P42892 · ECE1_HUMAN
- ProteinEndothelin-converting enzyme 1
- GeneECE1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids770 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
Cofactor
Activity regulation
Activated by K49-P1-20, a twenty-residue synthetic peptide shortened from the snake B.asper myotoxin II (PubMed:26931059).
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEndothelin-converting enzyme 1
- EC number
- Short namesECE-1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP42892
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-68 | Cytoplasmic | ||||
Sequence: MRGVWPPPVSALLSALGMSTYKRATLDEEDLVDSLSEGDAYPNGLQVNFHSPRSGQRCWAARTQVEKR | ||||||
Transmembrane | 69-89 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LVVLVVLLAAGLVACLAALGI | ||||||
Topological domain | 90-770 | Extracellular | ||||
Sequence: QYQTRSPSVCLSEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Hirschsprung disease, cardiac defects, and autonomic dysfunction (HCAD)
- Note
- 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 alsoMIM:613870
Natural variants in HCAD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_026747 | 754 | R>C | in HCAD; dbSNP:rs3026906 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_011972 | 341 | in dbSNP:rs1076669 | |||
Sequence: T → I | ||||||
Mutagenesis | 428 | Abolishes dimerization. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_026747 | 754 | in HCAD; dbSNP:rs3026906 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 718 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), disulfide bond, glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000078220 | 1-770 | UniProt | Endothelin-converting enzyme 1 | |||
Sequence: MRGVWPPPVSALLSALGMSTYKRATLDEEDLVDSLSEGDAYPNGLQVNFHSPRSGQRCWAARTQVEKRLVVLVVLLAAGLVACLAALGIQYQTRSPSVCLSEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW | |||||||
Modified residue | 25 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 99↔104 | UniProt | |||||
Sequence: CLSEAC | |||||||
Disulfide bond | 122↔755 | UniProt | |||||
Sequence: CHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRC | |||||||
Disulfide bond | 130↔715 | UniProt | |||||
Sequence: CGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWC | |||||||
Glycosylation | 166 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 185↔435 | UniProt | |||||
Sequence: CMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFC | |||||||
Glycosylation | 187 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 210 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 270 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 316 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 362 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 383 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 539 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 632 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 644↔767 | UniProt | |||||
Sequence: CMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKC | |||||||
Glycosylation | 651 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PPP1R16B (By similarity).
Interacts with TSPAN8; this interaction recruits the endothelin converting enzyme ECE1 to tetraspanin-enriched microdomains and positively modulates its enzymatic activity (PubMed:37835445).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P42892 | CLK2 P49760 | 6 | EBI-2859983, EBI-750020 | |
BINARY | P42892 | CYSRT1 A8MQ03 | 3 | EBI-2859983, EBI-3867333 | |
BINARY | P42892 | KRTAP1-3 Q8IUG1 | 3 | EBI-2859983, EBI-11749135 | |
BINARY | P42892 | KRTAP10-5 P60370 | 3 | EBI-2859983, EBI-10172150 | |
BINARY | P42892 | KRTAP10-8 P60410 | 3 | EBI-2859983, EBI-10171774 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 98-770 | Peptidase M13 | ||||
Sequence: VCLSEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
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.
- NameB
- Length770
- Mass (Da)87,164
- Last updated1996-10-01 v2
- ChecksumDD88A59748B22F80
P42892-2
- NameA
- Differences from canonical
- 1-44: MRGVWPPPVSALLSALGMSTYKRATLDEEDLVDSLSEGDAYPNG → MPLQGLGLQRNPFLQGKRGPGLTSSPPLLPPS
P42892-3
- NameC
- Differences from canonical
- 1-17: MRGVWPPPVSALLSALG → M
P42892-4
- NameD
- Differences from canonical
- 1-17: MRGVWPPPVSALLSALG → MEALRESVLHLALQ
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B4DKB2 | B4DKB2_HUMAN | ECE1 | 738 | ||
E9PN99 | E9PN99_HUMAN | ECE1 | 103 | ||
E9PJG1 | E9PJG1_HUMAN | ECE1 | 77 | ||
E9PHZ1 | E9PHZ1_HUMAN | ECE1 | 134 | ||
A0A3B3ISF9 | A0A3B3ISF9_HUMAN | ECE1 | 842 |
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_005504 | 1-17 | in isoform C | |||
Sequence: MRGVWPPPVSALLSALG → M | ||||||
Alternative sequence | VSP_005503 | 1-17 | in isoform D | |||
Sequence: MRGVWPPPVSALLSALG → MEALRESVLHLALQ | ||||||
Alternative sequence | VSP_005502 | 1-44 | in isoform A | |||
Sequence: MRGVWPPPVSALLSALGMSTYKRATLDEEDLVDSLSEGDAYPNG → MPLQGLGLQRNPFLQGKRGPGLTSSPPLLPPS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D49471 EMBL· GenBank· DDBJ | BAA08442.1 EMBL· GenBank· DDBJ | mRNA | ||
D43698 EMBL· GenBank· DDBJ | BAA07800.1 EMBL· GenBank· DDBJ | mRNA | ||
X91922 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91923 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91924 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91925 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91926 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91927 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91928 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91929 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91930 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91931 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91932 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91933 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91934 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91935 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91936 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91937 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91938 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91939 EMBL· GenBank· DDBJ | CAA63015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91923 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91924 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91925 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91926 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91927 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91928 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91929 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91930 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91931 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91932 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91933 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91934 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91935 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91936 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91937 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91938 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91939 EMBL· GenBank· DDBJ | CAA63016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB031742 EMBL· GenBank· DDBJ | BAA83687.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290656 EMBL· GenBank· DDBJ | BAF83345.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304167 EMBL· GenBank· DDBJ | BAG65053.1 EMBL· GenBank· DDBJ | mRNA | ||
AY953519 EMBL· GenBank· DDBJ | AAX35820.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL031005 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL031728 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471134 EMBL· GenBank· DDBJ | EAW94959.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471134 EMBL· GenBank· DDBJ | EAW94964.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC117256 EMBL· GenBank· DDBJ | AAI17257.1 EMBL· GenBank· DDBJ | mRNA | ||
BC126257 EMBL· GenBank· DDBJ | AAI26258.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ130828 EMBL· GenBank· DDBJ | CAB46443.1 EMBL· GenBank· DDBJ | mRNA | ||
X98272 EMBL· GenBank· DDBJ | CAA66922.1 EMBL· GenBank· DDBJ | mRNA | ||
Z35307 EMBL· GenBank· DDBJ | CAA84548.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF018034 EMBL· GenBank· DDBJ | AAD21221.1 EMBL· GenBank· DDBJ | Genomic DNA |