| IED ID | IndEnz0002016534 |
| Enzyme Type ID | protease016534 |
| Protein Name |
Angiotensin-converting enzyme 2 EC 3.4.17.23 Angiotensin-converting enzyme homolog ACEH Angiotensin-converting enzyme-related carboxypeptidase ACE-related carboxypeptidase EC 3.4.17.- Metalloprotease MPROT15 Cleaved into: Processed angiotensin-converting enzyme 2 |
| Gene Name | ACE2 UNQ868/PRO1885 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF |
| Enzyme Length | 805 |
| Uniprot Accession Number | Q9BYF1 |
| Absorption | |
| Active Site | ACT_SITE 375; /note="Proton acceptor"; /evidence="ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402"; ACT_SITE 505; /note="Proton donor"; /evidence="ECO:0000305|PubMed:14754895" |
| Activity Regulation | ACTIVITY REGULATION: Regulated by chloride and fluoride, but not bromide (PubMed:11815627). Chloride increases angiotensin I and decreases angiotensin II cleavage (PubMed:19021774). Inhibited by MLN-4760, cFP_Leu, and EDTA (PubMed:15231706, PubMed:10924499), but not by the ACE inhibitors lisinopril, captopril and enalaprilat (PubMed:10969042, PubMed:10924499). Highly potent and selective in vitro ACE2 inhibitors were identified (PubMed:12358520). {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:12358520, ECO:0000269|PubMed:15231706, ECO:0000269|PubMed:19021774}. |
| Binding Site | BINDING 169; /note="Chloride"; /evidence="ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774"; BINDING 273; /note="Substrate"; /evidence="ECO:0000305|PubMed:14754895"; BINDING 477; /note="Chloride"; /evidence="ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774"; BINDING 481; /note="Chloride"; /evidence="ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774"; BINDING 515; /note="Substrate"; /evidence="ECO:0000305|PubMed:14754895" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine; Xref=Rhea:RHEA:26554, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:58506, ChEBI:CHEBI:58922; EC=3.4.17.23; Evidence={ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:19021774, ECO:0000305|PubMed:14504186};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26555; Evidence={ECO:0000269|PubMed:14504186}; CATALYTIC ACTIVITY: Reaction=angiotensin I + H2O = angiotensin-(1-9) + L-leucine; Xref=Rhea:RHEA:63532, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427, ChEBI:CHEBI:147350, ChEBI:CHEBI:147351; Evidence={ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:19021774};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63533; Evidence={ECO:0000305|PubMed:10924499, ECO:0000305|PubMed:10969042, ECO:0000305|PubMed:11815627, ECO:0000305|PubMed:19021774}; CATALYTIC ACTIVITY: Reaction=[des-Arg(9)]-bradykinin + H2O = [des-Phe(8), des-Arg(9)]-bradykinin + L-phenylalanine; Xref=Rhea:RHEA:63536, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:133069, ChEBI:CHEBI:147352; Evidence={ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63537; Evidence={ECO:0000305|PubMed:10969042, ECO:0000305|PubMed:11815627}; CATALYTIC ACTIVITY: Reaction=H2O + neurotensin = L-leucine + neurotensin-(1-12); Xref=Rhea:RHEA:63540, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427, ChEBI:CHEBI:147362, ChEBI:CHEBI:147363; Evidence={ECO:0000269|PubMed:10969042};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63541; Evidence={ECO:0000305|PubMed:10969042}; CATALYTIC ACTIVITY: Reaction=H2O + neurotensin-(1-8) = L-arginine + neurotensin-(1-7); Xref=Rhea:RHEA:63572, ChEBI:CHEBI:15377, ChEBI:CHEBI:32682, ChEBI:CHEBI:147393, ChEBI:CHEBI:147394; Evidence={ECO:0000269|PubMed:11815627};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63573; Evidence={ECO:0000305|PubMed:11815627}; CATALYTIC ACTIVITY: Reaction=H2O + kinetensin = kinetensin-(1-8) + L-leucine; Xref=Rhea:RHEA:63544, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427, ChEBI:CHEBI:147364, ChEBI:CHEBI:147365; Evidence={ECO:0000269|PubMed:10969042};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63545; Evidence={ECO:0000305|PubMed:10969042}; CATALYTIC ACTIVITY: Reaction=dynorphin A-(1-13) + H2O = dynorphin A-(1-12) + L-lysine; Xref=Rhea:RHEA:63556, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:147381, ChEBI:CHEBI:147383; Evidence={ECO:0000269|PubMed:11815627};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63557; Evidence={ECO:0000305|PubMed:11815627}; CATALYTIC ACTIVITY: Reaction=apelin-13 + H2O = apelin-12 + L-phenylalanine; Xref=Rhea:RHEA:63564, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:147395, ChEBI:CHEBI:147396; Evidence={ECO:0000269|PubMed:11815627};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63565; Evidence={ECO:0000305|PubMed:11815627}; CATALYTIC ACTIVITY: Reaction=[Pyr1]apelin-13 + H2O = [Pyr1]apelin-12 + L-phenylalanine; Xref=Rhea:RHEA:63604, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:147415, ChEBI:CHEBI:147416; Evidence={ECO:0000269|PubMed:27217402, ECO:0000269|PubMed:28293165};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63605; Evidence={ECO:0000269|PubMed:27217402}; CATALYTIC ACTIVITY: Reaction=apelin-17 + H2O = apelin-16 + L-phenylalanine; Xref=Rhea:RHEA:63608, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:147421, ChEBI:CHEBI:147422; Evidence={ECO:0000269|PubMed:27217402};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63609; Evidence={ECO:0000269|PubMed:27217402}; CATALYTIC ACTIVITY: Reaction=beta-casomorphin-7 + H2O = beta-casomorphin-6 + L-isoleucine; Xref=Rhea:RHEA:63568, ChEBI:CHEBI:15377, ChEBI:CHEBI:58045, ChEBI:CHEBI:147390, ChEBI:CHEBI:147391; Evidence={ECO:0000269|PubMed:11815627};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63569; Evidence={ECO:0000305|PubMed:11815627}; CATALYTIC ACTIVITY: Reaction=H2O + neocasomorphin = L-isoleucine + neocasomorphin-(1-5); Xref=Rhea:RHEA:63600, ChEBI:CHEBI:15377, ChEBI:CHEBI:58045, ChEBI:CHEBI:147417, ChEBI:CHEBI:147418; Evidence={ECO:0000269|PubMed:11815627};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63601; Evidence={ECO:0000305|PubMed:11815627}; |
| DNA Binding | |
| EC Number | 3.4.17.23; 3.4.17.- |
| Enzyme Function | FUNCTION: Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis (PubMed:27217402). Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II (PubMed:10969042, PubMed:10924499, PubMed:11815627, PubMed:19021774, PubMed:14504186). Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin (PubMed:10969042, PubMed:11815627). Also cleaves other biological peptides, such as apelins (apelin-13, [Pyr1]apelin-13, apelin-17, apelin-36), casomorphins (beta-casomorphin-7, neocasomorphin) and dynorphin A with high efficiency (PubMed:11815627, PubMed:27217402, PubMed:28293165). In addition, ACE2 C-terminus is homologous to collectrin and is responsible for the trafficking of the neutral amino acid transporter SL6A19 to the plasma membrane of gut epithelial cells via direct interaction, regulating its expression on the cell surface and its catalytic activity (PubMed:18424768, PubMed:19185582). {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:14504186, ECO:0000269|PubMed:18424768, ECO:0000269|PubMed:19021774, ECO:0000269|PubMed:19185582, ECO:0000269|PubMed:27217402}.; FUNCTION: [Isoform 2]: Non-functional as a carboxypeptidase. {ECO:0000269|PubMed:33077916}.; FUNCTION: (Microbial infection) Acts as a receptor for human coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus NL63/HCoV-NL63. {ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:15452268, ECO:0000269|PubMed:15791205, ECO:0000269|PubMed:15897467, ECO:0000269|PubMed:19901337, ECO:0000269|PubMed:24227843, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32221306, ECO:0000269|PubMed:32225175, ECO:0000269|PubMed:33000221, ECO:0000269|PubMed:33082294, ECO:0000269|PubMed:33432067}.; FUNCTION: [Isoform 2]: (Microbial infection) Non-functional as a receptor for human coronavirus SARS-CoV-2. {ECO:0000269|PubMed:33077916, ECO:0000269|PubMed:33432184}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9. {ECO:0000269|PubMed:11815627}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Beta strand (13); Binding site (5); Chain (2); Compositional bias (1); Disulfide bond (3); Glycosylation (7); Helix (32); Metal binding (3); Modified residue (2); Motif (5); Mutagenesis (66); Natural variant (4); Region (7); Sequence caution (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (12) |
| Keywords | 3D-structure;Alternative splicing;Carboxypeptidase;Cell membrane;Cell projection;Chloride;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Host cell receptor for virus entry;Host-virus interaction;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Receptor;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc |
| Interact With | Itself; P01019; P01019; P05067; Q01523; P11021; P05556; O60341; P01042; P30990; P35247; Q695T7; O14745; O15393; P52293; A0A6G6A1M4; A0A6M3G9R1; P0DTC2; P0DTC2; P59594; P59594; Q5GDB5; Q6Q1S2 |
| Induction | INDUCTION: Up-regulated in failing heart (PubMed:14504186, PubMed:15151696, PubMed:15671045). Expression is induced by IFNA and IFNG (PubMed:32413319, PubMed:32425701). Exposure to cigarette smoke increases expression in lungs (PubMed:32425701). Expression is decreased in nasal and bronchial epithelium of individuals with allergy after allergen challenge (PubMed:32333915). IL13 stimulation decreases expression in nasal and bronchial epithelium (PubMed:32333915). {ECO:0000269|PubMed:14504186, ECO:0000269|PubMed:15151696, ECO:0000269|PubMed:15671045, ECO:0000269|PubMed:32333915, ECO:0000269|PubMed:32413319, ECO:0000269|PubMed:32425701}.; INDUCTION: [Isoform 1]: Not induced by interferons such as IFNA, IFNB and IFNG. {ECO:0000269|PubMed:33077916}.; INDUCTION: [Isoform 2]: Expression is induced by interferons such as IFNA, IFNB and IFNG. It seems that isoform 2 is an interferon-stimulated gene (ISG) but not isoform 1. {ECO:0000269|PubMed:33077916}.; INDUCTION: (Microbial infection) In airway epithelial cells, expression is increased upon influenza A virus infection (PubMed:32413319). {ECO:0000269|PubMed:32413319}.; INDUCTION: [Isoform 2]: (Microbial infection) In airway epithelial cells, expression is induced by viruses such rhinoviruses and influenza virus. {ECO:0000269|PubMed:33077916, ECO:0000269|PubMed:33432184}.; INDUCTION: [Isoform 2]: (Microbial infection) Induced by human coronavirus SARS-CoV-2. {ECO:0000269|PubMed:33077916}. |
| Subcellular Location | SUBCELLULAR LOCATION: [Processed angiotensin-converting enzyme 2]: Secreted {ECO:0000269|PubMed:15983030, ECO:0000269|PubMed:33713620}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18424768}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8R0I0}. Cell projection, cilium {ECO:0000269|PubMed:33432184}. Apical cell membrane {ECO:0000269|PubMed:33432184}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:Q8R0I0}.; SUBCELLULAR LOCATION: [Isoform 2]: Apical cell membrane {ECO:0000269|PubMed:33432184}. |
| Modified Residue | MOD_RES 781; /note="Phosphotyrosine"; /evidence="ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498"; MOD_RES 783; /note="Phosphoserine"; /evidence="ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498" |
| Post Translational Modification | PTM: N-glycosylation on Asn-90 may limit SARS infectivity. {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19159218}.; PTM: Proteolytic cleavage by ADAM17 generates a secreted form (PubMed:15983030, PubMed:33713620). Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1. {ECO:0000269|PubMed:15983030, ECO:0000269|PubMed:21068237, ECO:0000269|PubMed:21563828, ECO:0000269|PubMed:24227843, ECO:0000269|PubMed:32132184, ECO:0000269|PubMed:33713620}.; PTM: Phosphorylated. Phosphorylation at Tyr-781 probably inhibits interaction with AP2M1 and enables interactions with proteins containing SH2 domains. {ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | Electron microscopy (55); X-ray crystallography (21) |
| Cross Reference PDB | 1R42; 1R4L; 2AJF; 3D0G; 3D0H; 3D0I; 3KBH; 3SCI; 3SCJ; 3SCK; 3SCL; 6ACG; 6ACJ; 6ACK; 6CS2; 6LZG; 6M0J; 6M17; 6M18; 6M1D; 6VW1; 7A91; 7A92; 7A94; 7A95; 7A96; 7A97; 7A98; 7BH9; 7CT5; 7DDO; 7DDP; 7DF4; 7DMU; 7DRV; 7DWX; 7DX4; 7DX5; 7DX6; 7DX7; 7DX8; 7DX9; 7E7E; 7FDG; 7FDH; 7FDI; 7JVO; 7KJ2; 7KJ3; 7KJ4; 7KMB; 7KMS; 7KMZ; 7KNB; 7KNE; 7KNH; 7KNI; 7L0N; 7L7F; 7LO4; 7MJM; 7MJN; 7NXC; 7V7Z; 7V80; 7V81; 7V82; 7V83; 7V84; 7V85; 7V86; 7V87; 7V88; 7V89; 7V8A; 7V8B; |
| Mapped Pubmed ID | 12967627; 14670965; 15010527; 15140961; 15163706; 15165741; 15233982; 15283675; 15361769; 15380922; 15474033; 15640278; 15769906; 15979045; 16001071; 16006956; 16055515; 16088128; 16115318; 16166094; 16211375; 16215952; 16283142; 16315782; 16338465; 16459167; 16510163; 16574921; 16647014; 16690935; 16866021; 16912312; 16962475; 17037534; 17037543; 17037544; 17037581; 17079315; 17303661; 17473847; 17504232; 17703127; 17897017; 17906677; 18022600; 18070603; 18208662; 18223023; 18223027; 18223028; 18258853; 18310257; 18389211; 18441099; 18448527; 18490652; 18496132; 18502721; 18554741; 18560893; 18660448; 18753062; 18814896; 18926157; 18931070; 19020433; 19034303; 19051693; 19067252; 19077694; 19136547; 19141296; 19164471; 19164480; 19212105; 19286756; 19286757; 19289653; 19297479; 19321428; 19411314; 19461648; 19684612; 19700132; 19716087; 19864379; 19913121; 19924243; 19926873; 19934006; 20060185; 20117248; 20117991; 20142028; 20160196; 20204277; 20224560; 20349406; 20484496; 20541774; 20559404; 20592051; 20628086; 20660625; 20674894; 20679547; 20692300; 20703229; 20798044; 20813695; 20831027; 20854388; 20926566; 21052031; 21072744; 21189404; 21265092; 21316680; 21325420; 21346373; 21411533; 21457402; 21490025; 21670585; 21814048; 21864606; 21880865; 21946695; 21952934; 21963832; 21993363; 22025374; 22033511; 22048948; 22179088; 22291007; 22297693; 22475818; 22523556; 22647782; 22718567; 22749485; 22750422; 22816037; 23077079; 23091417; 23144053; 23230080; 23328447; 23488800; 23545945; 23630610; 23816468; 23893738; 23921915; 24014829; 24054336; 24100303; 24112034; 24134599; 24142614; 24147777; 24158104; 24172901; 24191856; 24342297; 24564768; 24662240; 24691269; 24728465; 24838502; 24842388; 24920267; 25200929; 25237166; 25237167; 25359286; 25519733; 25534429; 25663464; 25665060; 25701390; 25721616; 25791940; 25813276; 25815490; 25869724; 26067610; 26995300; 27063099; 27093376; 27121444; 27310975; 27460845; 27488276; 27500554; 27615597; 27738071; 27884212; 27889958; 27925380; 27965422; 27983983; 28186543; 28223093; 28440441; 28605813; 28744816; 28935640; 29128354; 29351514; 29441892; 29561187; 29570986; 30055537; 30056001; 30227878; 30326474; 30335025; 30342552; 30347406; 30440128; 30514826; 30542083; 30591810; 30759273; 30784777; 30917908; 31023337; 31430320; 31607667; 31847529; 32094336; 32100877; 32125455; 32132184; 32149769; 32169277; 32221983; 32246845; 32249956; 32251718; 32268515; 32275855; 32276140; 32283335; 32283711; 32293672; 32302706; 32303424; 32324479; 32329629; 32333601; 32345140; 32345362; 32361911; 32362314; 32365180; 32365751; 32374427; 32380511; 32383269; 32404529; 32410141; 32410735; 32414646; 32423095; 32427288; 32428380; 32432483; 32435059; 32441816; 32445872; 32448590; 32454066; 32463098; 32484368; 32496587; 32497323; 32501810; 32504757; 32512290; 32522846; 32525008; 32531372; 32532959; 32544566; 32558150; 32565362; 32584474; 32593613; 32594644; 32599080; 32602627; 32620366; 32623546; 32627059; 32635188; 32639084; 32642005; 32658093; 32661393; 32664879; 32673162; 32675312; 32676883; 32681121; 32691370; 32691890; 32694292; 32705281; 32726325; 32748812; 32759995; 32768580; 32776522; 32778033; 32786692; 32791137; 32798244; 32806067; 32826754; 32828550; 32831104; 32831324; 32833435; 32841605; 32851645; 32851697; 32858292; 32861070; 32880862; 32882331; 32883878; 32916258; 32917283; 32917504; 32919067; 32927621; 32936531; 32936832; 32942285; 32945396; 32950735; 32980345; 32986926; 32991819; 32995768; 32996784; 33003587; 33008593; 33016778; 33022363; 33024003; 33031602; 33038424; 33042151; 33046696; 33053430; 33064147; 33077915; 33081421; 33082574; 33084449; 33104520; 33112147; 33112187; 33112891; 33116139; 33119197; 33122196; 33125431; 33129880; 33155280; 33160965; 33164751; 33172369; 33175551; 33177651; 33181224; 33188579; 33190150; 33197855; 33207244; 33207245; 33210729; 33231620; 33239166; 33241696; 33243086; 33244196; 33246692; 33247425; 33249264; 33251580; 33253796; 33255902; 33257679; 33268377; 33271067; 33272568; 33275517; 33275540; 33277323; 33278516; 33284956; 33289868; 33293627; 33303459; 33309272; 33310017; 33315943; 33322198; 33323800; 33335073; 33338639; 33340519; 33347434; 33349849; 33358483; 33370311; 33374416; 33386398; 33400951; 33401657; 33403489; 33407110; 33413387; 33418950; 33421967; 33421977; 33432247; 33441985; 33442728; 33443816; 33462852; 33465158; 33483864; 33486479; 33492586; 33497607; 33497931; 33499313; 33505220; 33511992; 33514423; 33517235; 33524990; 33525415; 33525682; 33533060; 33536584; 33554856; 33556147; 33558493; 33563197; 33576441; 33578036; 33595589; 33597251; 33602129; 33602511; 33607086; 33607284; 33609497; 33621484; 33624300; 33631165; 33635001; 33657582; 33668756; 33669132; 33704002; 33705542; 33707427; 33707526; 33716040; 33727353; 33728680; 33737693; 33738989; 33752217; 33755980; 33760889; 33765612; 33774672; 33782449; 33794092; 33812037; 33818000; 33819740; 33828231; 33833750; 33846513; 33852911; 33853968; 33864655; 33879756; 33880537; 33884270; 33893649; 33895782; 33900725; 33903171; 33906662; 33910120; 33914735; 33928889; 33946649; 33958627; 33958745; 33962629; 33963054; 33963249; 33965375; 33973994; 33979162; 33979391; 33980808; 33987897; 33992693; 33999091; 34001841; 34004284; 34006835; 34012108; 34013346; 34030677; 34031383; 34045511; 34047452; 34048457; 34052578; 34067878; 34068579; 34075603; 34086459; 34097714; 34102107; 34105996; 34108510; 34111408; 34111482; 34111949; 34115612; 34118117; 34131396; 34133899; 34138966; 34139177; 34142714; 34155214; 34160563; 34161778; 34185793; 34193390; 34201415; 34214142; 34257580; 34257745; 34282808; 34287040; 34289058; 34293134; 34293137; 34304698; 34305888; 34312429; 34338772; 34341401; 34354120; 34356057; 34356070; 34359894; 34369278; 34375715; 34378348; 34390216; 34400835; 34407940; 34413267; 34414454; 34416267; 34416436; 34417262; 34418496; 34425281; 34428252; 34445373; 34449302; 34463644; 34471195; 34471421; 34474076; 34478478; 34502041; 34514615; 34516024; 34531369; 34538460; 34551157; 34561952; 34562851; 34578296; 34588290; 34590312; 34601723; 34635175; 34637655; 34644391; 34655895; 34668773; 34671049; 34674152; 34689596; 34719202; 34746028; 34751326; 34769052; 34772947; 34807265; 34815389; 34819448; 34819560; 34824253; 34835087; 34856802; 34856891; 34883069; 34889898; 34900223; 34904376; 34914928; 34915409; 34919090; 34927585; 34930910; 34932561; 34995294; 35012625; 35022007; |
| Motif | MOTIF 778..786; /note="LIR"; /evidence="ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498"; MOTIF 781..785; /note="SH2-binding"; /evidence="ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498"; MOTIF 781..784; /note="Endocytic sorting signal"; /evidence="ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498"; MOTIF 792..795; /note="PTB"; /evidence="ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498"; MOTIF 803..805; /note="PDZ-binding"; /evidence="ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498" |
| Gene Encoded By | |
| Mass | 92,463 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.9 uM for angiotensin I {ECO:0000269|PubMed:11815627}; KM=2.0 uM for angiotensin II {ECO:0000269|PubMed:11815627}; KM=6.8 uM for apelin-13 {ECO:0000269|PubMed:11815627}; KM=290 uM for [des-Arg(9)]-bradykinin {ECO:0000269|PubMed:11815627}; KM=130 uM for Lys-[des-Arg(9)]-bradykinin {ECO:0000269|PubMed:11815627}; KM=31 uM for beta-casomorphin {ECO:0000269|PubMed:11815627}; KM=5.5 uM for dynorphin A-(1-13) {ECO:0000269|PubMed:11815627}; KM=300 uM for neurotensin-(1-8) {ECO:0000269|PubMed:11815627}; KM=58.6 uM for angiotensin II {ECO:0000269|PubMed:19021774}; KM=12 uM for [Pyr1]apelin-13 {ECO:0000269|PubMed:27217402}; KM=19 uM for apelin-17 {ECO:0000269|PubMed:27217402}; Vmax=28.7 nmol/min/mg enzyme with angiotensin II as substrate {ECO:0000269|PubMed:19021774}; Note=kcat is 0.034 sec(-1) with angiotensin I as substrate. kcat is 3.5 sec(-1) with angiotensin II as substrate. kcat is 13 sec(-1) with apelin-13 as substrate. kcat is 62 sec(-1) with [des-Arg(9)]-bradykinin as substrate. kcat is 26 sec(-1) with Lys-[des-Arg(9)]-bradykinin as substrate. kcat is 6.8 sec(-1) with beta-casomorphin as substrate. kcat is 16 sec(-1) with dynorphin A-(1-13) as substrate. kcat is 57 sec(-1) with neurotensin-(1-8) as substrate (PubMed:11815627). kcat is 19.1 sec(-1) with [Pyr1]apelin-13 as substrate. kcat is 7.7 sec(-1) with apelin-17 as substrate (PubMed:27217402). {ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:27217402}; |
| Metal Binding | METAL 374; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:14754895; METAL 378; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:14754895; METAL 402; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:14754895 |
| Rhea ID | RHEA:26554; RHEA:26555; RHEA:63532; RHEA:63533; RHEA:63536; RHEA:63537; RHEA:63540; RHEA:63541; RHEA:63572; RHEA:63573; RHEA:63544; RHEA:63545; RHEA:63556; RHEA:63557; RHEA:63564; RHEA:63565; RHEA:63604; RHEA:63605; RHEA:63608; RHEA:63609; RHEA:63568; RHEA:63569; RHEA:63600; RHEA:63601 |
| Cross Reference Brenda | 3.4.15.1;3.4.17.23; |