ACE2
entrez
59272
canonical
uniprot
Q9BYF1
canonical
ensembl
ENSG00000130234
resolver
ensp
ENSP00000252519
resolver
ensp
ENSP00000389326
resolver
ensp
ENSP00000504010
resolver
ensp
ENSP00000504747
resolver
ensp
ENSP00000541987
resolver
ensp
ENSP00000541988
resolver
enst
ENST00000679278
resolver
genesymbol
ACE2
resolver
hgnc
HGNC:13557
resolver
uniprot
A0A7D6JAD5
resolver
uniprot
A0A7I2V4H0
resolver
uniprot
C7ECU1
resolver
uniprot
Q6UWP0
resolver
uniprot
Q86WT0
resolver
uniprot
Q9NRA7
resolver
uniprot
Q9UFZ6
resolver
uniprot_entry
A0A7I2V4H0_HUMAN
resolver
uniprot_entry
ACE2_HUMAN
resolver
uniprot_sec
A0A7D6JAD5
resolver
uniprot_sec
C7ECU1
resolver
uniprot_sec
Q6UWP0
resolver
uniprot_sec
Q86WT0
resolver
uniprot_sec
Q9NRA7
resolver
uniprot_sec
Q9UFZ6
resolver
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:10924499, PubMed:10969042). 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}.
uniprot
proteins
amino_acid_sequence
MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF
uniprot
proteins
ec_number
3.4.17.-
uniprot
proteins
ec_number
3.4.17.23
uniprot
proteins
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:10924499, PubMed:10969042, PubMed:11815627, PubMed:14504186, PubMed:19021774). 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: (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:32221306, ECO:0000269|PubMed:32225175, ECO:0000269|PubMed:33000221, ECO:0000269|PubMed:33082294, ECO:0000269|PubMed:33432067}.; FUNCTION: [Isoform 2]: Non-functional as a carboxypeptidase. {ECO:0000269|PubMed:33077916}.; FUNCTION: [Isoform 2]: (Microbial infection) Non-functional as a receptor for human coronavirus SARS-CoV-2. {ECO:0000269|PubMed:33077916, ECO:0000269|PubMed:33432184}.
uniprot
proteins
mass_dalton
92463
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="S->P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 24..26; /note="QAK->KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 24; /note="Q->T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 25; /note="A->V: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 27; /note="T->Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-330 and L-386."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 29; /note="L->F: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 31; /note="K->D: Abolishes interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 31; /note="K->Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 33; /note="N->D: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 34; /note="H->A: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 37; /note="E->A: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 38; /note="D->A: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 39; /note="L->R: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 40; /note="F->D: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 41; /note="Y->A: Strongly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 41; /note="Y->R: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 42; /note="Q->L: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 68; /note="K->D: Slightly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 69; /note="W->V: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 72; /note="F->Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 75; /note="E->K: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 76; /note="Q->T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 79; /note="L->T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 82..84; /note="MYP->NFS: Inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 89; /note="Q->P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 90; /note="N->Q: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 91; /note="L->P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 92; /note="T->Q: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 110; /note="E->P: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 135..136; /note="PD->SM: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 160; /note="E->R: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 169; /note="R->Q: About 95% loss of angiotensin I cleavage."; /evidence="ECO:0000269|PubMed:19021774"; MUTAGEN 192; /note="R->D: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 219; /note="R->D: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 239; /note="H->Q: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 271; /note="W->Q: About 95% loss of angiotensin I cleavage."; /evidence="ECO:0000269|PubMed:19021774"; MUTAGEN 273; /note="R->Q: Complete loss of enzyme activity. Does not affect amino acid transport activity of SLC6A19."; /evidence="ECO:0000269|PubMed:16008552, ECO:0000269|PubMed:19185582"; MUTAGEN 309; /note="K->D: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 312; /note="E->A: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 324; /note="T->A: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 324; /note="T->P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 325; /note="Q->P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 330; /note="N->Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-27 and L-386."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 338..340; /note="NVQ->DDR: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 345; /note="H->A: Complete loss of enzyme activity."; /evidence="ECO:0000269|PubMed:16008552"; MUTAGEN 350; /note="D->A: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 351; /note="L->F: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 353; /note="K->H,A,D: Abolishes interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 355; /note="D->A: Strongly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 357; /note="R->A: Strongly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 359; /note="L->K,A: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 383; /note="M->A: Slightly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 386; /note="A->L: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-27 and Y-330."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 389; /note="P->A: Slightly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 389; /note="P->D: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 393; /note="R->A: Slightly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 393; /note="R->K: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 425..427; /note="SPD->PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 465..467; /note="KGE->QDK: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 481; /note="K->Q: About 80% loss of angiotensin I cleavage."; /evidence="ECO:0000269|PubMed:19021774"; MUTAGEN 505; /note="H->A: Complete loss of enzyme activity."; /evidence="ECO:0000269|PubMed:16008552"; MUTAGEN 514; /note="R->Q: About 50% loss of angiotensin I cleavage but two-fold greater activity with angiotensin II."; /evidence="ECO:0000269|PubMed:19021774"; MUTAGEN 518; /note="R->G: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein."; /evidence="ECO:0000269|PubMed:32753553"; MUTAGEN 559; /note="R->S: Slightly inhibits interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 603; /note="F->T: No effect on interaction with SARS-CoV spike glycoprotein."; /evidence="ECO:0000269|PubMed:15791205"; MUTAGEN 788; /note="K->R: Increases ACE2 protein stability."; /evidence="ECO:0000269|PubMed:36876523"; MUTAGEN 802..805; /note="QTSF->AAAA: Loss of interaction with NHERF1."; /evidence="ECO:0000269|PubMed:34189428
uniprot
proteins
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}.; PTM: Ubiquitinated. Ubiquitinated on Lys-788 via 'Lys-48'-linked ubiquitin (PubMed:36876523). 'Lys-48'-linked deubiquitinated by USP50 on the Lys-788; leading to its stabilization (PubMed:36876523). {ECO:0000269|PubMed:36876523}.
uniprot
proteins
protein_family
Peptidase M2 family
uniprot
proteins
pubmed
10924499
uniprot
proteins
pubmed
10969042
uniprot
proteins
pubmed
11815627
uniprot
proteins
pubmed
12358520
uniprot
proteins
pubmed
12459472
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14504186
uniprot
proteins
pubmed
14647384
uniprot
proteins
pubmed
14754895
uniprot
proteins
pubmed
15084671
uniprot
proteins
pubmed
15141377
uniprot
proteins
pubmed
15151696
uniprot
proteins
pubmed
15231706
uniprot
proteins
pubmed
15276642
uniprot
proteins
pubmed
15452268
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15671045
uniprot
proteins
pubmed
15791205
uniprot
proteins
pubmed
15897467
uniprot
proteins
pubmed
15937940
uniprot
proteins
pubmed
15983030
uniprot
proteins
pubmed
16008552
uniprot
proteins
pubmed
16166518
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18424768
uniprot
proteins
pubmed
19021774
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19185582
uniprot
proteins
pubmed
19901337
uniprot
proteins
pubmed
21068237
uniprot
proteins
pubmed
21563828
uniprot
proteins
pubmed
24227843
uniprot
proteins
pubmed
27217402
uniprot
proteins
pubmed
28293165
uniprot
proteins
pubmed
30102747
uniprot
proteins
pubmed
30356097
uniprot
proteins
pubmed
32075877
uniprot
proteins
pubmed
32132184
uniprot
proteins
pubmed
32142651
uniprot
proteins
pubmed
32170560
uniprot
proteins
pubmed
32221306
uniprot
proteins
pubmed
32225175
uniprot
proteins
pubmed
32225176
uniprot
proteins
pubmed
32327758
uniprot
proteins
pubmed
32333915
uniprot
proteins
pubmed
32358202
uniprot
proteins
pubmed
32404436
uniprot
proteins
pubmed
32413319
uniprot
proteins
pubmed
32425701
uniprot
proteins
pubmed
32558308
uniprot
proteins
pubmed
32715618
uniprot
proteins
pubmed
32753553
uniprot
proteins
pubmed
33000221
uniprot
proteins
pubmed
33077916
uniprot
proteins
pubmed
33082294
uniprot
proteins
pubmed
33102950
uniprot
proteins
pubmed
33133145
uniprot
proteins
pubmed
33432067
uniprot
proteins
pubmed
33432184
uniprot
proteins
pubmed
33436497
uniprot
proteins
pubmed
33436498
uniprot
proteins
pubmed
33713620
uniprot
proteins
pubmed
34189428
uniprot
proteins
pubmed
36228039
uniprot
proteins
pubmed
36735681
uniprot
proteins
pubmed
36757924
uniprot
proteins
pubmed
36876523
uniprot
proteins
sequence_length
805
uniprot
proteins
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}.
uniprot
proteins
transmembrane_region
TRANSMEM 741..761; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01354
uniprot
proteins