Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 99 (11 Dec 2019)
Sequence version 1 (01 Mar 2001)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Angiotensin-converting enzyme

Gene

ACE

Organism
Pan troglodytes (Chimpanzee)
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>
-Protein inferred from homologyi <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 (By similarity).By similarity

<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:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei229Chloride 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi388Zinc 1; catalyticBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei3891PROSITE-ProRule annotation1
Metal bindingi392Zinc 1; catalyticBy similarity1
Metal bindingi416Zinc 1; catalyticBy similarity1
Binding sitei527Chloride 1By similarity1
Binding sitei789Chloride 2By similarity1
Binding sitei827Chloride 3By similarity1
Metal bindingi986Zinc 2; catalyticBy similarity1
Active sitei9872PROSITE-ProRule annotation1
Metal bindingi990Zinc 2; catalyticBy similarity1
Metal bindingi1014Zinc 2; catalyticBy similarity1
Binding sitei1088Chloride 2By similarity1
Binding sitei1092Chloride 2By similarity1
Binding sitei1125Chloride 3By similarity1

<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

GO - Biological processi

<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

<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:
<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: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>OrganismiPan troglodytes (Chimpanzee)
<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 identifieri9598 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
<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
  • UP000002277 <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

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:51632 ACE

<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 domaini28 – 1257ExtracellularSequence analysisAdd BLAST1230
<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>Transmembranei1258 – 1274HelicalSequence analysisAdd BLAST17
Topological domaini1275 – 1304CytoplasmicSequence analysisAdd BLAST30

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

<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 – 27By similarityAdd BLAST27
<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_000002854528 – 1304Angiotensin-converting enzymeAdd BLAST1277
ChainiPRO_000002854628 – 1230Angiotensin-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_00000285471231 – 1304Removed in secreted formBy similarityAdd 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>Glycosylationi36N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi72N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi109N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi144N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi155 ↔ 163By similarity
Glycosylationi158N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi316N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi440N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi443N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi507N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi675N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi693N-linked (GlcNAc...) (complex) asparagineBy similarity1
Glycosylationi712N-linked (GlcNAc...) (complex) asparagineBy similarity1
Disulfide bondi755 ↔ 761By similarity
Glycosylationi758N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi940N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi955 ↔ 973By similarity
Disulfide bondi1141 ↔ 1153By similarity
Glycosylationi1189N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei1297PhosphoserineBy similarity1

<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-1297; which allows membrane retention.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9GLN7

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9598.ENSPTRP00000038991

<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

3D structure databases

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

More...
SMRi
Q9GLN7

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Regioni28 – 628Peptidase M2 1Add BLAST601
Regioni629 – 1230Peptidase 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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000162051

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9GLN7

Identification of Orthologs from Complete Genome Data

More...
OMAi
SIFARVW

Database of Orthologous Groups

More...
OrthoDBi
422699at2759

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, 4 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform Somatic (identifier: Q9GLN7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 GLLLPLLLLL PPQPALALDP GLQPGNFSAD EAGAQLFAQS
60 70 80 90 100
YNSSAEQVLF QSVAASWAHD TNITAENARR QEEAALLSQE FAEAWGQKAK
110 120 130 140 150
ELYEPVWQNF TDPQLRRIIG AVRTLGSANL PLAKRQQYNA LLSNMSRIYS
160 170 180 190 200
TAKVCLPNKT ATCWSLDPDL TNILASSRSY AMLLFAWEGW HNAAGIPLKP
210 220 230 240 250
LYEDFTALSN EAYKQDGFTD TGAYWRSWYN SPTFEDDLEH LYQQLEPLYL
260 270 280 290 300
NLHAFVRRAL HRRYGDRYIN LRGPIPAHLL GDMWAQSWEN IYDMVVPFPD
310 320 330 340 350
KPNLDVTSTM LQQGWNATHM FRVAEEFFTS LELSPMPPEF WEGSMLEKPA
360 370 380 390 400
DGREVVCHAS AWDFYNRKDF RIKQCTRVTM DQLSTVHHEM GHIQYYLQYK
410 420 430 440 450
DLPVSLRGGA NPGFHEAIGD VLALSVSTPA HLHKIGLLDN VTNDTESDIN
460 470 480 490 500
YLLKMALEKI AFLPFGYLVD QWRWGVFSGR TPNSRYNFDW WYLRTKYQGI
510 520 530 540 550
CPPVTRNETH FDAGAKFHVP NVTPYIRYFV SFVLQFQFHE ALCKEAGYEG
560 570 580 590 600
PLHQCDIYQS TKAGAKLRKV LQAGSSRPWQ EVLKDMVGLD ALDAQPLLKY
610 620 630 640 650
FQPVTQWLQE QNQQNGEVLG WPEYQWHPPL PDNYPEGIDL VTDEAEASKF
660 670 680 690 700
VEEYDRTSQV VWNEYAEANW NYNTNITTET SKILLQKNMQ IANHTLKYGT
710 720 730 740 750
QARRFDVNQL QNTTIKRIIK KVQDLERAAL PAQELEEYNK ILLDMETTYS
760 770 780 790 800
VATVCHTNGS CLQLEPDLTN VMATSRKYED LLWAWEGWRD KAGRAILQFY
810 820 830 840 850
PKYVELINQA ARLNGYVDAG DSWRSMYETP SLEQDLERLF QELQPLYLNL
860 870 880 890 900
HAYVRRALHR HYGAQHINLE GPIPAHLLGN MWAQTWSNIY DLVVPFPSAP
910 920 930 940 950
SMDTTEAMLK QGWTPRRMFK EADDFFTSLG LLPVPPEFWN KSMLEKPTDG
960 970 980 990 1000
REVVCHASAW DFYNGKDFRI KQCTTVNLED LVVAHHEMGH IQYFMQYKDL
1010 1020 1030 1040 1050
PVALREGANP GFHEAIGDVL ALSVSTPKHL HSLNLLSSEG GSDEHDINFL
1060 1070 1080 1090 1100
MKMALDKIAF IPFSYLVDQW RWRVFDGSIT KENYNQEWWS LRLKYQGLCP
1110 1120 1130 1140 1150
PVPRTQGDFD PGAKFHIPSS VPYIRYFVSF IIQFQFHEAL CQAAGHTGPL
1160 1170 1180 1190 1200
HKCDIYQSKE AGQRLATAMK LGFSRPWPEA MQLITGQPNM SASAMLSYFK
1210 1220 1230 1240 1250
PLLDWLRTEN ELHGEKLGWP QYNWTPNSAR SEGPLPDSGR VSFLGLDLDA
1260 1270 1280 1290 1300
QQARVGQWLL LFLGIALLVA TLGLSQRLFS IRHRSLHRHS HGPQFDSEVE

LRHS
Length:1,304
Mass (Da):149,370
Last modified:March 1, 2001 - 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:iDCF728D0BA0F1314
GO
Isoform Testis-specific (identifier: Q9GLN7-2) [UniParc] [UniParc]FASTAAdd to basket
Also known as: ACE-T

The sequence of this isoform differs from the canonical sequence as follows:
     1-572: Missing.
     573-639: AGSSRPWQEV...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN

Show »
Length:732
Mass (Da):83,429
Checksum:iC43D06443A47E74B
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H2QZH0H2QZH0_PANTR
Angiotensin-converting enzyme
ACE
1,306Annotation 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>
A0A2I3SKE0A0A2I3SKE0_PANTR
Angiotensin-converting enzyme
ACE
691Annotation 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>
H2QDM6H2QDM6_PANTR
Angiotensin-converting enzyme
ACE CK820_G0011626
739Annotation 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>
A0A2I3T2T2A0A2I3T2T2_PANTR
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>

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_0376401 – 572Missing in isoform Testis-specific. CuratedAdd BLAST572
Alternative sequenceiVSP_037641573 – 639AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEAPRQVTVTHG TSSQATTSGQTTTHQATAHQ TSAQSPN in isoform Testis-specific. CuratedAdd BLAST67

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
AF193486 AF193466 Genomic DNA Translation: AAG31358.1
AF193486 AF193485 Genomic DNA Translation: AAG31359.1

NCBI Reference Sequences

More...
RefSeqi
XP_016785980.1, XM_016930491.1 [Q9GLN7-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSPTRT00000102035; ENSPTRP00000073589; ENSPTRG00000009513 [Q9GLN7-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
449567

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193486 AF193466 Genomic DNA Translation: AAG31358.1
AF193486 AF193485 Genomic DNA Translation: AAG31359.1
RefSeqiXP_016785980.1, XM_016930491.1 [Q9GLN7-2]

3D structure databases

SMRiQ9GLN7
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000038991

Proteomic databases

PRIDEiQ9GLN7

Genome annotation databases

EnsembliENSPTRT00000102035; ENSPTRP00000073589; ENSPTRG00000009513 [Q9GLN7-2]
GeneIDi449567

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1636
VGNCiVGNC:51632 ACE

Phylogenomic databases

GeneTreeiENSGT00940000162051
InParanoidiQ9GLN7
OMAiSIFARVW
OrthoDBi422699at2759

Family and domain databases

CDDicd06461 M2_ACE, 2 hits
InterProiView protein in InterPro
IPR001548 Peptidase_M2
PANTHERiPTHR10514 PTHR10514, 4 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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_PANTR
<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: Q9GLN7
Secondary accession number(s): Q9GLN6
<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 30, 2005
Last sequence update: March 1, 2001
Last modified: December 11, 2019
This is version 99 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. Peptidase families
    Classification of peptidase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again