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UniProtKB - P12821 (ACE_HUMAN)

Protein

Angiotensin-converting enzyme

Gene

ACE

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

Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.

Miscellaneous

Inhibitors of ACE are commonly used to treat hypertension and some types of renal and cardiac dysfunction.
The glycosidase activity probably uses different active site residues than the metalloprotease activity.

<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

  • Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II. EC:3.4.15.1

<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:

Cofactori (for Isoform Testis-specific)

Zn2+Note: Isoform Testis-specific only binds 1 Zn2+ ion per subunit.

<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

Strongly activated by chloride. Specifically inhibited by lisinopril, captopril and enalaprilat.

<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=2.51 mM for Hip-His-Leu2 Publications

    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 sitei231Chloride 11
    <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 bindingi390Zinc 1; catalytic1 Publication1
    <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 sitei39111
    Metal bindingi394Zinc 1; catalytic1 Publication1
    Metal bindingi418Zinc 1; catalytic1 Publication1
    Binding sitei529Chloride 11
    Binding sitei791Chloride 21
    Binding sitei829Chloride 31
    Metal bindingi988Zinc 2; catalytic1 Publication1
    Active sitei98921
    Metal bindingi992Zinc 2; catalytic1 Publication1
    Metal bindingi1016Zinc 2; catalytic1 Publication1
    Binding sitei1090Chloride 21
    Binding sitei1094Chloride 21
    Binding sitei1127Chloride 31

    <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

    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, Hydrolase, Metalloprotease, Protease
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:HS08412-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.4.15.1 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    		P12821

    SignaLink: a signaling pathway resource with multi-layered regulatory networks

    More...    SignaLinki    		P12821

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		P12821

    Protein family/group databases

    MEROPS protease database

    More...    MEROPSi    		M02.001

    <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 (EC:3.2.1.-, EC:3.4.15.1)
    Short name:
    ACE
    Alternative name(s):
    Dipeptidyl carboxypeptidase I
    Kininase II
    CD_antigen: CD143
    Cleaved into the following chain:
    Angiotensin-converting enzyme, soluble form
    <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:ACE
    Synonyms:DCP, DCP1
    <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 17

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000159640.15

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:2707 ACE

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		106180 gene+phenotype

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P12821

    <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; 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 domaini30 – 1256ExtracellularSequence analysisAdd BLAST1227
    <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>Transmembranei1257 – 1277HelicalSequence analysisAdd BLAST21
    Topological domaini1278 – 1306CytoplasmicSequence analysisAdd BLAST29

    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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Ischemic stroke (ISCHSTR)1 Publication
    Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Disease descriptionA stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
    See also OMIM:601367
    Renal tubular dysgenesis (RTD)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAutosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).
    See also OMIM:267430
    Microvascular complications of diabetes 3 (MVCD3)1 Publication
    Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Disease descriptionPathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
    See also OMIM:612624
    Intracerebral hemorrhage (ICH)1 Publication
    Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Disease descriptionA pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.
    See also OMIM:614519

    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>Mutagenesisi1299S → A: Abolishes phosphorylation and decreases membrane retention. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		1636

    MalaCards human disease database

    More...    MalaCardsi    		ACE
    MIMi106180 gene+phenotype
    267430 phenotype
    601367 phenotype
    612624 phenotype
    614519 phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000159640

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...    Orphaneti    		34145 NON RARE IN EUROPE: Berger disease
    97369 Renal tubular dysgenesis of genetic origin

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA139

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL1808

    Drug and drug target database

    More...    DrugBanki    		DB02032 1-(3-Mercapto-2-Methyl-Propionyl)-Pyrrolidine-2-Carboxylic Acid
    DB00542 Benazepril
    DB00616 Candoxatril
    DB01197 Captopril
    DB01340 Cilazapril
    DB00584 Enalapril
    DB09477 Enalaprilat
    DB00492 Fosinopril
    DB00722 Lisinopril
    DB00691 Moexipril
    DB03740 N-acetyl-alpha-D-glucosamine
    DB00886 Omapatrilat
    DB00790 Perindopril
    DB00881 Quinapril
    DB00178 Ramipril
    DB01180 Rescinnamine
    DB01348 Spirapril
    DB08836 Temocapril
    DB00519 Trandolapril
    DB13166 Zofenopril

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		1613

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		ACE

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		113045

    <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 – 291 PublicationAdd BLAST29
    <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_000002853030 – 1306Angiotensin-converting enzymeAdd BLAST1277
    ChainiPRO_000002853130 – 1232Angiotensin-converting enzyme, soluble formAdd BLAST1203
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000285321233 – 1306Removed in soluble formAdd BLAST74

    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>Glycosylationi38N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi54N-linked (GlcNAc...) asparagine2 Publications1
    Glycosylationi74N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi111N-linked (GlcNAc...) asparagine2 Publications1
    Glycosylationi146N-linked (GlcNAc...) asparagine2 Publications1
    <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 bondi157 ↔ 1651 Publication
    Glycosylationi160N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi318N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi445N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi509N-linked (GlcNAc...) asparagine3 Publications1
    Glycosylationi677N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi695N-linked (GlcNAc...) (complex) asparagine2 Publications1
    Glycosylationi714N-linked (GlcNAc...) (complex) asparagine3 Publications1
    Disulfide bondi757 ↔ 7631 Publication
    Glycosylationi760N-linked (GlcNAc...) asparagine; partial1 Publication1
    Glycosylationi942N-linked (GlcNAc...) asparagine; partial1 Publication1
    Disulfide bondi957 ↔ 9751 Publication
    Disulfide bondi1143 ↔ 11551 Publication
    Glycosylationi1191N-linked (GlcNAc...) asparagine; partial1 Publication1
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1299Phosphoserine1 Publication1

    <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

    Phosphorylated by CK2 on Ser-1299; which allows membrane retention.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1225Not glycosylated1 Publication1

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P12821

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P12821

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

    More...    PaxDbi    		P12821

    PeptideAtlas

    More...    PeptideAtlasi    		P12821

    PRoteomics IDEntifications database

    More...    PRIDEi    		P12821

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		52874
    52875 [P12821-2]
    52876 [P12821-3]
    52877 [P12821-4]

    PTM databases

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		1011

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P12821

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

    More...    PhosphoSitePlusi    		P12821

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...    PMAP-CutDBi    		P12821

    <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

    Ubiquitously expressed, with highest levels in lung, kidney, heart, gastrointestinal system and prostate. Isoform Testis-specific is expressed in spermatocytes and adult testis.4 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    		ENSG00000159640 Expressed in 115 organ(s), highest expression level in testis

    CleanEx database of gene expression profiles

    More...    CleanExi    		HS_ACE

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P12821 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P12821 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		CAB002426
    CAB002921
    HPA029298
    HPA069790

    <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

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		108004, 8 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		P12821

    Protein interaction database and analysis system

    More...    IntActi    		P12821, 1 interactor

    Molecular INTeraction database

    More...    MINTi    		P12821

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000290866

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P12821

    <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

    11306
    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
    1O86X-ray2.00A642-1230[»]
    1O8AX-ray2.00A642-1230[»]
    1UZEX-ray1.82A642-1230[»]
    1UZFX-ray2.00A642-1230[»]
    2C6FX-ray3.01A/B30-641[»]
    2C6NX-ray3.00A/B30-641[»]
    2IULX-ray2.01A642-1232[»]
    2IUXX-ray2.80A642-1232[»]
    2OC2X-ray2.25A642-1232[»]
    2XY9X-ray1.97A645-1228[»]
    2XYDX-ray2.15A/B30-639[»]
    2YDMX-ray2.44A642-1230[»]
    3BKKX-ray2.17A642-1232[»]
    3BKLX-ray2.18A642-1232[»]
    3L3NX-ray2.30A642-1232[»]
    3NXQX-ray1.99A/B30-658[»]
    4APHX-ray1.99A642-1230[»]
    4APJX-ray2.60A642-1230[»]
    4BXKX-ray2.20A/B30-657[»]
    4BZRX-ray1.84A642-1230[»]
    4BZSX-ray2.10A/B30-657[»]
    4C2NX-ray2.59A642-1230[»]
    4C2OX-ray1.80A642-1230[»]
    4C2PX-ray1.99A642-1230[»]
    4C2QX-ray2.40A642-1230[»]
    4C2RX-ray2.30A642-1230[»]
    4CA5X-ray1.85A642-1230[»]
    4CA6X-ray1.91A/B30-639[»]
    4UFAX-ray1.80A/B30-657[»]
    4UFBX-ray1.80A/B/C/D30-657[»]
    5AM8X-ray1.90A/B/C/D30-658[»]
    5AM9X-ray1.80A/B/C/D30-658[»]
    5AMAX-ray1.80A/B/C/D30-658[»]
    5AMBX-ray1.55A/B30-658[»]
    5AMCX-ray1.65A/B30-658[»]
    6EN5X-ray1.75A/B/C/D30-657[»]
    6EN6X-ray1.80A/B/C/D30-657[»]
    6F9RX-ray1.85A/B30-657[»]
    6F9TX-ray1.60A642-1232[»]
    6F9UX-ray1.90A642-1232[»]
    6F9VX-ray1.69A/B30-657[»]
    6H5WX-ray1.37A642-1232[»]
    6H5XX-ray1.80A/B30-657[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P12821

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

    More...    SMRi    		P12821

    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    		P12821

    <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 – 630Peptidase M2 1Add BLAST601
    Regioni631 – 1232Peptidase M2 2Add BLAST602

    <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

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG3690 Eukaryota
    ENOG410XPJ3 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000162051

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000007838

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG000264

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P12821

    KEGG Orthology (KO)

    More...    KOi    		K01283

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		VTMEQLF

    Database of Orthologous Groups

    More...    OrthoDBi    		238880at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P12821

    TreeFam database of animal gene trees

    More...    TreeFami    		TF312861

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd06461 M2_ACE, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001548 Peptidase_M2

    The PANTHER Classification System

    More...    PANTHERi    		PTHR10514 PTHR10514, 2 hits

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01401 Peptidase_M2, 2 hits

    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, 2 hits

    <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 (4+)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 4 <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

    This entry has 4 described isoforms and 9 potential isoforms that are computationally mapped.Show allAlign All

    Isoform Somatic-1 (identifier: P12821-1) [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
    MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA 
            60         70         80         90        100
    QSYNSSAEQV LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK 
           110        120        130        140        150
    AKELYEPIWQ NFTDPQLRRI IGAVRTLGSA NLPLAKRQQY NALLSNMSRI 
           160        170        180        190        200
    YSTAKVCLPN KTATCWSLDP DLTNILASSR SYAMLLFAWE GWHNAAGIPL 
           210        220        230        240        250
    KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL EHLYQQLEPL 
           260        270        280        290        300
    YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF 
           310        320        330        340        350
    PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK 
           360        370        380        390        400
    PADGREVVCH ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ 
           410        420        430        440        450
    YKDLPVSLRR GANPGFHEAI GDVLALSVST PEHLHKIGLL DRVTNDTESD 
           460        470        480        490        500
    INYLLKMALE KIAFLPFGYL VDQWRWGVFS GRTPPSRYNF DWWYLRTKYQ 
           510        520        530        540        550
    GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF HEALCKEAGY 
           560        570        580        590        600
    EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL 
           610        620        630        640        650
    KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS 
           660        670        680        690        700
    KFVEEYDRTS QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY 
           710        720        730        740        750
    GTQARKFDVN QLQNTTIKRI IKKVQDLERA ALPAQELEEY NKILLDMETT 
           760        770        780        790        800
    YSVATVCHPN GSCLQLEPDL TNVMATSRKY EDLLWAWEGW RDKAGRAILQ 
           810        820        830        840        850
    FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER LFQELQPLYL 
           860        870        880        890        900
    NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS 
           910        920        930        940        950
    APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT 
           960        970        980        990       1000
    DGREVVCHAS AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK 
          1010       1020       1030       1040       1050
    DLPVALREGA NPGFHEAIGD VLALSVSTPK HLHSLNLLSS EGGSDEHDIN 
          1060       1070       1080       1090       1100
    FLMKMALDKI AFIPFSYLVD QWRWRVFDGS ITKENYNQEW WSLRLKYQGL 
          1110       1120       1130       1140       1150
    CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE ALCQAAGHTG 
          1160       1170       1180       1190       1200
    PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY 
          1210       1220       1230       1240       1250
    FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL 
          1260       1270       1280       1290       1300
    DAQQARVGQW LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE 

    VELRHS
    Length:1,306
    Mass (Da):149,715
    Last modified:October 1, 1989 - v1
    <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:i1B33BCA7301A26AA
    GO
    Isoform Somatic-2 (identifier: P12821-2) [UniParc]FASTAAdd to basket
    Also known as: Soluble

    The sequence of this isoform differs from the canonical sequence as follows:
         1137-1145: QFHEALCQA → HPFSQHTAA
         1146-1306: Missing.

    Note: Incomplete sequence.
    Show »
    Length:1,145
    Mass (Da):131,659
    Checksum:iB7EED12CAB675583
    GO
    Isoform Testis-specific (identifier: P12821-3) [UniParc] [UniParc]FASTAAdd to basket
    Also known as: ACE-T

    The sequence of this isoform differs from the canonical sequence as follows:
         1-574: Missing.
         575-641: AGSSRPWQEV...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN

    Show »
    Length:732
    Mass (Da):83,330
    Checksum:i80E0D19CFA642313
    GO
    Isoform 4 (identifier: P12821-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-641: MGAASGRRGP...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN
         1128-1168: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:691
    Mass (Da):78,694
    Checksum:iF31FE078F52FF0B2
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    A0A0A0MSN4A0A0A0MSN4_HUMAN
    Angiotensin-converting enzyme
    ACE
    		1,242Annotation score:

    Annotation score:2 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>
    J3KS28J3KS28_HUMAN
    Angiotensin-converting enzyme
    ACE
    		314Annotation score:

    Annotation score:2 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>
    J3KTB8J3KTB8_HUMAN
    Angiotensin-converting enzyme
    ACE
    		282Annotation score:

    Annotation score:2 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>
    J3KSQ5J3KSQ5_HUMAN
    Angiotensin-converting enzyme
    ACE
    		208Annotation score:

    Annotation score:1 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>
    J3KTH9J3KTH9_HUMAN
    Angiotensin-converting enzyme
    ACE
    		168Annotation score:

    Annotation score:1 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>
    J3KRH5J3KRH5_HUMAN
    Angiotensin-converting enzyme
    ACE
    		145Annotation score:

    Annotation score:1 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>
    J3QLR4J3QLR4_HUMAN
    Angiotensin-converting enzyme
    ACE
    		119Annotation score:

    Annotation score:1 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>
    J3QRX8J3QRX8_HUMAN
    Angiotensin-converting enzyme
    ACE
    		138Annotation score:

    Annotation score:1 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>
    J3QSC7J3QSC7_HUMAN
    Angiotensin-converting enzyme
    ACE
    		36Annotation score:

    Annotation score:1 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>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence BAD92208 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    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 conflicti35Q → E AA sequence (PubMed:2558109).Curated1
    Sequence conflicti42D → R AA sequence (PubMed:2558109).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_029139154A → T. Corresponds to variant dbSNP:rs13306087Ensembl.1
    Natural variantiVAR_029140183A → T. Corresponds to variant dbSNP:rs12720754Ensembl.1
    Natural variantiVAR_023430244Y → C. Corresponds to variant dbSNP:rs3730025Ensembl.1
    Natural variantiVAR_054000260R → C. Corresponds to variant dbSNP:rs4302Ensembl.1
    Natural variantiVAR_054001260R → L. Corresponds to variant dbSNP:rs4303EnsemblClinVar.1
    Natural variantiVAR_011707261A → S1 PublicationCorresponds to variant dbSNP:rs4303EnsemblClinVar.1
    Natural variantiVAR_074173295D → N1 PublicationCorresponds to variant dbSNP:rs989500910Ensembl.1
    Natural variantiVAR_023431351P → L. Corresponds to variant dbSNP:rs2229839EnsemblClinVar.1
    Natural variantiVAR_035434354G → R1 PublicationCorresponds to variant dbSNP:rs56394458EnsemblClinVar.1
    Natural variantiVAR_029141379R → Q. Corresponds to variant dbSNP:rs13306085Ensembl.1
    Natural variantiVAR_029142524V → A. Corresponds to variant dbSNP:rs12720746Ensembl.1
    Natural variantiVAR_011708561R → W1 PublicationCorresponds to variant dbSNP:rs4314Ensembl.1
    Natural variantiVAR_020053592D → G. Corresponds to variant dbSNP:rs12709426EnsemblClinVar.1
    Natural variantiVAR_034602828M → T. Corresponds to variant dbSNP:rs13306091EnsemblClinVar.1
    Natural variantiVAR_023432916T → M. Corresponds to variant dbSNP:rs3730043Ensembl.1
    Natural variantiVAR_0141891018I → T1 PublicationCorresponds to variant dbSNP:rs4976Ensembl.1
    Natural variantiVAR_0141901051F → V1 PublicationCorresponds to variant dbSNP:rs4977Ensembl.1
    Natural variantiVAR_0234331187T → M. Corresponds to variant dbSNP:rs12709442Ensembl.1
    Natural variantiVAR_0234341228P → L No effect on activity; increases secretion; rate of solubilization is 2.5-fold higher than wild-type. 3 PublicationsCorresponds to variant dbSNP:rs121912703EnsemblClinVar.1
    Natural variantiVAR_0141911279R → Q1 PublicationCorresponds to variant dbSNP:rs4980EnsemblClinVar.1
    Natural variantiVAR_0117091286R → S2 PublicationsCorresponds to variant dbSNP:rs4364EnsemblClinVar.1
    Natural variantiVAR_0141921296Q → P1 PublicationCorresponds to variant dbSNP:rs4981Ensembl.1
    Isoform Testis-specific (identifier: P12821-3)
    Natural varianti32S → P. Corresponds to variant dbSNP:rs4317Ensembl.1
    Natural varianti49S → G. Corresponds to variant dbSNP:rs4318Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0548361 – 641MGAAS…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform 4. 1 PublicationAdd BLAST641
    Alternative sequenceiVSP_0351201 – 574Missing in isoform Testis-specific. 2 PublicationsAdd BLAST574
    Alternative sequenceiVSP_035121575 – 641AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform Testis-specific. 2 PublicationsAdd BLAST67
    Alternative sequenceiVSP_0548371128 – 1168Missing in isoform 4. 1 PublicationAdd BLAST41
    Alternative sequenceiVSP_0299321137 – 1145QFHEALCQA → HPFSQHTAA in isoform Somatic-2. 1 Publication9
    Alternative sequenceiVSP_0299331146 – 1306Missing in isoform Somatic-2. 1 PublicationAdd BLAST161

    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
    		J04144 mRNA Translation: AAA51684.1
    M26657 mRNA Translation: AAA60611.1
    X16295 mRNA Translation: CAA34362.1
    AF118569 Genomic DNA Translation: AAD28560.1
    AY436326 Genomic DNA Translation: AAR03504.1
    AK301988 mRNA Translation: BAG63395.1
    EU332840 Genomic DNA Translation: ABY87529.1
    AB208971 mRNA Translation: BAD92208.1 Different initiation.
    AC113554 Genomic DNA No translation available.

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS11637.1 [P12821-1]
    CCDS45755.1 [P12821-3]
    CCDS54155.1 [P12821-4]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A31759
    PW0053
    S05238

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000780.1, NM_000789.3 [P12821-1]
    NP_001171528.1, NM_001178057.1 [P12821-4]
    NP_690043.1, NM_152830.2 [P12821-3]

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.298469

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000290863; ENSP00000290863; ENSG00000159640 [P12821-3]
    ENST00000290866; ENSP00000290866; ENSG00000159640 [P12821-1]
    ENST00000413513; ENSP00000392247; ENSG00000159640 [P12821-4]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		1636

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:1636

    UCSC genome browser

    More...    UCSCi    		uc002jau.3 human [P12821-1]

    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

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		J04144 mRNA Translation: AAA51684.1
    M26657 mRNA Translation: AAA60611.1
    X16295 mRNA Translation: CAA34362.1
    AF118569 Genomic DNA Translation: AAD28560.1
    AY436326 Genomic DNA Translation: AAR03504.1
    AK301988 mRNA Translation: BAG63395.1
    EU332840 Genomic DNA Translation: ABY87529.1
    AB208971 mRNA Translation: BAD92208.1 Different initiation.
    AC113554 Genomic DNA No translation available.
    CCDSiCCDS11637.1 [P12821-1]
    CCDS45755.1 [P12821-3]
    CCDS54155.1 [P12821-4]
    PIRiA31759
    PW0053
    S05238
    RefSeqiNP_000780.1, NM_000789.3 [P12821-1]
    NP_001171528.1, NM_001178057.1 [P12821-4]
    NP_690043.1, NM_152830.2 [P12821-3]
    UniGeneiHs.298469

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1O86X-ray2.00A642-1230[»]
    1O8AX-ray2.00A642-1230[»]
    1UZEX-ray1.82A642-1230[»]
    1UZFX-ray2.00A642-1230[»]
    2C6FX-ray3.01A/B30-641[»]
    2C6NX-ray3.00A/B30-641[»]
    2IULX-ray2.01A642-1232[»]
    2IUXX-ray2.80A642-1232[»]
    2OC2X-ray2.25A642-1232[»]
    2XY9X-ray1.97A645-1228[»]
    2XYDX-ray2.15A/B30-639[»]
    2YDMX-ray2.44A642-1230[»]
    3BKKX-ray2.17A642-1232[»]
    3BKLX-ray2.18A642-1232[»]
    3L3NX-ray2.30A642-1232[»]
    3NXQX-ray1.99A/B30-658[»]
    4APHX-ray1.99A642-1230[»]
    4APJX-ray2.60A642-1230[»]
    4BXKX-ray2.20A/B30-657[»]
    4BZRX-ray1.84A642-1230[»]
    4BZSX-ray2.10A/B30-657[»]
    4C2NX-ray2.59A642-1230[»]
    4C2OX-ray1.80A642-1230[»]
    4C2PX-ray1.99A642-1230[»]
    4C2QX-ray2.40A642-1230[»]
    4C2RX-ray2.30A642-1230[»]
    4CA5X-ray1.85A642-1230[»]
    4CA6X-ray1.91A/B30-639[»]
    4UFAX-ray1.80A/B30-657[»]
    4UFBX-ray1.80A/B/C/D30-657[»]
    5AM8X-ray1.90A/B/C/D30-658[»]
    5AM9X-ray1.80A/B/C/D30-658[»]
    5AMAX-ray1.80A/B/C/D30-658[»]
    5AMBX-ray1.55A/B30-658[»]
    5AMCX-ray1.65A/B30-658[»]
    6EN5X-ray1.75A/B/C/D30-657[»]
    6EN6X-ray1.80A/B/C/D30-657[»]
    6F9RX-ray1.85A/B30-657[»]
    6F9TX-ray1.60A642-1232[»]
    6F9UX-ray1.90A642-1232[»]
    6F9VX-ray1.69A/B30-657[»]
    6H5WX-ray1.37A642-1232[»]
    6H5XX-ray1.80A/B30-657[»]
    ProteinModelPortaliP12821
    SMRiP12821
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108004, 8 interactors
    CORUMiP12821
    IntActiP12821, 1 interactor
    MINTiP12821
    STRINGi9606.ENSP00000290866

    Chemistry databases

    BindingDBiP12821
    ChEMBLiCHEMBL1808
    DrugBankiDB02032 1-(3-Mercapto-2-Methyl-Propionyl)-Pyrrolidine-2-Carboxylic Acid
    DB00542 Benazepril
    DB00616 Candoxatril
    DB01197 Captopril
    DB01340 Cilazapril
    DB00584 Enalapril
    DB09477 Enalaprilat
    DB00492 Fosinopril
    DB00722 Lisinopril
    DB00691 Moexipril
    DB03740 N-acetyl-alpha-D-glucosamine
    DB00886 Omapatrilat
    DB00790 Perindopril
    DB00881 Quinapril
    DB00178 Ramipril
    DB01180 Rescinnamine
    DB01348 Spirapril
    DB08836 Temocapril
    DB00519 Trandolapril
    DB13166 Zofenopril
    GuidetoPHARMACOLOGYi1613

    Protein family/group databases

    MEROPSiM02.001

    PTM databases

    GlyConnecti1011
    iPTMnetiP12821
    PhosphoSitePlusiP12821

    Polymorphism and mutation databases

    BioMutaiACE
    DMDMi113045

    Proteomic databases

    jPOSTiP12821
    MaxQBiP12821
    PaxDbiP12821
    PeptideAtlasiP12821
    PRIDEiP12821
    ProteomicsDBi52874
    52875 [P12821-2]
    52876 [P12821-3]
    52877 [P12821-4]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000290863; ENSP00000290863; ENSG00000159640 [P12821-3]
    ENST00000290866; ENSP00000290866; ENSG00000159640 [P12821-1]
    ENST00000413513; ENSP00000392247; ENSG00000159640 [P12821-4]
    GeneIDi1636
    KEGGihsa:1636
    UCSCiuc002jau.3 human [P12821-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		1636
    DisGeNETi1636
    EuPathDBiHostDB:ENSG00000159640.15

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		ACE
    HGNCiHGNC:2707 ACE
    HPAiCAB002426
    CAB002921
    HPA029298
    HPA069790
    MalaCardsiACE
    MIMi106180 gene+phenotype
    267430 phenotype
    601367 phenotype
    612624 phenotype
    614519 phenotype
    neXtProtiNX_P12821
    OpenTargetsiENSG00000159640
    Orphaneti34145 NON RARE IN EUROPE: Berger disease
    97369 Renal tubular dysgenesis of genetic origin
    PharmGKBiPA139

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG3690 Eukaryota
    ENOG410XPJ3 LUCA
    GeneTreeiENSGT00940000162051
    HOGENOMiHOG000007838
    HOVERGENiHBG000264
    InParanoidiP12821
    KOiK01283
    OMAiVTMEQLF
    OrthoDBi238880at2759
    PhylomeDBiP12821
    TreeFamiTF312861

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08412-MONOMER
    BRENDAi3.4.15.1 2681
    ReactomeiR-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
    SABIO-RKiP12821
    SignaLinkiP12821
    SIGNORiP12821

    Miscellaneous databases

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

    More...    ChiTaRSi    		ACE human
    EvolutionaryTraceiP12821

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		Angiotensin-converting_enzyme

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

    More...    GenomeRNAii    		1636
    PMAP-CutDBiP12821

    Protein Ontology

    More...    PROi    		PR:P12821

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000159640 Expressed in 115 organ(s), highest expression level in testis
    CleanExiHS_ACE
    ExpressionAtlasiP12821 baseline and differential
    GenevisibleiP12821 HS

    Family and domain databases

    CDDicd06461 M2_ACE, 2 hits
    InterProiView protein in InterPro
    IPR001548 Peptidase_M2
    PANTHERiPTHR10514 PTHR10514, 2 hits
    PfamiView protein in Pfam
    PF01401 Peptidase_M2, 2 hits
    PRINTSiPR00791 PEPDIPTASEA
    PROSITEiView protein in PROSITE
    PS00142 ZINC_PROTEASE, 2 hits

    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 nameiACE_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: P12821
    Secondary accession number(s): B0LPF0
    , B4DXI3, E7EU16, P22966, Q53YX9, Q59GY8, Q7M4L4
    <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: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: January 16, 2019
    This is version 232 of the entry and version 1 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    7. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    8. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    9. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
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