ACE2

Functionⁱ

Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function.4 Publications

(Microbial infection) Acts as a receptor for SARS coronavirus/SARS-CoV.3 Publications

(Microbial infection) Acts as a receptor for Human coronavirus NL63/HCoV-NL63.1 Publication

Catalytic activityⁱ

Angiotensin II + H₂O = angiotensin-_1-7 + L-phenylalanine.

Cofactorⁱ

Protein has several cofactor binding sites:

Activity regulationⁱ

Activated by chloride and fluoride, but not bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the ACE inhibitors linosipril, captopril and enalaprilat.4 Publications

Kineticsⁱ

pH dependenceⁱ

Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	169	Chloride	1
Binding siteⁱ	273	Substrate	1
Binding siteⁱ	345	Substrate	1
Binding siteⁱ	346	Substrate; via carbonyl oxygen	1
Binding siteⁱ	371	Substrate	1
Metal bindingⁱ	374	Zinc; catalytic	1
Active siteⁱ	375		1
Metal bindingⁱ	378	Zinc; catalytic	1
Metal bindingⁱ	402	Zinc; catalytic	1
Binding siteⁱ	477	Chloride	1
Binding siteⁱ	481	Chloride	1
Active siteⁱ	505		1
Binding siteⁱ	515	Substrate	1

GO - Molecular functionⁱ

carboxypeptidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10969042
endopeptidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 15283675
exopeptidase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
metallocarboxypeptidase activity
Source: Reactome
Inferred from experimentⁱ
virus receptor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 18343844
zinc ion binding
Source: BHF-UCL
Traceable author statementⁱ
- 10924499

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

angiotensin maturation Source: Reactome
angiotensin-mediated drinking behavior
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 18258853
positive regulation of amino acid transport
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19185582
positive regulation of cardiac muscle contraction Source: Ensembl
positive regulation of gap junction assembly
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12967627
positive regulation of reactive oxygen species metabolic process
Source: BHF-UCL
Inferred by curatorⁱ
- 15380922
receptor biosynthetic process
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 18258853
receptor-mediated virion attachment to host cell
Source: BHF-UCL
Inferred from direct assayⁱ
- 18343844
regulation of blood vessel diameter
Source: BHF-UCL
Inferred by curatorⁱ
- 15380922
regulation of cardiac conduction
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12967627
regulation of cell proliferation
Source: BHF-UCL
Traceable author statementⁱ
- 17703127
regulation of cytokine production
Source: BHF-UCL
Inferred by curatorⁱ
- 15380922
regulation of inflammatory response
Source: BHF-UCL
Inferred by curatorⁱ
- 15380922
regulation of systemic arterial blood pressure by renin-angiotensin
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 18258853
regulation of vasoconstriction
Source: BHF-UCL
Inferred by curatorⁱ
- 15380922
tryptophan transport Source: Ensembl
viral entry into host cell
Source: UniProtKB
Traceable author statementⁱ
- 15165741

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Carboxypeptidase, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor
Biological process	Host-virus interaction
Ligand	Chloride, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	3.4.15.1 2681 3.4.17.23 2681
Reactomeⁱ	R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
SABIO-RKⁱ	Q9BYF1

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	M02.006

MEROPSⁱ

M02.006

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Angiotensin-converting enzyme 2 (EC:3.4.17.23) Alternative name(s): ACE-related carboxypeptidase Angiotensin-converting enzyme homolog Short name: ACEH Metalloprotease MPROT15 Cleaved into the following chain: Processed angiotensin-converting enzyme 2
Gene namesⁱ	Name:ACE2 ORF Names:UNQ868/PRO1885
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome X

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000130234.10
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:13557 ACE2
MIMⁱ	300335 gene
neXtProtⁱ	NX_Q9BYF1

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	18 – 740	ExtracellularSequence analysisAdd BLAST	723
Transmembraneⁱ	741 – 761	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	762 – 805	CytoplasmicSequence analysisAdd BLAST	44

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Membrane, Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	24 – 26	QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	3
Mutagenesisⁱ	31	K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	37	E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	38	D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	41	Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	68	K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	82 – 84	MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	3
Mutagenesisⁱ	110	E → P: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	135 – 136	PD → SM: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	2
Mutagenesisⁱ	160	E → R: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	192	R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	219	R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	239	H → Q: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	309	K → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	312	E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	324	T → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	338 – 340	NVQ → DDR: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	3
Mutagenesisⁱ	350	D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	353	K → H, A or D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	355	D → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	357	R → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	359	L → K or A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	383	M → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	389	P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	393	R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	425 – 427	SPD → PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	3
Mutagenesisⁱ	465 – 467	KGE → QDK: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	3
Mutagenesisⁱ	559	R → S: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication	1
Mutagenesisⁱ	603	F → T: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	59272
Open Targets More...OpenTargetsⁱ	ENSG00000130234
PharmGKBⁱ	PA425

Chemistry databases

ChEMBLⁱ	CHEMBL3736
Drug and drug target database More...DrugBankⁱ	DB00722 Lisinopril DB00691 Moexipril DB05203 SPP1148 DB05358 TAK-491
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1614

Polymorphism and mutation databases

BioMutaⁱ	ACE2
DMDMⁱ	71658783

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 17	Sequence analysisAdd BLAST	17
ChainⁱPRO_0000028570	18 – 805	Angiotensin-converting enzyme 2Add BLAST	788
ChainⁱPRO_0000292268	18 – 708	Processed angiotensin-converting enzyme 2Add BLAST	691

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	53	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	90	N-linked (GlcNAc...) asparagine2 Publications	1
Glycosylationⁱ	103	N-linked (GlcNAc...) asparagine1 Publication	1
Disulfide bondⁱ	133 ↔ 141	1 Publication
Glycosylationⁱ	322	N-linked (GlcNAc...) asparagine1 Publication	1
Disulfide bondⁱ	344 ↔ 361	1 Publication
Glycosylationⁱ	432	N-linked (GlcNAc...) asparagine1 Publication	1
Disulfide bondⁱ	530 ↔ 542	1 Publication
Glycosylationⁱ	546	N-linked (GlcNAc...) asparagine2 Publications	1
Glycosylationⁱ	690	N-linked (GlcNAc...) asparagineSequence analysis	1

Post-translational modificationⁱ

N-glycosylation on Asn-90 may limit SARS infectivity.5 Publications

Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1.4 Publications

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbⁱ	Q9BYF1
PeptideAtlas More...PeptideAtlasⁱ	Q9BYF1
PRIDEⁱ	Q9BYF1
ProteomicsDBⁱ	79634 79635 [Q9BYF1-2]

PTM databases

GlyConnectⁱ	1012
iPTMnetⁱ	Q9BYF1
PhosphoSitePlusⁱ	Q9BYF1

Miscellaneous databases

PMAP-CutDBⁱ	Q9BYF1

PMAP-CutDBⁱ

Q9BYF1

Expressionⁱ

Tissue specificityⁱ

Expressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells. Expressed in lung alveolar epithelial cells, enterocytes of the small intestine, Leydig cells and Sertoli cells (at protein level). Expressed in heart, kidney, testis, and gastrointestinal system.6 Publications

Inductionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000130234 Expressed in 129 organ(s), highest expression level in jejunal mucosa
CleanExⁱ	HS_ACE2
Genevisibleⁱ	Q9BYF1 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB026174 HPA000288

HPAⁱ

CAB026174
HPA000288

Interactionⁱ

Subunit structureⁱ

Interacts with ITGB1. Interacts with the catalytically active form of TMPRSS2.3 Publications

(Microbial infection) Interacts with SARS coronavirus/SARS-CoV.3 Publications

(Microbial infection) Interacts with Human coronavirus NL63/HCoV-NL63 spike glycoprotein.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
S	Q6Q1S2	3	EBI-15814450,EBI-15814420	From Human coronavirus NL63.

With

Entry

#Exp.

IntAct

Notes

S

Q6Q1S2

3

EBI-15814450,EBI-15814420

From Human coronavirus NL63.

Protein-protein interaction databases

BioGridⁱ	121864, 7 interactors
Database of interacting proteins More...DIPⁱ	DIP-44689N
IntActⁱ	Q9BYF1, 3 interactors
Molecular INTeraction database More...MINTⁱ	Q9BYF1
STRINGⁱ	9606.ENSP00000252519

Chemistry databases

BindingDBⁱ

Q9BYF1

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	23 – 52	Combined sources	30
Helixⁱ	56 – 77	Combined sources	22
Turnⁱ	78 – 82	Combined sources	5
Helixⁱ	85 – 87	Combined sources	3
Helixⁱ	91 – 100	Combined sources	10
Helixⁱ	104 – 107	Combined sources	4
Helixⁱ	110 – 129	Combined sources	20
Beta strandⁱ	131 – 134	Combined sources	4
Beta strandⁱ	137 – 143	Combined sources	7
Turnⁱ	144 – 146	Combined sources	3
Helixⁱ	148 – 154	Combined sources	7
Helixⁱ	158 – 171	Combined sources	14
Helixⁱ	173 – 193	Combined sources	21
Beta strandⁱ	196 – 198	Combined sources	3
Helixⁱ	199 – 204	Combined sources	6
Turnⁱ	205 – 207	Combined sources	3
Turnⁱ	213 – 215	Combined sources	3
Helixⁱ	220 – 251	Combined sources	32
Turnⁱ	253 – 255	Combined sources	3
Beta strandⁱ	258 – 260	Combined sources	3
Helixⁱ	264 – 266	Combined sources	3
Beta strandⁱ	267 – 271	Combined sources	5
Helixⁱ	276 – 278	Combined sources	3
Helixⁱ	279 – 282	Combined sources	4
Turnⁱ	284 – 287	Combined sources	4
Turnⁱ	294 – 297	Combined sources	4
Helixⁱ	298 – 300	Combined sources	3
Helixⁱ	304 – 316	Combined sources	13
Turnⁱ	317 – 319	Combined sources	3
Helixⁱ	327 – 330	Combined sources	4
Beta strandⁱ	338 – 340	Combined sources	3
Beta strandⁱ	347 – 352	Combined sources	6
Beta strandⁱ	355 – 359	Combined sources	5
Helixⁱ	366 – 384	Combined sources	19
Turnⁱ	385 – 387	Combined sources	3
Helixⁱ	390 – 392	Combined sources	3
Helixⁱ	400 – 413	Combined sources	14
Helixⁱ	415 – 420	Combined sources	6
Turnⁱ	422 – 426	Combined sources	5
Helixⁱ	432 – 446	Combined sources	15
Helixⁱ	449 – 465	Combined sources	17
Beta strandⁱ	466 – 468	Combined sources	3
Helixⁱ	470 – 472	Combined sources	3
Helixⁱ	473 – 483	Combined sources	11
Beta strandⁱ	486 – 488	Combined sources	3
Helixⁱ	499 – 502	Combined sources	4
Helixⁱ	504 – 507	Combined sources	4
Helixⁱ	514 – 531	Combined sources	18
Turnⁱ	532 – 534	Combined sources	3
Helixⁱ	539 – 541	Combined sources	3
Helixⁱ	548 – 558	Combined sources	11
Turnⁱ	559 – 562	Combined sources	4
Helixⁱ	566 – 574	Combined sources	9
Beta strandⁱ	575 – 578	Combined sources	4
Helixⁱ	582 – 598	Combined sources	17
Beta strandⁱ	600 – 602	Combined sources	3
Beta strandⁱ	607 – 609	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9BYF1
SMRⁱ	Q9BYF1
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9BYF1

EvolutionaryTraceⁱ

Q9BYF1

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	30 – 41	Interaction with SARS-CoV spike glycoproteinAdd BLAST	12
Regionⁱ	82 – 84	Interaction with SARS-CoV spike glycoprotein	3
Regionⁱ	353 – 357	Interaction with SARS-CoV spike glycoprotein	5
Regionⁱ	652 – 659	Essential for cleavage by ADAM17	8
Regionⁱ	697 – 716	Essential for cleavage by TMPRSS11D and TMPRSS2Add BLAST	20

Sequence similaritiesⁱ

Belongs to the peptidase M2 family.Curated

Keywords - Domainⁱ

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3690 Eukaryota ENOG410XPJ3 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00520000055576
HOGENOMⁱ	HOG000292210
HOVERGENⁱ	HBG000265
InParanoidⁱ	Q9BYF1
KEGG Orthology (KO) More...KOⁱ	K09708
OMAⁱ	KGDFRIK
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G033S
PhylomeDBⁱ	Q9BYF1
TreeFamⁱ	TF312861

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06461 M2_ACE, 1 hit
InterProⁱ	View protein in InterPro IPR031588 Collectrin_dom IPR001548 Peptidase_M2
PANTHERⁱ	PTHR10514 PTHR10514, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16959 Collectrin, 1 hit PF01401 Peptidase_M2, 1 hit
PRINTSⁱ	PR00791 PEPDIPTASEA
PROSITEⁱ	View protein in PROSITE PS00142 ZINC_PROTEASE, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

Isoform 1 (identifier: Q9BYF1-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY 
        60         70         80         90        100
NTNITEENVQ NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL 
       110        120        130        140        150
QQNGSSVLSE DKSKRLNTIL NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE 
       160        170        180        190        200
IMANSLDYNE RLWAWESWRS EVGKQLRPLY EEYVVLKNEM ARANHYEDYG 
       210        220        230        240        250
DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL HAYVRAKLMN 
       260        270        280        290        300
AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ 
       310        320        330        340        350
AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD 
       360        370        380        390        400
LGKGDFRILM CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF 
       410        420        430        440        450
HEAVGEIMSL SAATPKHLKS IGLLSPDFQE DNETEINFLL KQALTIVGTL 
       460        470        480        490        500
PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM KREIVGVVEP VPHDETYCDP 
       510        520        530        540        550
ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH KCDISNSTEA 
       560        570        580        590        600
GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK 
       610        620        630        640        650
NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA 
       660        670        680        690        700
MRQYFLKVKN QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV 
       710        720        730        740        750
EKAIRMSRSR INDAFRLNDN SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM 
       760        770        780        790        800
GVIVVGIVIL IFTGIRDRKK KNKARSGENP YASIDISKGE NNPGFQNTDD 

VQTSF

Length:805

Mass (Da):92,463

Last modified:August 2, 2005 - v2

Checksum:ⁱ8EE6EB0A931550E8

GO

Isoform 2 (identifier: Q9BYF1-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
555-555: F → L
556-805: Missing.

« Hide

        10         20         30         40         50
MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY 
        60         70         80         90        100
NTNITEENVQ NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL 
       110        120        130        140        150
QQNGSSVLSE DKSKRLNTIL NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE 
       160        170        180        190        200
IMANSLDYNE RLWAWESWRS EVGKQLRPLY EEYVVLKNEM ARANHYEDYG 
       210        220        230        240        250
DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL HAYVRAKLMN 
       260        270        280        290        300
AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ 
       310        320        330        340        350
AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD 
       360        370        380        390        400
LGKGDFRILM CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF 
       410        420        430        440        450
HEAVGEIMSL SAATPKHLKS IGLLSPDFQE DNETEINFLL KQALTIVGTL 
       460        470        480        490        500
PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM KREIVGVVEP VPHDETYCDP 
       510        520        530        540        550
ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH KCDISNSTEA 

GQKLL

Note: No experimental confirmation available.

Show »

Length:555

Mass (Da):63,912

Checksum:ⁱ3A3842AB792E2DBC

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	18	Q → H in CAB53682 (PubMed:17974005).Curated	1
Sequence conflictⁱ	508	N → D in AAQ89076 (PubMed:12975309).Curated	1
Sequence conflictⁱ	631	K → R in BAB40370 (Ref. 5) Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_023082	26	K → R1 PublicationCorresponds to variant dbSNP:rs4646116Ensembl.		1
Natural variantⁱVAR_023083	638	N → S1 PublicationCorresponds to variant dbSNP:rs183135788Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_014901	555	F → L in isoform 2. 1 Publication		1
Alternative sequenceⁱVSP_014902	556 – 805	Missing in isoform 2. 1 PublicationAdd BLAST		250

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF291820 mRNA Translation: AAF99721.1 AF241254 mRNA Translation: AAF78220.1 AY623811 mRNA Translation: AAT45083.1 AB193259 mRNA Translation: BAD99266.1 AB193260 mRNA Translation: BAD99267.1 AB046569 mRNA Translation: BAB40370.1 E39033 mRNA No translation available. GQ262784 mRNA Translation: ACT66268.1 AY358714 mRNA Translation: AAQ89076.1 AY217547 Genomic DNA Translation: AAO25651.1 CH471074 Genomic DNA Translation: EAW98892.1 BC039902 mRNA Translation: AAH39902.1 BC048094 mRNA Translation: AAH48094.2 AL110224 mRNA Translation: CAB53682.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14169.1 [Q9BYF1-1]
PIRⁱ	T14762
NCBI Reference Sequences More...RefSeqⁱ	NP_068576.1, NM_021804.2 [Q9BYF1-1]
UniGeneⁱ	Hs.178098

Genome annotation databases

Ensemblⁱ	ENST00000252519; ENSP00000252519; ENSG00000130234 [Q9BYF1-1] ENST00000427411; ENSP00000389326; ENSG00000130234 [Q9BYF1-1]
GeneIDⁱ	59272
KEGGⁱ	hsa:59272
UCSC genome browser More...UCSCⁱ	uc004cxa.2 human [Q9BYF1-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9BYF1	Angiotensin-converting enzyme 2		PONAB		805	UniRef90_Q9BYF1
Angiotensin-converting enzyme		HUMAN		805
Angiotensin-converting enzyme		PANTR		805
Angiotensin-converting enzyme		MACMU		805
Angiotensin-converting enzyme		MACNE		805
+50
Q9BYF1-2	Angiotensin-converting enzyme		PANTR		694	UniRef90_Q9BYF1-2
Angiotensin-converting enzyme		PANPA		694
UPI0005D0169F		HUMAN		694
UPI000D18B6B4		HUMAN		605
UPI00024DB10F		HUMAN		603

Protein	Similar proteins		Species	Score	Length	Source
Q9BYF1	Angiotensin-converting enzyme 2		PONAB		805	UniRef50_Q9BYF1
Angiotensin-converting enzyme 2		BOVIN		804
Angiotensin-converting enzyme 2		MOUSE		805
Angiotensin-converting enzyme 2		RAT		805
Angiotensin-converting enzyme 2		FELCA		805
+414
Q9BYF1-2	Angiotensin-converting enzyme		PANPA		694	UniRef50_Q9BYF1-2
Angiotensin-converting enzyme		PANTR		694
Angiotensin-converting enzyme		FUKDA		693
Angiotensin-converting enzyme		CRIGR		644
Angiotensin-converting enzyme (Fragment)		NEOLE		679
+10

Cross-referencesⁱ

Web resourcesⁱ

SeattleSNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF291820 mRNA Translation: AAF99721.1 AF241254 mRNA Translation: AAF78220.1 AY623811 mRNA Translation: AAT45083.1 AB193259 mRNA Translation: BAD99266.1 AB193260 mRNA Translation: BAD99267.1 AB046569 mRNA Translation: BAB40370.1 E39033 mRNA No translation available. GQ262784 mRNA Translation: ACT66268.1 AY358714 mRNA Translation: AAQ89076.1 AY217547 Genomic DNA Translation: AAO25651.1 CH471074 Genomic DNA Translation: EAW98892.1 BC039902 mRNA Translation: AAH39902.1 BC048094 mRNA Translation: AAH48094.2 AL110224 mRNA Translation: CAB53682.1
CCDSⁱ	CCDS14169.1 [Q9BYF1-1]
PIRⁱ	T14762
RefSeqⁱ	NP_068576.1, NM_021804.2 [Q9BYF1-1]
UniGeneⁱ	Hs.178098

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1R42	X-ray	2.20	A	1-615	[»]
	1R4L	X-ray	3.00	A	1-615	[»]
	1XJP	model	-	B	19-615	[»]
	2AJF	X-ray	2.90	A/B	19-615	[»]
	3D0G	X-ray	2.80	A/B	56-615	[»]
	3D0H	X-ray	3.10	A/B	56-615	[»]
	3D0I	X-ray	2.90	A/B	56-615	[»]
	3KBH	X-ray	3.31	A/B/C/D	19-615	[»]
	3SCI	X-ray	2.90	A/B	19-615	[»]
	3SCJ	X-ray	3.00	A/B	19-615	[»]
	3SCK	X-ray	3.00	A/B	83-615	[»]
	3SCL	X-ray	3.00	A/B	83-615	[»]
	6ACG	electron microscopy	5.40	D	19-615	[»]
	6ACJ	electron microscopy	4.20	D	19-615	[»]
	6ACK	electron microscopy	4.50	D	19-615	[»]
	6CS2	electron microscopy	4.40	D	19-615	[»]
ProteinModelPortalⁱ	Q9BYF1
SMRⁱ	Q9BYF1
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	121864, 7 interactors
DIPⁱ	DIP-44689N
IntActⁱ	Q9BYF1, 3 interactors
MINTⁱ	Q9BYF1
STRINGⁱ	9606.ENSP00000252519

Chemistry databases

BindingDBⁱ	Q9BYF1
ChEMBLⁱ	CHEMBL3736
DrugBankⁱ	DB00722 Lisinopril DB00691 Moexipril DB05203 SPP1148 DB05358 TAK-491
GuidetoPHARMACOLOGYⁱ	1614

Protein family/group databases

MEROPSⁱ	M02.006

MEROPSⁱ

M02.006

PTM databases

GlyConnectⁱ	1012
iPTMnetⁱ	Q9BYF1
PhosphoSitePlusⁱ	Q9BYF1

Polymorphism and mutation databases

BioMutaⁱ	ACE2
DMDMⁱ	71658783

Proteomic databases

PaxDbⁱ	Q9BYF1
PeptideAtlasⁱ	Q9BYF1
PRIDEⁱ	Q9BYF1
ProteomicsDBⁱ	79634 79635 [Q9BYF1-2]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000252519; ENSP00000252519; ENSG00000130234 [Q9BYF1-1] ENST00000427411; ENSP00000389326; ENSG00000130234 [Q9BYF1-1]
GeneIDⁱ	59272
KEGGⁱ	hsa:59272
UCSCⁱ	uc004cxa.2 human [Q9BYF1-1]

Organism-specific databases

CTDⁱ	59272
DisGeNETⁱ	59272
EuPathDBⁱ	HostDB:ENSG00000130234.10
GeneCardsⁱ	ACE2
HGNCⁱ	HGNC:13557 ACE2
HPAⁱ	CAB026174 HPA000288
MIMⁱ	300335 gene
neXtProtⁱ	NX_Q9BYF1
OpenTargetsⁱ	ENSG00000130234
PharmGKBⁱ	PA425
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3690 Eukaryota ENOG410XPJ3 LUCA
GeneTreeⁱ	ENSGT00520000055576
HOGENOMⁱ	HOG000292210
HOVERGENⁱ	HBG000265
InParanoidⁱ	Q9BYF1
KOⁱ	K09708
OMAⁱ	KGDFRIK
OrthoDBⁱ	EOG091G033S
PhylomeDBⁱ	Q9BYF1
TreeFamⁱ	TF312861

Enzyme and pathway databases

BRENDAⁱ	3.4.15.1 2681 3.4.17.23 2681
Reactomeⁱ	R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
SABIO-RKⁱ	Q9BYF1

Miscellaneous databases

ChiTaRSⁱ	ACE2 human
EvolutionaryTraceⁱ	Q9BYF1
GeneWikiⁱ	Angiotensin-converting_enzyme_2
GenomeRNAiⁱ	59272
PMAP-CutDBⁱ	Q9BYF1
Protein Ontology More...PROⁱ	PR:Q9BYF1
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000130234 Expressed in 129 organ(s), highest expression level in jejunal mucosa
CleanExⁱ	HS_ACE2
Genevisibleⁱ	Q9BYF1 HS

Family and domain databases

CDDⁱ	cd06461 M2_ACE, 1 hit
InterProⁱ	View protein in InterPro IPR031588 Collectrin_dom IPR001548 Peptidase_M2
PANTHERⁱ	PTHR10514 PTHR10514, 1 hit
Pfamⁱ	View protein in Pfam PF16959 Collectrin, 1 hit PF01401 Peptidase_M2, 1 hit
PRINTSⁱ	PR00791 PEPDIPTASEA
PROSITEⁱ	View protein in PROSITE PS00142 ZINC_PROTEASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACE2_HUMAN
Accessionⁱ	Q9BYF1Primary (citable) accession number: Q9BYF1 Secondary accession number(s): C7ECU1 , Q6UWP0, Q86WT0, Q9NRA7, Q9UFZ6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 2, 2005
	Last sequence update:	August 2, 2005
	Last modified:	November 7, 2018
	This is version 167 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Peptidase families
Classification of peptidase families and list of entries
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome X
Human chromosome X: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

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UniRef

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Supporting data

UniProtKB - Q9BYF1 (ACE2_HUMAN)

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Angiotensin-converting enzyme 2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Plasma membrane

Other locations

Extracellular region or secreted

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Your basket is currently empty. ⁱ

Functionⁱ

Kineticsⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ