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P42892 (ECE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endothelin-converting enzyme 1

Short name=ECE-1
EC=3.4.24.71
Gene names
Name:ECE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length770 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts big endothelin-1 to endothelin-1. Ref.11

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit. Ref.21

Enzyme regulation

Inhibited by phosphoramidon.

Subunit structure

Homodimer; disulfide-linked. Ref.21

Subcellular location

Cell membrane; Single-pass type II membrane protein.

Tissue specificity

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. Ref.10 Ref.11

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

Sequence similarities

Belongs to the peptidase M13 family.

Sequence caution

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

The sequence CAA84548.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hirschsprung disease
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbradykinin catabolic process

Inferred from direct assay PubMed 18039931. Source: BHF-UCL

calcitonin catabolic process

Inferred from direct assay PubMed 18039931. Source: BHF-UCL

ear development

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

embryonic digit morphogenesis

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

endothelin maturation

Inferred from direct assay Ref.12. Source: BHF-UCL

heart development

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

hormone catabolic process

Inferred from direct assay Ref.2. Source: BHF-UCL

peptide hormone processing

Inferred from direct assay Ref.2. Source: BHF-UCL

pharyngeal system development

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor recycling

Inferred from mutant phenotype PubMed 18039931. Source: BHF-UCL

protein processing

Inferred from direct assay Ref.12. Source: BHF-UCL

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of systemic arterial blood pressure by endothelin

Inferred by curator Ref.12. Source: BHF-UCL

regulation of vasoconstriction

Inferred by curator Ref.12. Source: BHF-UCL

substance P catabolic process

Inferred from direct assay PubMed 18039931. Source: BHF-UCL

   Cellular_componentWeibel-Palade body

Inferred from direct assay PubMed 9710124. Source: BHF-UCL

early endosome

Inferred from direct assay PubMed 18039931PubMed 18039931. Source: BHF-UCL

endosome

Inferred from direct assay PubMed 18039931. Source: BHF-UCL

external side of plasma membrane

Inferred from direct assay PubMed 9449382PubMed 9710124. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Inferred from direct assay Ref.12. Source: BHF-UCL

intrinsic component of endosome membrane

Traceable author statement PubMed 18039931. Source: BHF-UCL

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 9710124. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 18039931PubMed 18039931. Source: BHF-UCL

vesicle

Inferred from sequence or structural similarity PubMed 9449382. Source: BHF-UCL

   Molecular_functionendopeptidase activity

Inferred from direct assay PubMed 18039931Ref.12. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from sequence or structural similarity PubMed 8062389. Source: BHF-UCL

peptide hormone binding

Inferred by curator Ref.2. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction Ref.12. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P42892-1)

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.
Isoform A (identifier: P42892-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MRGVWPPPVS...LSEGDAYPNG → MPLQGLGLQRNPFLQGKRGPGLTSSPPLLPPS
Isoform C (identifier: P42892-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MRGVWPPPVSALLSALG → M
Isoform D (identifier: P42892-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 770770Endothelin-converting enzyme 1
PRO_0000078220

Regions

Topological domain1 – 6868Cytoplasmic Potential
Transmembrane69 – 8921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain90 – 770681Extracellular Potential

Sites

Active site6081
Active site6711Proton donor By similarity
Metal binding6071Zinc; catalytic
Metal binding6111Zinc; catalytic
Metal binding6671Zinc; catalytic

Amino acid modifications

Modified residue251Phosphothreonine Ref.19
Glycosylation1661N-linked (GlcNAc...) Ref.17 Ref.18
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Ref.15 Ref.17 Ref.18
Glycosylation2701N-linked (GlcNAc...) Ref.17
Glycosylation3161N-linked (GlcNAc...) Ref.17
Glycosylation3621N-linked (GlcNAc...) Ref.18
Glycosylation3831N-linked (GlcNAc...) Ref.18
Glycosylation5391N-linked (GlcNAc...) Potential
Glycosylation6321N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Disulfide bond428Interchain

Natural variations

Alternative sequence1 – 4444MRGVW…AYPNG → MPLQGLGLQRNPFLQGKRGP GLTSSPPLLPPS in isoform A.
VSP_005502
Alternative sequence1 – 1717MRGVW…LSALG → M in isoform C.
VSP_005504
Alternative sequence1 – 1717MRGVW…LSALG → MEALRESVLHLALQ in isoform D.
VSP_005503
Natural variant3411T → I. Ref.6
Corresponds to variant rs1076669 [ dbSNP | Ensembl ].
VAR_011972
Natural variant6301W → R.
Corresponds to variant rs2229451 [ dbSNP | Ensembl ].
VAR_054007
Natural variant7541R → C in HSCRCDAD. Ref.22
Corresponds to variant rs3026906 [ dbSNP | Ensembl ].
VAR_026747

Experimental info

Mutagenesis4281C → S: Abolishes dimerization. Ref.21

Secondary structure

................................................................................................ 770
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: DD88A59748B22F80

FASTA77087,164
        10         20         30         40         50         60 
MRGVWPPPVS ALLSALGMST YKRATLDEED LVDSLSEGDA YPNGLQVNFH SPRSGQRCWA 

        70         80         90        100        110        120 
ARTQVEKRLV VLVVLLAAGL VACLAALGIQ YQTRSPSVCL SEACVSVTSS ILSSMDPTVD 

       130        140        150        160        170        180 
PCHDFFSYAC GGWIKANPVP DGHSRWGTFS NLWEHNQAII KHLLENSTAS VSEAERKAQV 

       190        200        210        220        230        240 
YYRACMNETR IEELRAKPLM ELIERLGGWN ITGPWAKDNF QDTLQVVTAH YRTSPFFSVY 

       250        260        270        280        290        300 
VSADSKNSNS NVIQVDQSGL GLPSRDYYLN KTENEKVLTG YLNYMVQLGK LLGGGDEEAI 

       310        320        330        340        350        360 
RPQMQQILDF ETALANITIP QEKRRDEELI YHKVTAAELQ TLAPAINWLP FLNTIFYPVE 

       370        380        390        400        410        420 
INESEPIVVY DKEYLEQIST LINTTDRCLL NNYMIWNLVR KTSSFLDQRF QDADEKFMEV 

       430        440        450        460        470        480 
MYGTKKTCLP RWKFCVSDTE NNLGFALGPM FVKATFAEDS KSIATEIILE IKKAFEESLS 

       490        500        510        520        530        540 
TLKWMDEETR KSAKEKADAI YNMIGYPNFI MDPKELDKVF NDYTAVPDLY FENAMRFFNF 

       550        560        570        580        590        600 
SWRVTADQLR KAPNRDQWSM TPPMVNAYYS PTKNEIVFPA GILQAPFYTR SSPKALNFGG 

       610        620        630        640        650        660 
IGVVVGHELT HAFDDQGREY DKDGNLRPWW KNSSVEAFKR QTECMVEQYS NYSVNGEPVN 

       670        680        690        700        710        720 
GRHTLGENIA DNGGLKAAYR AYQNWVKKNG AEHSLPTLGL TNNQLFFLGF AQVWCSVRTP 

       730        740        750        760        770 
ESSHEGLITD PHSPSRFRVI GSLSNSKEFS EHFRCPPGSP MNPPHKCEVW 

« Hide

Isoform A [UniParc].

Checksum: 4768314E789DFF96
Show »

FASTA75885,808
Isoform C [UniParc].

Checksum: A16E45032B03029D
Show »

FASTA75485,562
Isoform D [UniParc].

Checksum: 09B58AF5A63882F4
Show »

FASTA76787,022

References

« Hide 'large scale' references
[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]"Cloning and functional expression of human endothelin-converting enzyme cDNA."
Shimada K., Matsushita Y., Wakabayashi K., Takahashi M., Matsubara A., Iijima Y., Tanzawa K.
Biochem. Biophys. Res. Commun. 207:807-812(1995) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49471 mRNA. Translation: BAA08442.1.
D43698 mRNA. Translation: BAA07800.1.
X91922 expand/collapse EMBL AC list , X91923, X91924, X91925, X91926, X91927, X91928, X91929, X91930, X91931, X91932, X91933, X91934, X91935, X91936, X91937, X91938, X91939 Genomic DNA. Translation: CAA63015.1.
X91923 expand/collapse EMBL AC list , 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.
PIRJC2521.
JC4136.
RefSeqNP_001106818.1. NM_001113347.1.
NP_001106819.1. NM_001113348.1.
NP_001106820.1. NM_001113349.1.
NP_001388.1. NM_001397.2.
UniGeneHs.195080.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWBX-ray2.38A101-770[»]
ProteinModelPortalP42892.
SMRP42892. Positions 101-770.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108218. 16 interactions.
IntActP42892. 3 interactions.

Chemistry

BindingDBP42892.
ChEMBLCHEMBL4791.
GuidetoPHARMACOLOGY1615.

Protein family/group databases

MEROPSM13.002.

PTM databases

PhosphoSiteP42892.

Polymorphism databases

DMDM1706563.

Proteomic databases

PaxDbP42892.
PRIDEP42892.

Protocols and materials databases

DNASU1889.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264205; ENSP00000264205; ENSG00000117298. [P42892-4]
ENST00000357071; ENSP00000349581; ENSG00000117298. [P42892-2]
ENST00000374893; ENSP00000364028; ENSG00000117298. [P42892-1]
ENST00000415912; ENSP00000405088; ENSG00000117298. [P42892-3]
GeneID1889.
KEGGhsa:1889.
UCSCuc001bei.2. human. [P42892-4]
uc001bej.2. human. [P42892-2]
uc001bek.2. human. [P42892-1]
uc001bem.2. human. [P42892-3]

Organism-specific databases

CTD1889.
GeneCardsGC01M021543.
H-InvDBHIX0159964.
HGNCHGNC:3146. ECE1.
HPAHPA001490.
HPA013616.
MIM600423. gene.
613870. phenotype.
neXtProtNX_P42892.
Orphanet388. Hirschsprung disease.
PharmGKBPA27594.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3590.
HOVERGENHBG005554.
InParanoidP42892.
KOK01415.
OMAMYGTKKS.
OrthoDBEOG7PZRWQ.
PhylomeDBP42892.
TreeFamTF315192.

Gene expression databases

ArrayExpressP42892.
BgeeP42892.
GenevestigatorP42892.

Family and domain databases

Gene3D3.40.390.10. 2 hits.
InterProIPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERPTHR11733. PTHR11733. 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...

Other

ChiTaRSECE1. human.
EvolutionaryTraceP42892.
GeneWikiEndothelin_converting_enzyme_1.
GenomeRNAi1889.
NextBio7703.
PROP42892.
SOURCESearch...

Entry information

Entry nameECE1_HUMAN
AccessionPrimary (citable) accession number: P42892
Secondary accession number(s): A8K3P1 expand/collapse secondary AC list , B4E291, Q14217, Q17RN5, Q2Z2K8, Q58GE7, Q5THM5, Q5THM7, Q5THM8, Q9UJQ6, Q9UPF4, Q9UPM4, Q9Y501
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM