. human.

    Organism-specific databases

    CTDi4311.
    DisGeNETi4311.
    GeneCardsiMME.
    HGNCiHGNC:7154. MME.
    HPAiCAB000013.
    HPA052583.
    HPA056072.
    MalaCardsiMME.
    MIMi120520. gene.
    neXtProtiNX_P08473.
    OpenTargetsiENSG00000196549.
    PharmGKBiPA30864.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3624. Eukaryota.
    COG3590. LUCA.
    GeneTreeiENSGT00760000119162.
    HOGENOMiHOG000245574.
    HOVERGENiHBG005554.
    InParanoidiP08473.
    KOiK01389.
    OMAiKLSKFTY.
    OrthoDBiEOG091G025Y.
    PhylomeDBiP08473.
    TreeFamiTF315192.

    Enzyme and pathway databases

    BioCyciZFISH:HS03802-MONOMER.
    BRENDAi3.4.24.11. 2681.
    ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
    R-HSA-6798695. Neutrophil degranulation.
    SIGNORiP08473.

    Miscellaneous databases

    ChiTaRSiMME. human.
    EvolutionaryTraceiP08473.
    GeneWikiiNeprilysin.
    GenomeRNAii4311.
    PROiP08473.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000196549.
    CleanExiHS_MME.
    ExpressionAtlasiP08473. baseline and differential.
    GenevisibleiP08473. HS.

    Family and domain databases

    CDDicd08662. M13. 1 hit.
    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]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 204 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.