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Q9BYF1

- ACE2_HUMAN

UniProt

Q9BYF1 - ACE2_HUMAN

Protein

Angiotensin-converting enzyme 2

Gene

ACE2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (02 Aug 2005)
      Previous versions | rss
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    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. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.4 Publications

    Catalytic activityi

    Angiotensin II + H2O = angiotensin-1-7 + L-phenylalanine.

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication
    Binds 1 chloride ion per subunit.1 Publication

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei169 – 1691Chloride
    Binding sitei273 – 2731Substrate
    Binding sitei345 – 3451Substrate
    Binding sitei346 – 3461Substrate; via carbonyl oxygen
    Binding sitei371 – 3711Substrate
    Metal bindingi374 – 3741Zinc; catalytic
    Active sitei375 – 3751
    Metal bindingi378 – 3781Zinc; catalytic
    Metal bindingi402 – 4021Zinc; catalytic
    Binding sitei477 – 4771Chloride
    Binding sitei481 – 4811Chloride
    Active sitei505 – 5051
    Binding sitei515 – 5151Substrate

    GO - Molecular functioni

    1. carboxypeptidase activity Source: UniProtKB
    2. endopeptidase activity Source: UniProtKB
    3. glycoprotein binding Source: BHF-UCL
    4. peptide hormone binding Source: Ensembl
    5. protein binding Source: UniProtKB
    6. virus receptor activity Source: UniProtKB
    7. zinc ion binding Source: BHF-UCL

    GO - Biological processi

    1. angiotensin catabolic process in blood Source: BHF-UCL
    2. angiotensin maturation Source: Reactome
    3. angiotensin-mediated drinking behavior Source: BHF-UCL
    4. cellular protein metabolic process Source: Reactome
    5. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
    6. receptor biosynthetic process Source: BHF-UCL
    7. receptor-mediated virion attachment to host cell Source: BHF-UCL
    8. regulation of cell proliferation Source: BHF-UCL
    9. regulation of cytokine production Source: BHF-UCL
    10. regulation of inflammatory response Source: BHF-UCL
    11. regulation of systemic arterial blood pressure by renin-angiotensin Source: BHF-UCL
    12. regulation of vasoconstriction Source: BHF-UCL
    13. regulation of vasodilation Source: BHF-UCL
    14. response to virus Source: GOC
    15. viral entry into host cell Source: UniProtKB

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    Chloride, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.15.1. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKQ9BYF1.

    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
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13557. ACE2.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cytoplasm By similarity
    Note: Detected in both cell membrane and cytoplasm in neurons.By similarity

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of membrane Source: UniProtKB-KW
    6. membrane raft Source: BHF-UCL
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 263QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi31 – 311K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi37 – 371E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi38 – 381D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi41 – 411Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi68 – 681K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi82 – 843MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi110 – 1101E → P: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi135 – 1362PD → SM: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi160 – 1601E → R: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi192 – 1921R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi219 – 2191R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi239 – 2391H → Q: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi309 – 3091K → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi312 – 3121E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi324 – 3241T → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi338 – 3403NVQ → DDR: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi350 – 3501D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi353 – 3531K → H, A or D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi355 – 3551D → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi357 – 3571R → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi359 – 3591L → K or A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi383 – 3831M → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi389 – 3891P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi393 – 3931R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi425 – 4273SPD → PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi465 – 4673KGE → QDK: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi559 – 5591R → S: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
    Mutagenesisi603 – 6031F → T: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication

    Organism-specific databases

    PharmGKBiPA425.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 805788Angiotensin-converting enzyme 2PRO_0000028570Add
    BLAST
    Chaini18 – 708691Processed angiotensin-converting enzyme 2PRO_0000292268Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi53 – 531N-linked (GlcNAc...)1 Publication
    Glycosylationi90 – 901N-linked (GlcNAc...)2 Publications
    Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
    Disulfide bondi133 ↔ 1411 Publication
    Glycosylationi322 – 3221N-linked (GlcNAc...)1 Publication
    Disulfide bondi344 ↔ 3611 Publication
    Glycosylationi432 – 4321N-linked (GlcNAc...)1 Publication
    Disulfide bondi530 ↔ 5421 Publication
    Glycosylationi546 – 5461N-linked (GlcNAc...)2 Publications
    Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis

    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.
    PRIDEiQ9BYF1.

    PTM databases

    PhosphoSiteiQ9BYF1.

    Miscellaneous databases

    PMAP-CutDBQ9BYF1.

    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

    BgeeiQ9BYF1.
    CleanExiHS_ACE2.
    GenevestigatoriQ9BYF1.

    Organism-specific databases

    HPAiCAB026174.
    HPA000288.

    Interactioni

    Subunit structurei

    Interacts with ITGB1. Interacts with SARS-CoV and HCoV-NL63 spike glycoprotein. Interacts with the catalytically active form of TMPRSS2.7 Publications

    Protein-protein interaction databases

    BioGridi121864. 3 interactions.
    DIPiDIP-44689N.
    IntActiQ9BYF1. 1 interaction.
    MINTiMINT-4538816.
    STRINGi9606.ENSP00000252519.

    Structurei

    Secondary structure

    1
    805
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 5230
    Helixi56 – 7722
    Turni78 – 825
    Helixi85 – 873
    Helixi91 – 10010
    Helixi104 – 1074
    Helixi110 – 12920
    Beta strandi131 – 1344
    Beta strandi137 – 1437
    Turni144 – 1463
    Helixi148 – 1547
    Helixi158 – 17114
    Helixi173 – 19321
    Beta strandi196 – 1983
    Helixi199 – 2046
    Turni205 – 2073
    Turni213 – 2153
    Helixi220 – 25132
    Turni253 – 2553
    Beta strandi258 – 2603
    Helixi264 – 2663
    Beta strandi267 – 2715
    Helixi276 – 2783
    Helixi279 – 2824
    Turni284 – 2874
    Turni294 – 2974
    Helixi298 – 3003
    Helixi304 – 31613
    Turni317 – 3193
    Helixi327 – 3304
    Beta strandi338 – 3403
    Beta strandi347 – 3526
    Beta strandi355 – 3595
    Helixi366 – 38419
    Turni385 – 3873
    Helixi390 – 3923
    Helixi400 – 41314
    Helixi415 – 4206
    Turni422 – 4265
    Helixi432 – 44615
    Helixi449 – 46517
    Beta strandi466 – 4683
    Helixi470 – 4723
    Helixi473 – 48311
    Beta strandi486 – 4883
    Helixi499 – 5024
    Helixi504 – 5074
    Helixi514 – 53118
    Turni532 – 5343
    Helixi539 – 5413
    Helixi548 – 55811
    Turni559 – 5624
    Helixi566 – 5749
    Beta strandi575 – 5784
    Helixi582 – 59817
    Beta strandi600 – 6023
    Beta strandi607 – 6093

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ9BYF1.
    SMRiQ9BYF1. Positions 19-615.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYF1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 740723ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini762 – 80544CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei741 – 76121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 4112Interaction with SARS-CoV spike glycoproteinAdd
    BLAST
    Regioni82 – 843Interaction with SARS-CoV spike glycoprotein
    Regioni353 – 3575Interaction with SARS-CoV spike glycoprotein
    Regioni652 – 6598Essential for cleavage by ADAM17
    Regioni697 – 71620Essential for cleavage by TMPRSS11D and TMPRSS2Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71044.
    HOGENOMiHOG000292210.
    HOVERGENiHBG000265.
    InParanoidiQ9BYF1.
    KOiK09708.
    OMAiRDGANEG.
    OrthoDBiEOG76HQ13.
    PhylomeDBiQ9BYF1.
    TreeFamiTF312861.

    Family and domain databases

    InterProiIPR001548. Peptidase_M2.
    [Graphical view]
    PANTHERiPTHR10514. PTHR10514. 1 hit.
    PfamiPF01401. Peptidase_M2. 1 hit.
    [Graphical view]
    PRINTSiPR00791. PEPDIPTASEA.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    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

    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

    MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY    50
    NTNITEENVQ NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL 100
    QQNGSSVLSE DKSKRLNTIL NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE 150
    IMANSLDYNE RLWAWESWRS EVGKQLRPLY EEYVVLKNEM ARANHYEDYG 200
    DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL HAYVRAKLMN 250
    AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ 300
    AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD 350
    LGKGDFRILM CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF 400
    HEAVGEIMSL SAATPKHLKS IGLLSPDFQE DNETEINFLL KQALTIVGTL 450
    PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM KREIVGVVEP VPHDETYCDP 500
    ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH KCDISNSTEA 550
    GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK 600
    NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA 650
    MRQYFLKVKN QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV 700
    EKAIRMSRSR INDAFRLNDN SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM 750
    GVIVVGIVIL IFTGIRDRKK KNKARSGENP YASIDISKGE NNPGFQNTDD 800
    VQTSF 805
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181Q → H in CAB53682. (PubMed:17974005)Curated
    Sequence conflicti508 – 5081N → D in AAQ89076. (PubMed:12975309)Curated
    Sequence conflicti631 – 6311K → R in BAB40370. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261K → R.1 Publication
    Corresponds to variant rs4646116 [ dbSNP | Ensembl ].
    VAR_023082
    Natural varianti638 – 6381N → S.1 Publication
    Corresponds to variant rs183135788 [ dbSNP | Ensembl ].
    VAR_023083

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei555 – 5551F → L in isoform 2. 1 PublicationVSP_014901
    Alternative sequencei556 – 805250Missing in isoform 2. 1 PublicationVSP_014902Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.1. human. [Q9BYF1-1]

    Polymorphism databases

    DMDMi71658783.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q9BYF1.
    SMRi Q9BYF1. Positions 19-615.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121864. 3 interactions.
    DIPi DIP-44689N.
    IntActi Q9BYF1. 1 interaction.
    MINTi MINT-4538816.
    STRINGi 9606.ENSP00000252519.

    Chemistry

    BindingDBi Q9BYF1.
    ChEMBLi CHEMBL2096989.
    DrugBanki DB00691. Moexipril.
    GuidetoPHARMACOLOGYi 1614.

    Protein family/group databases

    MEROPSi M02.006.

    PTM databases

    PhosphoSitei Q9BYF1.

    Polymorphism databases

    DMDMi 71658783.

    Proteomic databases

    PaxDbi Q9BYF1.
    PRIDEi Q9BYF1.

    Protocols and materials databases

    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.1. human. [Q9BYF1-1 ]

    Organism-specific databases

    CTDi 59272.
    GeneCardsi GC0XM015489.
    HGNCi HGNC:13557. ACE2.
    HPAi CAB026174.
    HPA000288.
    MIMi 300335. gene.
    neXtProti NX_Q9BYF1.
    PharmGKBi PA425.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71044.
    HOGENOMi HOG000292210.
    HOVERGENi HBG000265.
    InParanoidi Q9BYF1.
    KOi K09708.
    OMAi RDGANEG.
    OrthoDBi EOG76HQ13.
    PhylomeDBi Q9BYF1.
    TreeFami TF312861.

    Enzyme and pathway databases

    BRENDAi 3.4.15.1. 2681.
    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RK Q9BYF1.

    Miscellaneous databases

    ChiTaRSi ACE2. human.
    EvolutionaryTracei Q9BYF1.
    GeneWikii Angiotensin-converting_enzyme_2.
    GenomeRNAii 59272.
    NextBioi 65154.
    PMAP-CutDB Q9BYF1.
    PROi Q9BYF1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BYF1.
    CleanExi HS_ACE2.
    Genevestigatori Q9BYF1.

    Family and domain databases

    InterProi IPR001548. Peptidase_M2.
    [Graphical view ]
    PANTHERi PTHR10514. PTHR10514. 1 hit.
    Pfami PF01401. Peptidase_M2. 1 hit.
    [Graphical view ]
    PRINTSi PR00791. PEPDIPTASEA.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
      Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
      Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, ENZYME REGULATION.
      Tissue: Heart.
    2. "A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
      Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
      J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ENZYME REGULATION.
      Tissue: Lymphoma.
    3. "The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is selectively expressed by adult Leydig cells of the testis."
      Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A., Smith A.I., Lew R.A.
      Endocrinology 145:4703-4711(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION.
      Tissue: Testis.
    4. "Identification of an alternative 5'-untranslated exon and new polymorphisms of angiotensin-converting enzyme 2 gene: lack of association with SARS in the Vietnamese population."
      Itoyama S., Keicho N., Hijikata M., Quy T., Phi N.C., Long H.T., Ha L.D., Ban V.V., Matsushita I., Yanai H., Kirikae F., Kirikae T., Kuratsuji T., Sasazuki T.
      Am. J. Med. Genet. A 136:52-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-638.
      Tissue: Lung and Testis.
    5. "Cloning, expression analysis and chromosomal localization of a novel ACE like enzyme."
      Suzuki Y., Watanabe M., Sugano S.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "MPROT15 polypeptide and MPROT15 polynucleotide."
      Southan C., Burgess N.
      Patent number JP11318472, 24-NOV-1999
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    7. "Comparative susceptibility to SARS-CoV mediated by ACE2 protein of 15 different species."
      Li K.K.B., Yip C.W., Hon C.C., Lam C.Y., Leung F.C.C.
      Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    9. SeattleSNPs variation discovery resource
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-26.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain and Testis.
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-805 (ISOFORM 1).
      Tissue: Testis.
    13. "Interaction of ACE2 and integrin beta1 in failing human heart."
      Lin Q., Keller R.S., Weaver B., Zisman L.S.
      Biochim. Biophys. Acta 1689:175-178(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 679-689, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ITGB1.
    14. "Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme."
      Harmer D., Gilbert M., Borman R., Clark K.L.
      FEBS Lett. 532:107-110(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    15. "Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
      Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
      J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.
    16. "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus."
      Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A., Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H., Farzan M.
      Nature 426:450-454(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "ACE2 gene expression is up-regulated in the human failing heart."
      Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.
      BMC Med. 2:19-19(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    18. "Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis."
      Hamming I., Timens W., Bulthuis M.L.C., Lely A.T., Navis G.J., van Goor H.
      J. Pathol. 203:631-637(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    19. "Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2."
      Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M., Sullivan J.L., Farzan M., Choe H.
      J. Virol. 78:11429-11433(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN.
    20. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90.
      Tissue: Bile.
    21. Cited for: TISSUE SPECIFICITY, INDUCTION.
    22. Cited for: INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, MUTAGENESIS.
    23. "Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2)."
      Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T., Smith A.I., Hooper N.M., Turner A.J.
      J. Biol. Chem. 280:30113-30119(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE.
    24. "Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry."
      Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B., Poehlmann S.
      Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCOV-NL63 SPIKE GLYCOPROTEIN.
    25. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
      Tissue: Liver.
    26. "Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints."
      Lai Z.W., Hanchapola I., Steer D.L., Smith A.I.
      Biochemistry 50:5182-5194(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE.
    27. "A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry."
      Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S., Gallagher T.
      J. Virol. 85:873-882(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, INTERACTION WITH TMPRSS2.
    28. "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
      Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
      J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
    29. "ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis."
      Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T., Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A., Pantoliano M.W.
      J. Biol. Chem. 279:17996-18007(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-615, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-615 IN COMPLEX WITH MLN-4760, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND ASN-546.

    Entry informationi

    Entry nameiACE2_HUMAN
    AccessioniPrimary (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: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [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. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3