ID   Q3TU20_MOUSE            Unreviewed;      1312 AA.
AC   Q3TU20;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|ARBA:ARBA00039858, ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=Ace {ECO:0000313|EMBL:AAI10363.1, ECO:0000313|MGI:MGI:87874};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE36151.1};
RN   [1] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:AAI10363.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAI10363.1};
RC   TISSUE=Mammary tumor. C3 {ECO:0000313|EMBL:AAI10363.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAE36151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE36151.1};
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE36151.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
CC   -!- FUNCTION: Soluble form that is released in blood plasma and other body
CC       fluids following proteolytic cleavage in the juxtamembrane stalk
CC       region. {ECO:0000256|ARBA:ARBA00037200}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + Leu-enkephalin = L-phenylalanyl-L-leucine + L-
CC         tyrosylglycylglycine; Xref=Rhea:RHEA:71487, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:190689, ChEBI:CHEBI:190708, ChEBI:CHEBI:190710;
CC         Evidence={ECO:0000256|ARBA:ARBA00037024};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71488;
CC         Evidence={ECO:0000256|ARBA:ARBA00037024};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + Met-enkephalin = L-phenylalanyl-L-methionine + L-
CC         tyrosylglycylglycine; Xref=Rhea:RHEA:71483, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:189868, ChEBI:CHEBI:190708, ChEBI:CHEBI:190709;
CC         Evidence={ECO:0000256|ARBA:ARBA00036262};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71484;
CC         Evidence={ECO:0000256|ARBA:ARBA00036262};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + Met-enkephalin-Arg-Phe = L-arginyl-L-phenylalanine +
CC         Met-enkephalin; Xref=Rhea:RHEA:70675, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:189868, ChEBI:CHEBI:189869, ChEBI:CHEBI:189870;
CC         Evidence={ECO:0000256|ARBA:ARBA00036091};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70676;
CC         Evidence={ECO:0000256|ARBA:ARBA00036091};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11);
CC         Xref=Rhea:RHEA:71475, ChEBI:CHEBI:15377, ChEBI:CHEBI:147362,
CC         ChEBI:CHEBI:190704, ChEBI:CHEBI:190706;
CC         Evidence={ECO:0000256|ARBA:ARBA00034019};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71476;
CC         Evidence={ECO:0000256|ARBA:ARBA00034019};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + substance P = Gly-L-Leu-L-Met-NH2 + substance P(1-8);
CC         Xref=Rhea:RHEA:71463, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC         ChEBI:CHEBI:190694, ChEBI:CHEBI:190699;
CC         Evidence={ECO:0000256|ARBA:ARBA00035850};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71464;
CC         Evidence={ECO:0000256|ARBA:ARBA00035850};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9);
CC         Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC         ChEBI:CHEBI:190693, ChEBI:CHEBI:190700;
CC         Evidence={ECO:0000256|ARBA:ARBA00034071};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71460;
CC         Evidence={ECO:0000256|ARBA:ARBA00034071};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + substance P = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 +
CC         substance P(1-6); Xref=Rhea:RHEA:71471, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:190692, ChEBI:CHEBI:190696, ChEBI:CHEBI:190697;
CC         Evidence={ECO:0000256|ARBA:ARBA00036862};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71472;
CC         Evidence={ECO:0000256|ARBA:ARBA00036862};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa,
CC         when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion
CC         of angiotensin I to angiotensin II, with increase in vasoconstrictor
CC         activity, but no action on angiotensin II.; EC=3.4.15.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00036868};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=angiotensin I + H2O = angiotensin II + L-histidyl-L-leucine;
CC         Xref=Rhea:RHEA:63560, ChEBI:CHEBI:15377, ChEBI:CHEBI:58506,
CC         ChEBI:CHEBI:147350, ChEBI:CHEBI:147392; EC=3.4.15.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00036030};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63561;
CC         Evidence={ECO:0000256|ARBA:ARBA00036030};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bradykinin + H2O = bradykinin(1-7) + L-Phe-L-Arg;
CC         Xref=Rhea:RHEA:71451, ChEBI:CHEBI:15377, ChEBI:CHEBI:132988,
CC         ChEBI:CHEBI:133147, ChEBI:CHEBI:147352;
CC         Evidence={ECO:0000256|ARBA:ARBA00035977};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71452;
CC         Evidence={ECO:0000256|ARBA:ARBA00035977};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=goralatide + H2O = L-lysyl-L-proline + N-acetyl-L-seryl-L-
CC         aspartate; Xref=Rhea:RHEA:71455, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:190701, ChEBI:CHEBI:190702, ChEBI:CHEBI:190703;
CC         Evidence={ECO:0000256|ARBA:ARBA00036673};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71456;
CC         Evidence={ECO:0000256|ARBA:ARBA00036673};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361144};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; BC110362; AAI10363.1; -; mRNA.
DR   EMBL; AK161020; BAE36151.1; -; mRNA.
DR   RefSeq; NP_001268748.1; NM_001281819.1.
DR   RefSeq; NP_997507.1; NM_207624.5.
DR   SMR; Q3TU20; -.
DR   MEROPS; M02.004; -.
DR   SwissPalm; Q3TU20; -.
DR   MaxQB; Q3TU20; -.
DR   Antibodypedia; 31288; 981 antibodies from 43 providers.
DR   DNASU; 11421; -.
DR   GeneID; 11421; -.
DR   KEGG; mmu:11421; -.
DR   AGR; MGI:87874; -.
DR   CTD; 1636; -.
DR   MGI; MGI:87874; Ace.
DR   VEuPathDB; HostDB:ENSMUSG00000020681; -.
DR   OMA; DYSDFQD; -.
DR   OrthoDB; 2898149at2759; -.
DR   BioGRID-ORCS; 11421; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Ace; mouse.
DR   ExpressionAtlas; Q3TU20; baseline and differential.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR   GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR   GO; GO:0031711; F:bradykinin receptor binding; IEA:Ensembl.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031404; F:chloride ion binding; IEA:Ensembl.
DR   GO; GO:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:Ensembl.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR   GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IEA:Ensembl.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:Ensembl.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
DR   GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IEA:Ensembl.
DR   GO; GO:0002003; P:angiotensin maturation; IEA:Ensembl.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR   GO; GO:0010815; P:bradykinin catabolic process; IEA:Ensembl.
DR   GO; GO:1904045; P:cellular response to aldosterone; IEA:Ensembl.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0042447; P:hormone catabolic process; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; IEA:Ensembl.
DR   GO; GO:0046325; P:negative regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR   GO; GO:0060177; P:regulation of angiotensin metabolic process; IEA:Ensembl.
DR   GO; GO:0014910; P:regulation of smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0010814; P:substance P catabolic process; IEA:Ensembl.
DR   GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
DR   CDD; cd06461; M2_ACE; 2.
DR   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF25; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU361144};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361144};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..1312
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014309162"
FT   TRANSMEM        1265..1286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1312 AA;  150918 MW;  7DF9F5BE91762DFF CRC64;
     MGAASGQRGR WPLSPPLLML SLLVLLLQPS PAPALDPGLQ PGNFSPDEAG AQLFAESYNS
     SAEVVMFQST VASWAHDTNI TEENARRQEE AALVSQEFAE VWGKKAKELY ESIWQNFTDS
     KLRRIIGSIR TLGPANLPLA QRQQYNSLLS NMSRIYSTGK VCFPNKTATC WSLDPELTNI
     LASSRSYAKL LFAWEGWHDA VGIPLKPLYQ DFTAISNEAY RQDDFSDTGA FWRSWYESPS
     FEESLEHIYH QLEPLYLNLH AYVRRALHRR YGDKYVNLRG PIPAHLLGDM WAQSWENIYD
     MVVPFPDKPN LDVTSTMVQK GWNATHMFRV SEEFFTSLGL SPMPPEFWAE SMLEKPTDGR
     EVVCHASAWD FYNRKDFRIK QCTRVTMEQL ATVHHEMGHV QYYLQYKDLH VSLRRGANPG
     FHEAIGDVLA LSVSTPAHLH KIGLLDHVTN DIESDINYLL KMALEKIAFL PFGYLVDQWR
     WGVFSGRTPP SRYNFDWWYL RTKYQGICPP VARNETHFDA GAKFHIPNVT PYIRYFVSFV
     LQFQFHQALC KEAGHQGPLH QCDIYQSAQA GAKLKQVLQA GCSRPWQEVL KDLVGSDALD
     AKALLEYFQP VSQWLEEQNQ RNGEVLGWPE NQWRPPLPDN YPEGIDLETD EAKADRFVEE
     YDRTAQVLLN EYAEANWQYN TNITIEGSKI LLEKSTEVSN HTLKYGTRAK TFDVSNFQNS
     SIKRIIKKLQ NLDRAVLPPK ELEEYNQILL DMETTYSLSN ICYTNGTCMP LEPDLTNMMA
     TSRKYEELLW AWKSWRDKVG RAILPFFPKY VEFSNKIAKL NGYTDAGDSW RSLYESDNLE
     QDLEKLYQEL QPLYLNLHAY VRRSLHRHYG SEYINLDGPI PAHLLGNMWA QTWSNIYDLV
     APFPSAPNID ATEAMIKQGW TPRRIFKEAD NFFTSLGLLP VPPEFWNKSM LEKPTDGREV
     VCHPSAWDFY NGKDFRIKQC TSVNMEDLVI AHHEMGHIQY FMQYKDLPVT FREGANPGFH
     EAIGDIMALS VSTPKHLYSL NLLSTEGSGY EYDINFLMKM ALDKIAFIPF SYLIDQWRWR
     VFDGSITKEN YNQEWWSLRL KYQGLCPPVP RSQGDFDPGS KFHVPANVPY VRYFVSFIIQ
     FQFHEALCRA AGHTGPLHKC DIYQSKEAGK LLADAMKLGY SKPWPEAMKL ITGQPNMSAS
     AMMNYFKPLT EWLVTENRRH GETLGWPEYN WAPNTARAEG STAESNRVNF LGLYLEPQQA
     RVGQWVLLFL GVALLVATVG LAHRLYNIRN HHSLRRPHRG PQFGSEVELR HS
//