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Protein

Angiotensin-converting enzyme 2

Gene

ACE2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

  1. KM=6.9 µM for angiotensin I1 Publication
  2. KM=2 µM for angiotensin II1 Publication
  3. KM=6.8 µM for apelin-131 Publication
  4. KM=5.5 µM for dynorphin-131 Publication

    pH dependencei

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei169Chloride1
    Binding sitei273Substrate1
    Binding sitei345Substrate1
    Binding sitei346Substrate; via carbonyl oxygen1
    Binding sitei371Substrate1
    Metal bindingi374Zinc; catalytic1
    Active sitei3751
    Metal bindingi378Zinc; catalytic1
    Metal bindingi402Zinc; catalytic1
    Binding sitei477Chloride1
    Binding sitei481Chloride1
    Active sitei5051
    Binding sitei515Substrate1

    GO - Molecular functioni

    • carboxypeptidase activity Source: UniProtKB
    • endopeptidase activity Source: UniProtKB
    • exopeptidase activity Source: GO_Central
    • metallocarboxypeptidase activity Source: Reactome
    • virus receptor activity Source: BHF-UCL
    • zinc ion binding Source: BHF-UCL

    GO - Biological processi

    Keywordsi

    Molecular functionCarboxypeptidase, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor
    Biological processHost-virus interaction
    LigandChloride, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.15.1 2681
    3.4.17.23 2681
    ReactomeiR-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
    SABIO-RKiQ9BYF1

    Protein family/group databases

    MEROPSiM02.006

    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:
    Gene namesi
    Name:ACE2
    ORF Names:UNQ868/PRO1885
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000130234.10
    HGNCiHGNC:13557 ACE2
    MIMi300335 gene
    neXtProtiNX_Q9BYF1

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini18 – 740ExtracellularSequence analysisAdd BLAST723
    Transmembranei741 – 761HelicalSequence analysisAdd BLAST21
    Topological domaini762 – 805CytoplasmicSequence analysisAdd BLAST44

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi24 – 26QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi31K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi37E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi38D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi41Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi68K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi82 – 84MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi110E → P: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi135 – 136PD → SM: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication2
    Mutagenesisi160E → R: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi192R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi219R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi239H → Q: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi309K → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi312E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi324T → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi338 – 340NVQ → DDR: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi350D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi353K → H, A or D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi355D → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi357R → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi359L → K or A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi383M → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi389P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi393R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi425 – 427SPD → PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi465 – 467KGE → QDK: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi559R → S: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi603F → T: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1

    Organism-specific databases

    DisGeNETi59272
    OpenTargetsiENSG00000130234
    PharmGKBiPA425

    Chemistry databases

    ChEMBLiCHEMBL3736
    DrugBankiDB00722 Lisinopril
    DB00691 Moexipril
    DB05203 SPP1148
    DB05358 TAK-491
    GuidetoPHARMACOLOGYi1614

    Polymorphism and mutation databases

    BioMutaiACE2
    DMDMi71658783

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 17Sequence analysisAdd BLAST17
    ChainiPRO_000002857018 – 805Angiotensin-converting enzyme 2Add BLAST788
    ChainiPRO_000029226818 – 708Processed angiotensin-converting enzyme 2Add BLAST691

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi53N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi90N-linked (GlcNAc...) asparagine2 Publications1
    Glycosylationi103N-linked (GlcNAc...) asparagine1 Publication1
    Disulfide bondi133 ↔ 1411 Publication
    Glycosylationi322N-linked (GlcNAc...) asparagine1 Publication1
    Disulfide bondi344 ↔ 3611 Publication
    Glycosylationi432N-linked (GlcNAc...) asparagine1 Publication1
    Disulfide bondi530 ↔ 5421 Publication
    Glycosylationi546N-linked (GlcNAc...) asparagine2 Publications1
    Glycosylationi690N-linked (GlcNAc...) asparagineSequence analysis1

    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

    PaxDbiQ9BYF1
    PeptideAtlasiQ9BYF1
    PRIDEiQ9BYF1
    ProteomicsDBi79634
    79635 [Q9BYF1-2]

    PTM databases

    GlyConnecti1012
    iPTMnetiQ9BYF1
    PhosphoSitePlusiQ9BYF1

    Miscellaneous databases

    PMAP-CutDBiQ9BYF1

    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

    Up-regulated in failing heart.2 Publications

    Gene expression databases

    BgeeiENSG00000130234 Expressed in 129 organ(s), highest expression level in jejunal mucosa
    CleanExiHS_ACE2
    GenevisibleiQ9BYF1 HS

    Organism-specific databases

    HPAiCAB026174
    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

    WithEntry#Exp.IntActNotes
    SQ6Q1S23EBI-15814450,EBI-15814420From Human coronavirus NL63.

    Protein-protein interaction databases

    BioGridi121864, 7 interactors
    DIPiDIP-44689N
    IntActiQ9BYF1, 3 interactors
    MINTiQ9BYF1
    STRINGi9606.ENSP00000252519

    Chemistry databases

    BindingDBiQ9BYF1

    Structurei

    Secondary structure

    1805
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliQ9BYF1
    SMRiQ9BYF1
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYF1

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni30 – 41Interaction with SARS-CoV spike glycoproteinAdd BLAST12
    Regioni82 – 84Interaction with SARS-CoV spike glycoprotein3
    Regioni353 – 357Interaction with SARS-CoV spike glycoprotein5
    Regioni652 – 659Essential for cleavage by ADAM178
    Regioni697 – 716Essential for cleavage by TMPRSS11D and TMPRSS2Add BLAST20

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG3690 Eukaryota
    ENOG410XPJ3 LUCA
    GeneTreeiENSGT00520000055576
    HOGENOMiHOG000292210
    HOVERGENiHBG000265
    InParanoidiQ9BYF1
    KOiK09708
    OMAiKGDFRIK
    OrthoDBiEOG091G033S
    PhylomeDBiQ9BYF1
    TreeFamiTF312861

    Family and domain databases

    CDDicd06461 M2_ACE, 1 hit
    InterProiView protein in InterPro
    IPR031588 Collectrin_dom
    IPR001548 Peptidase_M2
    PANTHERiPTHR10514 PTHR10514, 1 hit
    PfamiView protein in Pfam
    PF16959 Collectrin, 1 hit
    PF01401 Peptidase_M2, 1 hit
    PRINTSiPR00791 PEPDIPTASEA
    PROSITEiView 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. AlignAdd to basket
    Isoform 1 (identifier: Q9BYF1-1) [UniParc]FASTAAdd 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]FASTAAdd to basket

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

    Note: No experimental confirmation available.
    Show »
    Length:555
    Mass (Da):63,912
    Checksum:i3A3842AB792E2DBC
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti18Q → H in CAB53682 (PubMed:17974005).Curated1
    Sequence conflicti508N → D in AAQ89076 (PubMed:12975309).Curated1
    Sequence conflicti631K → R in BAB40370 (Ref. 5) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_02308226K → R1 PublicationCorresponds to variant dbSNP:rs4646116Ensembl.1
    Natural variantiVAR_023083638N → S1 PublicationCorresponds to variant dbSNP:rs183135788Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_014901555F → L in isoform 2. 1 Publication1
    Alternative sequenceiVSP_014902556 – 805Missing in isoform 2. 1 PublicationAdd BLAST250

    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
    CCDSiCCDS14169.1 [Q9BYF1-1]
    PIRiT14762
    RefSeqiNP_068576.1, NM_021804.2 [Q9BYF1-1]
    UniGeneiHs.178098

    Genome annotation databases

    EnsembliENST00000252519; ENSP00000252519; ENSG00000130234 [Q9BYF1-1]
    ENST00000427411; ENSP00000389326; ENSG00000130234 [Q9BYF1-1]
    GeneIDi59272
    KEGGihsa:59272
    UCSCiuc004cxa.2 human [Q9BYF1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Similar proteinsi

    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
    CCDSiCCDS14169.1 [Q9BYF1-1]
    PIRiT14762
    RefSeqiNP_068576.1, NM_021804.2 [Q9BYF1-1]
    UniGeneiHs.178098

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1R42X-ray2.20A1-615[»]
    1R4LX-ray3.00A1-615[»]
    1XJPmodel-B19-615[»]
    2AJFX-ray2.90A/B19-615[»]
    3D0GX-ray2.80A/B56-615[»]
    3D0HX-ray3.10A/B56-615[»]
    3D0IX-ray2.90A/B56-615[»]
    3KBHX-ray3.31A/B/C/D19-615[»]
    3SCIX-ray2.90A/B19-615[»]
    3SCJX-ray3.00A/B19-615[»]
    3SCKX-ray3.00A/B83-615[»]
    3SCLX-ray3.00A/B83-615[»]
    6ACGelectron microscopy5.40D19-615[»]
    6ACJelectron microscopy4.20D19-615[»]
    6ACKelectron microscopy4.50D19-615[»]
    6CS2electron microscopy4.40D19-615[»]
    ProteinModelPortaliQ9BYF1
    SMRiQ9BYF1
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi121864, 7 interactors
    DIPiDIP-44689N
    IntActiQ9BYF1, 3 interactors
    MINTiQ9BYF1
    STRINGi9606.ENSP00000252519

    Chemistry databases

    BindingDBiQ9BYF1
    ChEMBLiCHEMBL3736
    DrugBankiDB00722 Lisinopril
    DB00691 Moexipril
    DB05203 SPP1148
    DB05358 TAK-491
    GuidetoPHARMACOLOGYi1614

    Protein family/group databases

    MEROPSiM02.006

    PTM databases

    GlyConnecti1012
    iPTMnetiQ9BYF1
    PhosphoSitePlusiQ9BYF1

    Polymorphism and mutation databases

    BioMutaiACE2
    DMDMi71658783

    Proteomic databases

    PaxDbiQ9BYF1
    PeptideAtlasiQ9BYF1
    PRIDEiQ9BYF1
    ProteomicsDBi79634
    79635 [Q9BYF1-2]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000252519; ENSP00000252519; ENSG00000130234 [Q9BYF1-1]
    ENST00000427411; ENSP00000389326; ENSG00000130234 [Q9BYF1-1]
    GeneIDi59272
    KEGGihsa:59272
    UCSCiuc004cxa.2 human [Q9BYF1-1]

    Organism-specific databases

    CTDi59272
    DisGeNETi59272
    EuPathDBiHostDB:ENSG00000130234.10
    GeneCardsiACE2
    HGNCiHGNC:13557 ACE2
    HPAiCAB026174
    HPA000288
    MIMi300335 gene
    neXtProtiNX_Q9BYF1
    OpenTargetsiENSG00000130234
    PharmGKBiPA425
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3690 Eukaryota
    ENOG410XPJ3 LUCA
    GeneTreeiENSGT00520000055576
    HOGENOMiHOG000292210
    HOVERGENiHBG000265
    InParanoidiQ9BYF1
    KOiK09708
    OMAiKGDFRIK
    OrthoDBiEOG091G033S
    PhylomeDBiQ9BYF1
    TreeFamiTF312861

    Enzyme and pathway databases

    BRENDAi3.4.15.1 2681
    3.4.17.23 2681
    ReactomeiR-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
    SABIO-RKiQ9BYF1

    Miscellaneous databases

    ChiTaRSiACE2 human
    EvolutionaryTraceiQ9BYF1
    GeneWikiiAngiotensin-converting_enzyme_2
    GenomeRNAii59272
    PMAP-CutDBiQ9BYF1
    PROiPR:Q9BYF1
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000130234 Expressed in 129 organ(s), highest expression level in jejunal mucosa
    CleanExiHS_ACE2
    GenevisibleiQ9BYF1 HS

    Family and domain databases

    CDDicd06461 M2_ACE, 1 hit
    InterProiView protein in InterPro
    IPR031588 Collectrin_dom
    IPR001548 Peptidase_M2
    PANTHERiPTHR10514 PTHR10514, 1 hit
    PfamiView protein in Pfam
    PF16959 Collectrin, 1 hit
    PF01401 Peptidase_M2, 1 hit
    PRINTSiPR00791 PEPDIPTASEA
    PROSITEiView protein in PROSITE
    PS00142 ZINC_PROTEASE, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACE2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYF1
    Secondary accession number(s): C7ECU1
    , Q6UWP0, Q86WT0, Q9NRA7, Q9UFZ6
    Entry historyiIntegrated 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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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

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