Q95161 · Q95161_CANLF

Function

function

Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • H2O + Leu-enkephalin = L-phenylalanyl-L-leucine + L-tyrosylglycylglycine
    This reaction proceeds in the forward direction.
  • H2O + Met-enkephalin = L-phenylalanyl-L-methionine + L-tyrosylglycylglycine
    This reaction proceeds in the forward direction.
  • H2O + Met-enkephalin-Arg-Phe = L-arginyl-L-phenylalanine + Met-enkephalin
    This reaction proceeds in the forward direction.
  • H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11)
    This reaction proceeds in the forward direction.
  • H2O + substance P = Gly-L-Leu-L-Met-NH2 + substance P(1-8)
    This reaction proceeds in the forward direction.
  • H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9)
    This reaction proceeds in the forward direction.
  • H2O + substance P = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-6)
    This reaction proceeds in the forward direction.
  • Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.
    EC:3.4.15.1 (UniProtKB | ENZYME | Rhea)
  • angiotensin I + H2O = angiotensin II + L-histidyl-L-leucine
    This reaction proceeds in the forward direction.
    EC:3.4.15.1 (UniProtKB | ENZYME | Rhea)
  • bradykinin + H2O = bradykinin(1-7) + L-Phe-L-Arg
    This reaction proceeds in the forward direction.
  • goralatide + H2O = L-lysyl-L-proline + N-acetyl-L-seryl-L-aspartate
    This reaction proceeds in the forward direction.

Cofactor

Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

chloride (UniProtKB | Rhea| CHEBI:17996 )

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentextracellular region
Cellular Componentmembrane
Molecular Functionmetallopeptidase activity
Molecular Functionpeptidyl-dipeptidase activity
Biological Processproteolysis

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Angiotensin-converting enzyme
  • EC number
  • Alternative names
    • Dipeptidyl carboxypeptidase I
    • Kininase II

Organism names

Accessions

  • Primary accession
    Q95161

Subcellular Location

Cytoplasm
Membrane
; Single-pass type I membrane protein
Secreted

PTM/Processing

Keywords

Family & Domains

Sequence similarities

Belongs to the peptidase M2 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    54
  • Mass (Da)
    6,318
  • Last updated
    1997-02-01 v1
  • Checksum
    B31B5DFADF45E367
ALHRRYGDRYINLRGPIPAHLLGDMWAQSWDNLYDMMVPFPDKPSLDVTSTMVR

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue54

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U67199
EMBL· GenBank· DDBJ
AAC48637.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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