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UniProtKB - Q9BYF1 (ACE2_HUMAN)

Entry version 170 (13 Feb 2019)
Sequence version 2 (02 Aug 2005)
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Protein

Angiotensin-converting enzyme 2

Gene

ACE2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SL6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity (By similarity).By similarity4 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<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

  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
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei169Chloride1
    Binding sitei273Substrate1
    Binding sitei345Substrate1
    Binding sitei346Substrate; via carbonyl oxygen1
    Binding sitei371Substrate1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi374Zinc; catalytic1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3751
    Metal bindingi378Zinc; catalytic1
    Metal bindingi402Zinc; catalytic1
    Binding sitei477Chloride1
    Binding sitei481Chloride1
    Active sitei5051
    Binding sitei515Substrate1

    <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

    • 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
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.4.15.1 2681
    3.4.17.23 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		Q9BYF1

    Protein family/group databases

    MEROPS protease database

    More...    MEROPSi    		M02.006

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ACE2
    ORF Names:UNQ868/PRO1885
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000130234.10

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:13557 ACE2

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		300335 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_Q9BYF1

    <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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 740ExtracellularSequence analysisAdd BLAST723
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei741 – 761HelicalSequence analysisAdd BLAST21
    Topological domaini762 – 805CytoplasmicSequence analysisAdd BLAST44

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    <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

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
    Mutagenesisi273R → Q: Does not affect amino acid transport activity of SLC6A19. 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

    DisGeNET

    More...    DisGeNETi    		59272

    Open Targets

    More...    OpenTargetsi    		ENSG00000130234

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA425

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    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

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		ACE2

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		71658783

    <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

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002857018 – 805Angiotensin-converting enzyme 2Add BLAST788
    ChainiPRO_000029226818 – 708Processed angiotensin-converting enzyme 2Add BLAST691

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi53N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi90N-linked (GlcNAc...) asparagine2 Publications1
    Glycosylationi103N-linked (GlcNAc...) asparagine1 Publication1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		Q9BYF1

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		Q9BYF1

    PeptideAtlas

    More...    PeptideAtlasi    		Q9BYF1

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q9BYF1

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		79634
    79635 [Q9BYF1-2]

    PTM databases

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		1012

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q9BYF1

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		Q9BYF1

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...    PMAP-CutDBi    		Q9BYF1

    <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

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated in failing heart.2 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000130234 Expressed in 129 organ(s), highest expression level in jejunal mucosa

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q9BYF1 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		CAB026174
    HPA000288

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with ITGB1. Interacts with the catalytically active form of TMPRSS2. Interacts with SLC6A19, this interaction is essential for expression and function of SLC6A19 in intestine (By similarity).By similarity3 Publications
    (Microbial infection) Interacts with SARS coronavirus/SARS-CoV.3 Publications
    (Microbial infection) Interacts with Human coronavirus NL63/HCoV-NL63 spike glycoprotein.1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		121864, 7 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-44689N

    Protein interaction database and analysis system

    More...    IntActi    		Q9BYF1, 3 interactors

    Molecular INTeraction database

    More...    MINTi    		Q9BYF1

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000252519

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		Q9BYF1

    <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

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

    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 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[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		Q9BYF1

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		Q9BYF1

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		Q9BYF1

    <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

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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

    <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

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG3690 Eukaryota
    ENOG410XPJ3 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000158077

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000292210

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG000265

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q9BYF1

    KEGG Orthology (KO)

    More...    KOi    		K09708

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		KGDFRIK

    Database of Orthologous Groups

    More...    OrthoDBi    		422699at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q9BYF1

    TreeFam database of animal gene trees

    More...    TreeFami    		TF312861

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd06461 M2_ACE, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR031588 Collectrin_dom
    IPR001548 Peptidase_M2

    The PANTHER Classification System

    More...    PANTHERi    		PTHR10514 PTHR10514, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF16959 Collectrin, 1 hit
    PF01401 Peptidase_M2, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00791 PEPDIPTASEA

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00142 ZINC_PROTEASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    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]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		T14762

    NCBI Reference Sequences

    More...    RefSeqi    		NP_068576.1, NM_021804.2 [Q9BYF1-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.178098

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000252519; ENSP00000252519; ENSG00000130234 [Q9BYF1-1]
    ENST00000427411; ENSP00000389326; ENSG00000130234 [Q9BYF1-1]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		59272

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:59272

    UCSC genome browser

    More...    UCSCi    		uc004cxa.2 human [Q9BYF1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <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

    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

    jPOSTiQ9BYF1
    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

    Comparative Toxicogenomics Database

    More...    CTDi    		59272
    DisGeNETi59272
    EuPathDBiHostDB:ENSG00000130234.10

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		ACE2
    HGNCiHGNC:13557 ACE2
    HPAiCAB026174
    HPA000288
    MIMi300335 gene
    neXtProtiNX_Q9BYF1
    OpenTargetsiENSG00000130234
    PharmGKBiPA425

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG3690 Eukaryota
    ENOG410XPJ3 LUCA
    GeneTreeiENSGT00940000158077
    HOGENOMiHOG000292210
    HOVERGENiHBG000265
    InParanoidiQ9BYF1
    KOiK09708
    OMAiKGDFRIK
    OrthoDBi422699at2759
    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

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...    ChiTaRSi    		ACE2 human
    EvolutionaryTraceiQ9BYF1

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		Angiotensin-converting_enzyme_2

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		59272
    PMAP-CutDBiQ9BYF1

    Protein Ontology

    More...    PROi    		PR:Q9BYF1

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

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

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACE2_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9BYF1
    Secondary accession number(s): C7ECU1
    , Q6UWP0, Q86WT0, Q9NRA7, Q9UFZ6
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2005
    Last sequence update: August 2, 2005
    Last modified: February 13, 2019
    This is version 170 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

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

    Documents

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