Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target for design of specific inhibitors | Mus musculus |
drug development | the enzyme is a target for design of specific inhibitors | Homo sapiens |
drug development | the enzyme is a target for design of specific inhibitors | Rattus norvegicus |
drug development | the enzyme is a target for design of specific inhibitors | Sus scrofa |
Cloned (Comment) | Organism |
---|---|
gene APA, DNA and amino acid sequence determination and analysis | Homo sapiens |
gene APA, DNA and amino acid sequence determination and analysis | Rattus norvegicus |
gene APA, DNA and amino acid sequence determination and analysis | Sus scrofa |
gene APA, DNA and amino acid sequence determination and analysis, genetic organization and structure | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of active site residue mutants | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
amastatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Homo sapiens | |
amastatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Mus musculus | |
amastatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Rattus norvegicus | |
amastatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Sus scrofa | |
bestatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Homo sapiens | |
bestatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Mus musculus | |
bestatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Rattus norvegicus | |
bestatin | inhibits the enzyme and blocks the metabolism of brain angiotensin II and III | Sus scrofa | |
Ca2+ | substrate-specific inhibition, overview | Homo sapiens | |
Ca2+ | substrate-specific inhibition, overview | Mus musculus | |
Ca2+ | substrate-specific inhibition, overview | Rattus norvegicus | |
Ca2+ | substrate-specific inhibition, overview | Sus scrofa | |
Cd2+ | - |
Homo sapiens | |
Cd2+ | - |
Mus musculus | |
Cd2+ | - |
Rattus norvegicus | |
Cd2+ | - |
Sus scrofa | |
Cu2+ | - |
Homo sapiens | |
Cu2+ | - |
Mus musculus | |
Cu2+ | - |
Rattus norvegicus | |
Cu2+ | - |
Sus scrofa | |
EC33 | highly selective APA inhibitor | Homo sapiens | |
EC33 | highly selective APA inhibitor | Mus musculus | |
EC33 | highly selective APA inhibitor | Rattus norvegicus | |
EC33 | highly selective APA inhibitor | Sus scrofa | |
Hg2+ | - |
Homo sapiens | |
Hg2+ | - |
Mus musculus | |
Hg2+ | - |
Rattus norvegicus | |
Hg2+ | - |
Sus scrofa | |
Ni2+ | - |
Homo sapiens | |
Ni2+ | - |
Mus musculus | |
Ni2+ | - |
Rattus norvegicus | |
Ni2+ | - |
Sus scrofa | |
Zn2+ | - |
Homo sapiens | |
Zn2+ | - |
Mus musculus | |
Zn2+ | - |
Rattus norvegicus | |
Zn2+ | - |
Sus scrofa |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | bound, type II integral membrane protein, the enzyme contains an ectodomain | Mus musculus | 16020 | - |
membrane | bound, type II integral membrane protein, the enzyme contains an ectodomain | Homo sapiens | 16020 | - |
membrane | bound, type II integral membrane protein, the enzyme contains an ectodomain | Rattus norvegicus | 16020 | - |
membrane | bound, type II integral membrane protein, the enzyme contains an ectodomain | Sus scrofa | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates, best at 1 mM, substrate-specific activation | Mus musculus | |
Ca2+ | activates, best at 1 mM, substrate-specific activation | Homo sapiens | |
Ca2+ | activates, best at 1 mM, substrate-specific activation | Rattus norvegicus | |
Ca2+ | activates, best at 1 mM, substrate-specific activation | Sus scrofa | |
Zn2+ | zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH | Homo sapiens | |
Zn2+ | zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH | Rattus norvegicus | |
Zn2+ | zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH | Sus scrofa | |
Zn2+ | zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH residues 385-389 with catalytically important Glu386 | Mus musculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
250000 | 300000 | - |
Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
angiotensin III + H2O | Mus musculus | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | angiotensin IV + Arg | - |
ir | |
angiotensin III + H2O | Homo sapiens | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | angiotensin IV + Arg | - |
ir | |
angiotensin III + H2O | Rattus norvegicus | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | angiotensin IV + Arg | - |
ir | |
angiotensin III + H2O | Sus scrofa | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | angiotensin IV + Arg | - |
ir | |
additional information | Mus musculus | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | ? | - |
? | |
additional information | Homo sapiens | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | ? | - |
? | |
additional information | Rattus norvegicus | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | ? | - |
? | |
additional information | Sus scrofa | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Rattus norvegicus | - |
WKY rats | - |
Sus scrofa | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | N-linked glycans | Mus musculus |
glycoprotein | N-linked glycans | Homo sapiens |
glycoprotein | N-linked glycans | Rattus norvegicus |
glycoprotein | N-linked glycans | Sus scrofa |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide | active site structure and organization | Homo sapiens | |
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide | active site structure and organization | Rattus norvegicus | |
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide | active site structure and organization | Sus scrofa | |
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide | active site structure and organization, modeling, residues Glu352, Glu386, Tyr471, and Glu408 are important in catalysis | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
adrenal gland | - |
Homo sapiens | - |
B-lymphocyte | immature B-lineage cell | Mus musculus | - |
B-lymphocyte | immature B-lineage cell | Homo sapiens | - |
B-lymphocyte | immature B-lineage cell | Rattus norvegicus | - |
B-lymphocyte | immature B-lineage cell | Sus scrofa | - |
bile duct | - |
Homo sapiens | - |
bone marrow | - |
Mus musculus | - |
bone marrow | - |
Homo sapiens | - |
bone marrow | - |
Rattus norvegicus | - |
bone marrow | - |
Sus scrofa | - |
brain | pericyte | Mus musculus | - |
brain | pericyte | Homo sapiens | - |
brain | pericyte | Rattus norvegicus | - |
brain | pericyte | Sus scrofa | - |
brain | pericyte and almost all structures, hyperactive in RAS and SHR, distribution overview | Rattus norvegicus | - |
epididymis | basement membrane | Homo sapiens | - |
epithelium | - |
Homo sapiens | - |
gall bladder epithelium | - |
Homo sapiens | - |
heart | - |
Homo sapiens | - |
hepatocyte | - |
Homo sapiens | - |
liver | bile canaliculi | Homo sapiens | - |
lung | - |
Homo sapiens | - |
ovary | theca interna | Homo sapiens | - |
pancreas | interlobular ducts | Homo sapiens | - |
pericyte | brain | Mus musculus | - |
pericyte | brain | Homo sapiens | - |
pericyte | brain | Rattus norvegicus | - |
pericyte | brain | Sus scrofa | - |
placenta | syncytiotrophoblast cells | Homo sapiens | - |
syncytiotrophoblast | - |
Homo sapiens | - |
thymus | stromal cells of the cortex | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
angiotensin I + H2O | cleavage only in vitro | Mus musculus | ? | - |
? | |
angiotensin I + H2O | cleavage only in vitro | Homo sapiens | ? | - |
? | |
angiotensin I + H2O | cleavage only in vitro | Rattus norvegicus | ? | - |
? | |
angiotensin I + H2O | cleavage only in vitro | Sus scrofa | ? | - |
? | |
angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Mus musculus | Asp + angiotensin III | i.e. Arg-Val-Tyr-Ile-His-Pro-Phe | ir | |
angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Homo sapiens | Asp + angiotensin III | i.e. Arg-Val-Tyr-Ile-His-Pro-Phe | ir | |
angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Rattus norvegicus | Asp + angiotensin III | i.e. Arg-Val-Tyr-Ile-His-Pro-Phe | ir | |
angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Sus scrofa | Asp + angiotensin III | i.e. Arg-Val-Tyr-Ile-His-Pro-Phe | ir | |
angiotensin III + H2O | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | Mus musculus | angiotensin IV + Arg | - |
ir | |
angiotensin III + H2O | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | Homo sapiens | angiotensin IV + Arg | - |
ir | |
angiotensin III + H2O | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | Rattus norvegicus | angiotensin IV + Arg | - |
ir | |
angiotensin III + H2O | the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension | Sus scrofa | angiotensin IV + Arg | - |
ir | |
cholecystokinin-8 + H2O | cleavage only in vitro | Mus musculus | ? | - |
? | |
cholecystokinin-8 + H2O | cleavage only in vitro | Homo sapiens | ? | - |
? | |
cholecystokinin-8 + H2O | cleavage only in vitro | Rattus norvegicus | ? | - |
? | |
cholecystokinin-8 + H2O | cleavage only in vitro | Sus scrofa | ? | - |
? | |
additional information | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | Mus musculus | ? | - |
? | |
additional information | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | Homo sapiens | ? | - |
? | |
additional information | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | Rattus norvegicus | ? | - |
? | |
additional information | the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview | Sus scrofa | ? | - |
? | |
additional information | substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides | Mus musculus | ? | - |
? | |
additional information | substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides | Homo sapiens | ? | - |
? | |
additional information | substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides | Rattus norvegicus | ? | - |
? | |
additional information | substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides | Sus scrofa | ? | - |
? | |
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O | - |
Mus musculus | ? | - |
? | |
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O | - |
Homo sapiens | ? | - |
? | |
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O | - |
Rattus norvegicus | ? | - |
? | |
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O | - |
Sus scrofa | ? | - |
? | |
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O | - |
Mus musculus | L-aspartic acid + 2-naphthylamine | - |
? | |
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O | - |
Homo sapiens | L-aspartic acid + 2-naphthylamine | - |
? | |
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O | - |
Rattus norvegicus | L-aspartic acid + 2-naphthylamine | - |
? | |
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O | - |
Sus scrofa | L-aspartic acid + 2-naphthylamine | - |
? | |
N-(alpha-L-glutamyl)-2-naphthylamide + H2O | - |
Mus musculus | L-glutamic acid + 2-naphthylamine | - |
? | |
N-(alpha-L-glutamyl)-2-naphthylamide + H2O | - |
Homo sapiens | L-glutamic acid + 2-naphthylamine | - |
? | |
N-(alpha-L-glutamyl)-2-naphthylamide + H2O | - |
Rattus norvegicus | L-glutamic acid + 2-naphthylamine | - |
? | |
N-(alpha-L-glutamyl)-2-naphthylamide + H2O | - |
Sus scrofa | L-glutamic acid + 2-naphthylamine | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 120000-185000, SDS-PAGE | Mus musculus |
dimer | 2 * 120000-185000, SDS-PAGE | Homo sapiens |
dimer | 2 * 120000-185000, SDS-PAGE | Sus scrofa |
dimer | three-dimensional structure determination and analysis, modeling | Rattus norvegicus |
monomer | three-dimensional structure determination and analysis, modeling | Rattus norvegicus |
More | three-dimensional structure determination and analysis, modeling | Homo sapiens |
More | three-dimensional structure determination and analysis, modeling | Sus scrofa |
More | three-dimensional structure determination and analysis, modeling, the enzyme contains a short N-terminal cytoplasmic domain of 17 amino acid residues, a transmembrane domain of 22 amino acid residues, and a large extracellular domain of 906 amino acid residues in cluding the active and the zinc-binding site | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
aminopeptidase A | - |
Mus musculus |
aminopeptidase A | - |
Homo sapiens |
aminopeptidase A | - |
Rattus norvegicus |
aminopeptidase A | - |
Sus scrofa |
APA | - |
Mus musculus |
APA | - |
Homo sapiens |
APA | - |
Rattus norvegicus |
APA | - |
Sus scrofa |
BP1/6C3 | - |
Mus musculus |
BP1/6C3 | - |
Homo sapiens |
BP1/6C3 | - |
Rattus norvegicus |
BP1/6C3 | - |
Sus scrofa |
More | the enzyme belongs to the zinc-metallopeptidase family of zincins | Mus musculus |
More | the enzyme belongs to the zinc-metallopeptidase family of zincins | Homo sapiens |
More | the enzyme belongs to the zinc-metallopeptidase family of zincins | Rattus norvegicus |
More | the enzyme belongs to the zinc-metallopeptidase family of zincins | Sus scrofa |