Protein detail

ACE2

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]

Protein symbol
ACE2
UniProt ID
EVMP score
0.38
Frequency
Transmembrane count
1
Protein classification
EnzymesMetabolic proteinsPredicted membrane proteinsPredicted secreted proteinsTransporters
Basic Information
Protein Names
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]
Protein Class
EnzymesMetabolic proteinsPredicted membrane proteinsPredicted secreted proteinsTransporters
Protein Function
  • Transporters:Electrochemical Potential-driven transporters
  • Enzymes
  • Predicted secreted proteins
  • Transporters:Accessory Factors Involved in Transport
  • ENZYME proteins:Hydrolases
  • Peptidases:Metallopeptidases
Transmembrane
741..761; Helical
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
ACEH
Gene Description
Angiotensin converting enzyme 2
Chromosome
X
Position
15494566-15607236
EVMP Score
0.38
Fluorescence & Localization
Cell SpecificErythrocyte progenitorsSecretome LocationSecreted to bloodSecretome FunctionEnzyme
Function & Pathway
Protein Function
  • Transporters:Electrochemical Potential-driven transporters
  • Enzymes
  • Predicted secreted proteins
  • Transporters:Accessory Factors Involved in Transport
  • ENZYME proteins:Hydrolases
  • Peptidases:Metallopeptidases
Canonical Pathways
M209 Pid p38 gamma delta pathway
Mediation Categories
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

1 record.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ACE2CSNK2A1P68400S787phosphorylationPhosphoSite

Ligand-Receptor Signaling

36 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorOmniPathNoYesYesYesNo
extracellularextracellularOmniPathNoNoYesYesNo
intracellularintracellularLOCATENoNoYesYesNo
intracellularintracellularGO_IntercellNoNoYesYesNo
intracellularintracellularOmniPathNoNoYesYesNo
intracellularintracellularUniProt_locationNoNoYesYesNo
cell_adhesioncell_adhesionCellinkerYesYesYesYesNo
adhesionadhesionOmniPathYesYesYesYesNo
cell_adhesioncell_adhesionOmniPathYesYesYesYesNo
transmembranetransmembraneUniProt_locationNoNoYesYesNo
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Regulatory Interaction Network

3 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
ACE2Q9BYF1ANGTP01019YesYesNoSIGNORHPRDHINTIntActInnateDBHPRD:11815627SIGNOR:11815627HINT:10969042IntAct:11815627HPRD:10969042InnateDB:10969042HINT:15283675IntAct:10969042
ACE2Q9BYF1APELQ9ULZ1YesYesNoSIGNORSIGNOR:11815627
CSK21P68400ACE2Q9BYF1YesNoNoPhosphoSitePhosphoSite_ProtMapperProtMapperPhosphoSite:20484496

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyImmunoaffinity CaptureR SequencingMass spectrometry6381689063940901530646616383215353519496532089743
Sequence, Structure & Domains

Sequences

Length
805
Mass
92,463
Sequence
MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=long; IsoId=Q9BYF1-1; Sequence=Displayed; Name=2; Synonyms=delta, dACE2, short; IsoId=Q9BYF1-3; Sequence=VSP_060903
Alternative Sequence
1..356; MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDF -> MREAGWDKGG (in isoform 2)

3D Structural Models

Turn
104..107; 144..146; 193..195; 213..215; 253..255; 284..287; 426..428; 559..562; 612..615
Helix
21..52; 56..79; 80..82; 85..87; 91..102; 110..129; 147..154; 158..171; 173..192; 199..204; 205..207; 219..251; 264..266; 276..278; 279..282; 294..299; 304..317; 325..330; 366..384; 385..387; 390..392; 400..412; 415..420; 432..465; 470..472; 473..483; 500..502; 504..507; 514..532; 539..541; 548..558; 566..574; 582..587; 589..598; 599..601; 624..627; 637..657; 667..669; 697..706; 708..715; 741..765
Beta Strand
131..133; 135..139; 141..143; 196..198; 258..260; 267..273; 332..334; 338..340; 347..352; 355..359; 396..399; 422..424; 466..468; 486..488; 494..496; 534..537; 575..578; 607..609; 618..622; 629..631; 670..673; 677..686; 690..694; 719..724
3D Structure
Electron microscopy (245); NMR spectroscopy (1); X-ray crystallography (74)

Domain & Motif Annotations

Compositional Bias
789..805; Polar residues
Motif
778..786; LIR; 781..785; SH2-binding; 781..784; Endocytic sorting signal; 792..795; PTB; 803..805; PDZ-binding
Domain (CC)
The extracellular region of the ACE2 enzyme is composed of two domains. The first is a zinc metallopeptidase domain (residues 19-611). The second domain is located at the C-terminus (residues 612-740) and is 48% identical to human collectrin.; DOMAIN: The cytoplasmic tail contains several linear motifs such as LIR, PDZ-binding, PTB and endocytic sorting signal motifs that would allow interaction with proteins that mediate endocytic trafficking and autophagy.
Domain (FT)
19..607; Peptidase M2; 614..805; Collectrin-like
Region
30..41; Interaction with SARS-CoV spike glycoprotein; 82..84; Interaction with SARS-CoV spike glycoprotein; 353..357; Interaction with SARS-CoV spike glycoprotein; 652..659; Essential for cleavage by ADAM17; 697..716; Essential for cleavage by TMPRSS11D and TMPRSS2; 772..805; Disordered
Protein Families
Peptidase M2 family
Sequence Similarities
Belongs to the peptidase M2 family.
Clinical Relevance
Biomarker
Phase 1/2; Phase 2; Phase 1; Discontinued in Phase 1; Investigative
Interaction Protein
ENSG00000026025ENSG00000044574ENSG00000109062ENSG00000143376ENSG00000150093ENSG00000161681ENSG00000164082ENSG00000174358ENSG00000174827ENSG00000184012
Interaction Count
10
Interaction Dataset
intact_biogrid