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Protein

Endothelin-converting enzyme 1

Gene

ECE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Zn2+1 PublicationNote: 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6868CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei69 – 8921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini90 – 770681ExtracellularSequence AnalysisAdd
BLAST

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: UniProtKB
  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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Hirschsprung disease cardiac defects and autonomic dysfunction1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613870
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

BgeeiP42892.
ExpressionAtlasiP42892. baseline and differential.
GenevestigatoriP42892.

Organism-specific databases

HPAiHPA001490.
HPA013616.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi108218. 20 interactions.
IntActiP42892. 3 interactions.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP42892.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3590.
GeneTreeiENSGT00760000119162.
HOVERGENiHBG005554.
InParanoidiP42892.
KOiK01415.
OMAiLQVNFHS.
OrthoDBiEOG7PZRWQ.
PhylomeDBiP42892.
TreeFamiTF315192.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR029734. ECE1.
IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF104. PTHR11733:SF104. 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

        10         20         30         40         50
MRGVWPPPVS ALLSALGMST YKRATLDEED LVDSLSEGDA YPNGLQVNFH
60 70 80 90 100
SPRSGQRCWA ARTQVEKRLV VLVVLLAAGL VACLAALGIQ YQTRSPSVCL
110 120 130 140 150
SEACVSVTSS ILSSMDPTVD PCHDFFSYAC GGWIKANPVP DGHSRWGTFS
160 170 180 190 200
NLWEHNQAII KHLLENSTAS VSEAERKAQV YYRACMNETR IEELRAKPLM
210 220 230 240 250
ELIERLGGWN ITGPWAKDNF QDTLQVVTAH YRTSPFFSVY VSADSKNSNS
260 270 280 290 300
NVIQVDQSGL GLPSRDYYLN KTENEKVLTG YLNYMVQLGK LLGGGDEEAI
310 320 330 340 350
RPQMQQILDF ETALANITIP QEKRRDEELI YHKVTAAELQ TLAPAINWLP
360 370 380 390 400
FLNTIFYPVE INESEPIVVY DKEYLEQIST LINTTDRCLL NNYMIWNLVR
410 420 430 440 450
KTSSFLDQRF QDADEKFMEV MYGTKKTCLP RWKFCVSDTE NNLGFALGPM
460 470 480 490 500
FVKATFAEDS KSIATEIILE IKKAFEESLS TLKWMDEETR KSAKEKADAI
510 520 530 540 550
YNMIGYPNFI MDPKELDKVF NDYTAVPDLY FENAMRFFNF SWRVTADQLR
560 570 580 590 600
KAPNRDQWSM TPPMVNAYYS PTKNEIVFPA GILQAPFYTR SSPKALNFGG
610 620 630 640 650
IGVVVGHELT HAFDDQGREY DKDGNLRPWW KNSSVEAFKR QTECMVEQYS
660 670 680 690 700
NYSVNGEPVN GRHTLGENIA DNGGLKAAYR AYQNWVKKNG AEHSLPTLGL
710 720 730 740 750
TNNQLFFLGF AQVWCSVRTP ESSHEGLITD PHSPSRFRVI GSLSNSKEFS
760 770
EHFRCPPGSP MNPPHKCEVW
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 AAX35820.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA84548.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi108218. 20 interactions.
IntActiP42892. 3 interactions.

Chemistry

BindingDBiP42892.
ChEMBLiCHEMBL4791.
GuidetoPHARMACOLOGYi1615.

Protein family/group databases

MEROPSiM13.002.

PTM databases

PhosphoSiteiP42892.

Polymorphism databases

DMDMi1706563.

Proteomic databases

MaxQBiP42892.
PaxDbiP42892.
PRIDEiP42892.

Protocols and materials databases

DNASUi1889.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi1889.
GeneCardsiGC01M021543.
GeneReviewsiECE1.
H-InvDBHIX0159964.
HGNCiHGNC:3146. ECE1.
HPAiHPA001490.
HPA013616.
MIMi600423. gene.
613870. phenotype.
neXtProtiNX_P42892.
Orphaneti388. Hirschsprung disease.
PharmGKBiPA27594.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3590.
GeneTreeiENSGT00760000119162.
HOVERGENiHBG005554.
InParanoidiP42892.
KOiK01415.
OMAiLQVNFHS.
OrthoDBiEOG7PZRWQ.
PhylomeDBiP42892.
TreeFamiTF315192.

Miscellaneous databases

ChiTaRSiECE1. human.
EvolutionaryTraceiP42892.
GeneWikiiEndothelin_converting_enzyme_1.
GenomeRNAii1889.
NextBioi7703.
PROiP42892.
SOURCEiSearch...

Gene expression databases

BgeeiP42892.
ExpressionAtlasiP42892. baseline and differential.
GenevestigatoriP42892.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR029734. ECE1.
IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF104. PTHR11733:SF104. 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...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 154 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

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 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.