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P42892

- ECE1_HUMAN

UniProt

P42892 - ECE1_HUMAN

Protein

Endothelin-converting enzyme 1

Gene

ECE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Converts big endothelin-1 to endothelin-1.1 Publication

    Catalytic activityi

    Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Enzyme regulationi

    Inhibited by phosphoramidon.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi607 – 6071Zinc; catalytic
    Active sitei608 – 6081
    Metal bindingi611 – 6111Zinc; catalytic
    Metal bindingi667 – 6671Zinc; catalytic
    Active sitei671 – 6711Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. endopeptidase activity Source: BHF-UCL
    2. metal ion binding Source: UniProtKB-KW
    3. metalloendopeptidase activity Source: BHF-UCL
    4. peptide hormone binding Source: BHF-UCL
    5. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. bradykinin catabolic process Source: BHF-UCL
    2. calcitonin catabolic process Source: BHF-UCL
    3. ear development Source: BHF-UCL
    4. embryonic digit morphogenesis Source: BHF-UCL
    5. endothelin maturation Source: BHF-UCL
    6. heart development Source: BHF-UCL
    7. hormone catabolic process Source: BHF-UCL
    8. peptide hormone processing Source: BHF-UCL
    9. pharyngeal system development Source: Ensembl
    10. positive regulation of receptor recycling Source: BHF-UCL
    11. protein processing Source: BHF-UCL
    12. regulation of systemic arterial blood pressure by endothelin Source: BHF-UCL
    13. regulation of vasoconstriction Source: BHF-UCL
    14. substance P catabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM13.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endothelin-converting enzyme 1 (EC:3.4.24.71)
    Short name:
    ECE-1
    Gene namesi
    Name:ECE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3146. ECE1.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome Source: BHF-UCL
    2. endosome Source: BHF-UCL
    3. external side of plasma membrane Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of membrane Source: BHF-UCL
    6. intrinsic component of endosome membrane Source: BHF-UCL
    7. lysosomal membrane Source: UniProtKB
    8. membrane Source: UniProtKB
    9. perinuclear region of cytoplasm Source: BHF-UCL
    10. plasma membrane Source: BHF-UCL
    11. vesicle Source: BHF-UCL
    12. Weibel-Palade body Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Hirschsprung disease cardiac defects and autonomic dysfunction (HSCRCDAD) [MIM:613870]: A disorder characterized by skip-lesions Hirschsprung disease, craniofacial abnormalities and other dysmorphic features, cardiac defects including ductus arteriosus, small subaortic ventricular septal defect, small atrial septal defect, and autonomic dysfunction.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti754 – 7541R → C in HSCRCDAD. 1 Publication
    Corresponds to variant rs3026906 [ dbSNP | Ensembl ].
    VAR_026747

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi428 – 4281C → S: Abolishes dimerization. 1 Publication

    Keywords - Diseasei

    Disease mutation, Hirschsprung disease

    Organism-specific databases

    MIMi613870. phenotype.
    Orphaneti388. Hirschsprung disease.
    PharmGKBiPA27594.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 770770Endothelin-converting enzyme 1PRO_0000078220Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Phosphothreonine1 Publication
    Glycosylationi166 – 1661N-linked (GlcNAc...)2 Publications
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi210 – 2101N-linked (GlcNAc...)3 Publications
    Glycosylationi270 – 2701N-linked (GlcNAc...)1 Publication
    Glycosylationi316 – 3161N-linked (GlcNAc...)1 Publication
    Glycosylationi362 – 3621N-linked (GlcNAc...)1 Publication
    Glycosylationi383 – 3831N-linked (GlcNAc...)1 Publication
    Disulfide bondi428 – 428Interchain
    Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi632 – 6321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP42892.
    PaxDbiP42892.
    PRIDEiP42892.

    PTM databases

    PhosphoSiteiP42892.

    Expressioni

    Tissue specificityi

    All isoforms are expressed in umbilical vein endothelial cells, polynuclear neutrophils, fibroblasts, atrium cardiomyocytes and ventricles. Isoforms A, B and C are also expressed in placenta, lung, heart, adrenal gland and phaeochromocytoma; isoforms A and C in liver, testis and small intestine; isoform B, C and D in endothelial cells and umbilical vein smooth muscle cells; isoforms C and D in saphenous vein cells, and isoform C in kidney.2 Publications

    Gene expression databases

    ArrayExpressiP42892.
    BgeeiP42892.
    GenevestigatoriP42892.

    Organism-specific databases

    HPAiHPA001490.
    HPA013616.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 Publication

    Protein-protein interaction databases

    BioGridi108218. 16 interactions.
    IntActiP42892. 3 interactions.

    Structurei

    Secondary structure

    1
    770
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi102 – 11413
    Turni121 – 1233
    Helixi125 – 13612
    Beta strandi144 – 1474
    Helixi148 – 16417
    Helixi173 – 18614
    Helixi189 – 1946
    Helixi197 – 2059
    Helixi220 – 22910
    Beta strandi235 – 24410
    Beta strandi247 – 25610
    Beta strandi261 – 2644
    Helixi266 – 2694
    Turni270 – 2734
    Helixi277 – 29115
    Helixi297 – 31721
    Helixi321 – 3244
    Helixi327 – 3304
    Beta strandi332 – 3354
    Helixi336 – 3427
    Helixi348 – 3558
    Beta strandi366 – 3705
    Helixi372 – 38413
    Helixi387 – 40216
    Helixi403 – 4053
    Helixi408 – 41811
    Helixi434 – 45522
    Helixi458 – 47922
    Helixi487 – 49913
    Beta strandi501 – 5066
    Helixi508 – 5114
    Helixi513 – 5208
    Helixi530 – 54617
    Turni547 – 5504
    Beta strandi568 – 5703
    Turni571 – 5744
    Beta strandi575 – 5795
    Helixi580 – 5823
    Turni585 – 5873
    Helixi594 – 5996
    Helixi601 – 61111
    Helixi617 – 6193
    Helixi632 – 64918
    Beta strandi653 – 6586
    Turni661 – 6644
    Helixi665 – 68925
    Beta strandi696 – 6983
    Helixi702 – 71312
    Beta strandi716 – 7183
    Helixi720 – 72910
    Helixi735 – 74410
    Helixi747 – 7537

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DWBX-ray2.38A101-770[»]
    ProteinModelPortaliP42892.
    SMRiP42892. Positions 101-770.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42892.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6868CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini90 – 770681ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei69 – 8921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M13 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3590.
    HOVERGENiHBG005554.
    InParanoidiP42892.
    KOiK01415.
    OMAiQVVTAHY.
    OrthoDBiEOG7PZRWQ.
    PhylomeDBiP42892.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: P42892-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRGVWPPPVS ALLSALGMST YKRATLDEED LVDSLSEGDA YPNGLQVNFH    50
    SPRSGQRCWA ARTQVEKRLV VLVVLLAAGL VACLAALGIQ YQTRSPSVCL 100
    SEACVSVTSS ILSSMDPTVD PCHDFFSYAC GGWIKANPVP DGHSRWGTFS 150
    NLWEHNQAII KHLLENSTAS VSEAERKAQV YYRACMNETR IEELRAKPLM 200
    ELIERLGGWN ITGPWAKDNF QDTLQVVTAH YRTSPFFSVY VSADSKNSNS 250
    NVIQVDQSGL GLPSRDYYLN KTENEKVLTG YLNYMVQLGK LLGGGDEEAI 300
    RPQMQQILDF ETALANITIP QEKRRDEELI YHKVTAAELQ TLAPAINWLP 350
    FLNTIFYPVE INESEPIVVY DKEYLEQIST LINTTDRCLL NNYMIWNLVR 400
    KTSSFLDQRF QDADEKFMEV MYGTKKTCLP RWKFCVSDTE NNLGFALGPM 450
    FVKATFAEDS KSIATEIILE IKKAFEESLS TLKWMDEETR KSAKEKADAI 500
    YNMIGYPNFI MDPKELDKVF NDYTAVPDLY FENAMRFFNF SWRVTADQLR 550
    KAPNRDQWSM TPPMVNAYYS PTKNEIVFPA GILQAPFYTR SSPKALNFGG 600
    IGVVVGHELT HAFDDQGREY DKDGNLRPWW KNSSVEAFKR QTECMVEQYS 650
    NYSVNGEPVN GRHTLGENIA DNGGLKAAYR AYQNWVKKNG AEHSLPTLGL 700
    TNNQLFFLGF AQVWCSVRTP ESSHEGLITD PHSPSRFRVI GSLSNSKEFS 750
    EHFRCPPGSP MNPPHKCEVW 770
    Length:770
    Mass (Da):87,164
    Last modified:October 1, 1996 - v2
    Checksum:iDD88A59748B22F80
    GO
    Isoform A (identifier: P42892-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: MRGVWPPPVS...LSEGDAYPNG → MPLQGLGLQRNPFLQGKRGPGLTSSPPLLPPS

    Show »
    Length:758
    Mass (Da):85,808
    Checksum:i4768314E789DFF96
    GO
    Isoform C (identifier: P42892-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MRGVWPPPVSALLSALG → M

    Show »
    Length:754
    Mass (Da):85,562
    Checksum:iA16E45032B03029D
    GO
    Isoform D (identifier: P42892-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MRGVWPPPVSALLSALG → MEALRESVLHLALQ

    Show »
    Length:767
    Mass (Da):87,022
    Checksum:i09B58AF5A63882F4
    GO

    Sequence cautioni

    The sequence CAA84548.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAX35820.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti341 – 3411T → I.1 Publication
    Corresponds to variant rs1076669 [ dbSNP | Ensembl ].
    VAR_011972
    Natural varianti630 – 6301W → R.
    Corresponds to variant rs2229451 [ dbSNP | Ensembl ].
    VAR_054007
    Natural varianti754 – 7541R → C in HSCRCDAD. 1 Publication
    Corresponds to variant rs3026906 [ dbSNP | Ensembl ].
    VAR_026747

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444MRGVW…AYPNG → MPLQGLGLQRNPFLQGKRGP GLTSSPPLLPPS in isoform A. 2 PublicationsVSP_005502Add
    BLAST
    Alternative sequencei1 – 1717MRGVW…LSALG → M in isoform C. 2 PublicationsVSP_005504Add
    BLAST
    Alternative sequencei1 – 1717MRGVW…LSALG → MEALRESVLHLALQ in isoform D. 1 PublicationVSP_005503Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49471 mRNA. Translation: BAA08442.1.
    D43698 mRNA. Translation: BAA07800.1.
    X91922
    , X91923, X91924, X91925, X91926, X91927, X91928, X91929, X91930, X91931, X91932, X91933, X91934, X91935, X91936, X91937, X91938, X91939 Genomic DNA. Translation: CAA63015.1.
    X91923
    , X91924, X91925, X91926, X91927, X91928, X91929, X91930, X91931, X91932, X91933, X91934, X91935, X91936, X91937, X91938, X91939 Genomic DNA. Translation: CAA63016.1.
    AB031742 mRNA. Translation: BAA83687.1.
    AK290656 mRNA. Translation: BAF83345.1.
    AK304167 mRNA. Translation: BAG65053.1.
    AY953519 Genomic DNA. Translation: AAX35820.1. Sequence problems.
    AL031005 Genomic DNA. Translation: CAI20195.1.
    AL031005, AL031728 Genomic DNA. Translation: CAI20192.1.
    AL031005, AL031728 Genomic DNA. Translation: CAI20194.1.
    AL031728 Genomic DNA. Translation: CAB52285.2.
    AL031728, AL031005 Genomic DNA. Translation: CAI19064.1.
    CH471134 Genomic DNA. Translation: EAW94959.1.
    CH471134 Genomic DNA. Translation: EAW94964.1.
    BC117256 mRNA. Translation: AAI17257.1.
    BC126257 mRNA. Translation: AAI26258.1.
    AJ130828 mRNA. Translation: CAB46443.1.
    X98272 mRNA. Translation: CAA66922.1.
    Z35307 mRNA. Translation: CAA84548.1. Different initiation.
    AF018034 Genomic DNA. Translation: AAD21221.1.
    CCDSiCCDS215.1. [P42892-1]
    CCDS44081.1. [P42892-3]
    CCDS44082.1. [P42892-4]
    CCDS44083.1. [P42892-2]
    PIRiJC2521.
    JC4136.
    RefSeqiNP_001106818.1. NM_001113347.1. [P42892-2]
    NP_001106819.1. NM_001113348.1. [P42892-3]
    NP_001106820.1. NM_001113349.1. [P42892-4]
    NP_001388.1. NM_001397.2. [P42892-1]
    XP_006710461.1. XM_006710398.1.
    UniGeneiHs.195080.

    Genome annotation databases

    EnsembliENST00000264205; ENSP00000264205; ENSG00000117298. [P42892-4]
    ENST00000357071; ENSP00000349581; ENSG00000117298. [P42892-2]
    ENST00000374893; ENSP00000364028; ENSG00000117298. [P42892-1]
    ENST00000415912; ENSP00000405088; ENSG00000117298. [P42892-3]
    GeneIDi1889.
    KEGGihsa:1889.
    UCSCiuc001bei.2. human. [P42892-4]
    uc001bej.2. human. [P42892-2]
    uc001bek.2. human. [P42892-1]
    uc001bem.2. human. [P42892-3]

    Polymorphism databases

    DMDMi1706563.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49471 mRNA. Translation: BAA08442.1 .
    D43698 mRNA. Translation: BAA07800.1 .
    X91922
    , X91923 , X91924 , X91925 , X91926 , X91927 , X91928 , X91929 , X91930 , X91931 , X91932 , X91933 , X91934 , X91935 , X91936 , X91937 , X91938 , X91939 Genomic DNA. Translation: CAA63015.1 .
    X91923
    , X91924 , X91925 , X91926 , X91927 , X91928 , X91929 , X91930 , X91931 , X91932 , X91933 , X91934 , X91935 , X91936 , X91937 , X91938 , X91939 Genomic DNA. Translation: CAA63016.1 .
    AB031742 mRNA. Translation: BAA83687.1 .
    AK290656 mRNA. Translation: BAF83345.1 .
    AK304167 mRNA. Translation: BAG65053.1 .
    AY953519 Genomic DNA. Translation: AAX35820.1 . Sequence problems.
    AL031005 Genomic DNA. Translation: CAI20195.1 .
    AL031005 , AL031728 Genomic DNA. Translation: CAI20192.1 .
    AL031005 , AL031728 Genomic DNA. Translation: CAI20194.1 .
    AL031728 Genomic DNA. Translation: CAB52285.2 .
    AL031728 , AL031005 Genomic DNA. Translation: CAI19064.1 .
    CH471134 Genomic DNA. Translation: EAW94959.1 .
    CH471134 Genomic DNA. Translation: EAW94964.1 .
    BC117256 mRNA. Translation: AAI17257.1 .
    BC126257 mRNA. Translation: AAI26258.1 .
    AJ130828 mRNA. Translation: CAB46443.1 .
    X98272 mRNA. Translation: CAA66922.1 .
    Z35307 mRNA. Translation: CAA84548.1 . Different initiation.
    AF018034 Genomic DNA. Translation: AAD21221.1 .
    CCDSi CCDS215.1. [P42892-1 ]
    CCDS44081.1. [P42892-3 ]
    CCDS44082.1. [P42892-4 ]
    CCDS44083.1. [P42892-2 ]
    PIRi JC2521.
    JC4136.
    RefSeqi NP_001106818.1. NM_001113347.1. [P42892-2 ]
    NP_001106819.1. NM_001113348.1. [P42892-3 ]
    NP_001106820.1. NM_001113349.1. [P42892-4 ]
    NP_001388.1. NM_001397.2. [P42892-1 ]
    XP_006710461.1. XM_006710398.1.
    UniGenei Hs.195080.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DWB X-ray 2.38 A 101-770 [» ]
    ProteinModelPortali P42892.
    SMRi P42892. Positions 101-770.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108218. 16 interactions.
    IntActi P42892. 3 interactions.

    Chemistry

    BindingDBi P42892.
    ChEMBLi CHEMBL4791.
    GuidetoPHARMACOLOGYi 1615.

    Protein family/group databases

    MEROPSi M13.002.

    PTM databases

    PhosphoSitei P42892.

    Polymorphism databases

    DMDMi 1706563.

    Proteomic databases

    MaxQBi P42892.
    PaxDbi P42892.
    PRIDEi P42892.

    Protocols and materials databases

    DNASUi 1889.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264205 ; ENSP00000264205 ; ENSG00000117298 . [P42892-4 ]
    ENST00000357071 ; ENSP00000349581 ; ENSG00000117298 . [P42892-2 ]
    ENST00000374893 ; ENSP00000364028 ; ENSG00000117298 . [P42892-1 ]
    ENST00000415912 ; ENSP00000405088 ; ENSG00000117298 . [P42892-3 ]
    GeneIDi 1889.
    KEGGi hsa:1889.
    UCSCi uc001bei.2. human. [P42892-4 ]
    uc001bej.2. human. [P42892-2 ]
    uc001bek.2. human. [P42892-1 ]
    uc001bem.2. human. [P42892-3 ]

    Organism-specific databases

    CTDi 1889.
    GeneCardsi GC01M021543.
    GeneReviewsi ECE1.
    H-InvDB HIX0159964.
    HGNCi HGNC:3146. ECE1.
    HPAi HPA001490.
    HPA013616.
    MIMi 600423. gene.
    613870. phenotype.
    neXtProti NX_P42892.
    Orphaneti 388. Hirschsprung disease.
    PharmGKBi PA27594.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3590.
    HOVERGENi HBG005554.
    InParanoidi P42892.
    KOi K01415.
    OMAi QVVTAHY.
    OrthoDBi EOG7PZRWQ.
    PhylomeDBi P42892.
    TreeFami TF315192.

    Miscellaneous databases

    ChiTaRSi ECE1. human.
    EvolutionaryTracei P42892.
    GeneWikii Endothelin_converting_enzyme_1.
    GenomeRNAii 1889.
    NextBioi 7703.
    PROi P42892.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42892.
    Bgeei P42892.
    Genevestigatori P42892.

    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. "Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2."
      Yorimitsu K., Moroi K., Inagaki N., Saito T., Masuda Y., Masaki T., Seino S., Kimura S.
      Biochem. Biophys. Res. Commun. 208:721-727(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    3. "Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)."
      Valdenaire O., Rohrbacher E., Mattei M.-G.
      J. Biol. Chem. 270:29794-29798(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
      Tissue: Placenta.
    4. "Human endothelin-converting enzyme-1c."
      Takayanagi R.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
      Tissue: Umbilical vein endothelial cell.
    5. "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] (ISOFORM B).
      Tissue: Trachea.
    6. NIEHS SNPs program
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-341.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM A).
      Tissue: Brain.
    10. "A fourth isoform of endothelin-converting enzyme (ECE-1) is generated from an additional promoter."
      Valdenaire O., Lepailleur-Enouf D., Egidy G., Thouard A., Barret A., Vranckx R., Tougard C., Michel J.-B.
      Eur. J. Biochem. 264:341-349(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-132 (ISOFORM D), TISSUE SPECIFICITY.
    11. "Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations."
      Schweizer A., Valdenaire O., Nelboeck P., Deuschle U., Dumas Milne Edwards J.B., Stumpf J.G., Loeffler B.-M.
      Biochem. J. 328:871-877(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM C), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Umbilical vein endothelial cell.
    12. "Molecular characterization of human and bovine endothelin converting enzyme (ECE-1)."
      Schmidt M., Kroeger B., Jacob E., Seulberger H., Subkowski T., Otter R., Meyer T., Schmalzing G., Hillen H.
      FEBS Lett. 356:238-243(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-770 (ISOFORM B).
      Tissue: Placenta.
    13. "Characterization of the human endothelin converting enzyme-1 gene (ECE-1): genomic structure and chromosomal localization."
      Flowers M.A., Tai S.C., Baluyut C.A., Cheung A.H., Kau C.L., Wong G.K.T., Marsden P.A.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 713-770.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210.
      Tissue: Platelet.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-210; ASN-270 AND ASN-316.
      Tissue: Liver.
    18. "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-166; ASN-210; ASN-362 AND ASN-383.
      Tissue: Leukemic T-cell.
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Structure of human endothelin-converting enzyme I complexed with phosphoramidon."
      Schulz H., Dale G.E., Karimi-Nejad Y., Oefner C.
      J. Mol. Biol. 385:178-187(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 101-770 OF MUTANT SER-428 IN COMPLEX WITH ZINC IONS AND PHOSPHORAMIDON, COFACTOR, SUBUNIT, MUTAGENESIS OF CYS-428.
    22. "A loss-of-function mutation in the endothelin-converting enzyme 1 (ECE-1) associated with Hirschsprung disease, cardiac defects, and autonomic dysfunction."
      Hofstra R.M.W., Valdenaire O., Arch E., Osinga J., Kroes H., Loffler B.-M., Hamosh A., Meijers C., Buys C.H.C.M.
      Am. J. Hum. Genet. 64:304-308(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HSCRCDAD CYS-754.

    Entry informationi

    Entry nameiECE1_HUMAN
    AccessioniPrimary (citable) accession number: P42892
    Secondary accession number(s): A8K3P1
    , B4E291, Q14217, Q17RN5, Q2Z2K8, Q58GE7, Q5THM5, Q5THM7, Q5THM8, Q9UJQ6, Q9UPF4, Q9UPM4, Q9Y501
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3