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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: ACE_HUMAN B4DKH4_HUMAN
LinkDB: ACE_HUMAN B4DKH4_HUMAN
Original site: ACE_HUMAN B4DKH4_HUMAN 
ID   ACE_HUMAN               Reviewed;        1306 AA.
AC   P12821; B0LPF0; B4DXI3; E7EU16; P22966; Q53YX9; Q59GY8; Q7M4L4;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   30-AUG-2017, entry version 219.
DE   RecName: Full=Angiotensin-converting enzyme;
DE            Short=ACE;
DE            EC=3.2.1.-;
DE            EC=3.4.15.1;
DE   AltName: Full=Dipeptidyl carboxypeptidase I;
DE   AltName: Full=Kininase II;
DE   AltName: CD_antigen=CD143;
DE   Contains:
DE     RecName: Full=Angiotensin-converting enzyme, soluble form;
DE   Flags: Precursor;
GN   Name=ACE; Synonyms=DCP, DCP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC-1).
RX   PubMed=2849100; DOI=10.1073/pnas.85.24.9386;
RA   Soubrier F., Alhenc-Gelas F., Hubert C., Allegrini J., John M.,
RA   Tregear G., Corbol P.;
RT   "Two putative active centers in human angiotensin I-converting enzyme
RT   revealed by molecular cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:9386-9390(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
RX   PubMed=2547653; DOI=10.1016/0014-5793(89)80897-X;
RA   Lattion A.L., Soubrier F., Allegrini J., Hubert C., Corvol P.,
RA   Alhenc-Gelas F.;
RT   "The testicular transcript of the angiotensin I-converting enzyme
RT   encodes for the ancestral, non-duplicated form of the enzyme.";
RL   FEBS Lett. 252:99-104(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
RX   PubMed=2554286; DOI=10.1073/pnas.86.20.7741;
RA   Ehlers M.R.W., Fox E.A., Strydom D.J., Riordan J.F.;
RT   "Molecular cloning of human testicular angiotensin-converting enzyme:
RT   the testis isozyme is identical to the C-terminal half of endothelial
RT   angiotensin-converting enzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7741-7745(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-261; TRP-561 AND
RP   SER-1286.
RX   PubMed=10319862; DOI=10.1038/8760;
RA   Rieder M.J., Taylor S.L., Clark A.G., Nickerson D.A.;
RT   "Sequence variation in the human angiotensin converting enzyme.";
RL   Nat. Genet. 22:59-62(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1239 (ISOFORM SOMATIC-1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [9]
RP   PROTEIN SEQUENCE OF 30-46.
RC   TISSUE=Lung;
RX   PubMed=2558109;
RA   Takeuchi K., Shimizu T., Ohishi N., Seyama Y., Takaku F.,
RA   Yotsumoto H.;
RT   "Purification of human lung angiotensin-converting enzyme by high-
RT   performance liquid chromatography: properties and N-terminal amino
RT   acid sequence.";
RL   J. Biochem. 106:442-445(1989).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1114-1306 (ISOFORM SOMATIC-2), AND
RP   ALTERNATIVE SPLICING.
RC   TISSUE=Umbilical vein endothelial cell;
RX   PubMed=9642152; DOI=10.1006/bbrc.1998.8813;
RA   Sugimura K., Tian X.-L., Hoffmann S., Ganten D., Bader M.;
RT   "Alternative splicing of the mRNA coding for the human endothelial
RT   angiotensin-converting enzyme: a new mechanism for solubilization.";
RL   Biochem. Biophys. Res. Commun. 247:466-472(1998).
RN   [11]
RP   ZINC-BINDING.
RX   PubMed=1649623; DOI=10.1021/bi00243a012;
RA   Ehlers M.R.W., Riordan J.F.;
RT   "Angiotensin-converting enzyme: zinc- and inhibitor-binding
RT   stoichiometries of the somatic and testis isozymes.";
RL   Biochemistry 30:7118-7126(1991).
RN   [12]
RP   DISULFIDE BONDS.
RX   PubMed=8755737; DOI=10.1021/bi960243x;
RA   Sturrock E.D., Yu X.C., Wu Z., Biemann K., Riordan J.F.;
RT   "Assignment of free and disulfide-bonded cysteine residues in testis
RT   angiotensin-converting enzyme: functional implications.";
RL   Biochemistry 35:9560-9566(1996).
RN   [13]
RP   GLYCOSYLATION AT ASN-38; ASN-54; ASN-111; ASN-146; ASN-509; ASN-695;
RP   ASN-714; ASN-760; ASN-942 AND ASN-1191, LACK OF GLYCOSYLATION AT
RP   ASN-1225, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=9013598; DOI=10.1074/jbc.272.6.3511;
RA   Yu X.C., Sturrock E.D., Wu Z., Biemann K., Ehlers M.R.W.,
RA   Riordan J.F.;
RT   "Identification of N-linked glycosylation sites in human testis
RT   angiotensin-converting enzyme and expression of an active
RT   deglycosylated form.";
RL   J. Biol. Chem. 272:3511-3519(1997).
RN   [14]
RP   CLEAVAGE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10769174; DOI=10.1042/bj3470711;
RA   Woodman Z.L., Oppong S.Y., Cook S., Hooper N.M., Schwager S.L.U.,
RA   Brandt W.F., Ehlers M.R.W., Sturrock E.D.;
RT   "Shedding of somatic angiotensin-converting enzyme (ACE) is
RT   inefficient compared with testis ACE despite cleavage at identical
RT   stalk sites.";
RL   Biochem. J. 347:711-718(2000).
RN   [15]
RP   TISSUE SPECIFICITY.
RX   PubMed=10969042; DOI=10.1161/01.RES.87.5.e1;
RA   Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M.,
RA   Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R.,
RA   Breitbart R.E., Acton S.;
RT   "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2)
RT   converts angiotensin I to angiotensin 1-9.";
RL   Circ. Res. 87:E1-E9(2000).
RN   [16]
RP   TISSUE SPECIFICITY.
RX   PubMed=10924499; DOI=10.1074/jbc.M002615200;
RA   Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G.,
RA   Turner A.J.;
RT   "A human homolog of angiotensin-converting enzyme. Cloning and
RT   functional expression as a captopril-insensitive carboxypeptidase.";
RL   J. Biol. Chem. 275:33238-33243(2000).
RN   [17]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANT
RP   LEU-1228.
RX   PubMed=11076943; DOI=10.1074/jbc.M007706200;
RA   Eyries M., Michaud A., Deinum J., Agrapart M., Chomilier J.,
RA   Kramers C., Soubrier F.;
RT   "Increased shedding of angiotensin-converting enzyme by a mutation
RT   identified in the stalk region.";
RL   J. Biol. Chem. 276:5525-5532(2001).
RN   [18]
RP   PHOSPHORYLATION AT SER-1299, AND MUTAGENESIS OF SER-1299.
RX   PubMed=12386153; DOI=10.1161/01.RES.0000038114.17939.C8;
RA   Kohlstedt K., Shoghi F., Mueller-Esterl W., Busse R., Fleming I.;
RT   "CK2 phosphorylates the angiotensin-converting enzyme and regulates
RT   its retention in the endothelial cell plasma membrane.";
RL   Circ. Res. 91:749-756(2002).
RN   [19]
RP   TISSUE SPECIFICITY.
RX   PubMed=12459472; DOI=10.1016/S0014-5793(02)03640-2;
RA   Harmer D., Gilbert M., Borman R., Clark K.L.;
RT   "Quantitative mRNA expression profiling of ACE 2, a novel homologue of
RT   angiotensin converting enzyme.";
RL   FEBS Lett. 532:107-110(2002).
RN   [20]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND CLEAVAGE SITE.
RX   PubMed=12542396; DOI=10.1042/BJ20021842;
RA   Gordon K., Redelinghuys P., Schwager S.L.U., Ehlers M.R.W.,
RA   Papageorgiou A.C., Natesh R., Acharya K.R., Sturrock E.D.;
RT   "Deglycosylation, processing and crystallization of human testis
RT   angiotensin-converting enzyme.";
RL   Biochem. J. 371:437-442(2003).
RN   [21]
RP   INDUCTION.
RX   PubMed=15151696; DOI=10.1186/1741-7015-2-19;
RA   Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.;
RT   "ACE2 gene expression is up-regulated in the human failing heart.";
RL   BMC Med. 2:19-19(2004).
RN   [22]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15671045; DOI=10.1093/eurheartj/ehi114;
RA   Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S.,
RA   Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E.,
RA   Johnston C.I.;
RT   "Myocardial infarction increases ACE2 expression in rat and humans.";
RL   Eur. Heart J. 26:369-375(2005).
RN   [23]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509; ASN-695 AND ASN-714.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [24]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111; ASN-445 AND ASN-714.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230, AND X-RAY
RP   CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN COMPLEX WITH
RP   LISINOPRIL.
RX   PubMed=12540854; DOI=10.1038/nature01370;
RA   Natesh R., Schwager S.L.U., Sturrock E.D., Acharya K.R.;
RT   "Crystal structure of the human angiotensin-converting enzyme-
RT   lisinopril complex.";
RL   Nature 421:551-554(2003).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 642-1230 IN COMPLEX WITH
RP   ENALAPRILAT, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN
RP   COMPLEX WITH CAPTOPRIL.
RX   PubMed=15236580; DOI=10.1021/bi049480n;
RA   Natesh R., Schwager S.L.U., Evans H.R., Sturrock E.D., Acharya K.R.;
RT   "Structural details on the binding of antihypertensive drugs captopril
RT   and enalaprilat to human testicular angiotensin I-converting enzyme.";
RL   Biochemistry 43:8718-8724(2004).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-641 IN COMPLEX WITH
RP   LISINOPRIL; ZINC AND CHLORIDE IONS, AND GLYCOSYLATION AT ASN-54;
RP   ASN-74; ASN-146; ASN-318 AND ASN-509.
RX   PubMed=16476442; DOI=10.1016/j.jmb.2006.01.048;
RA   Corradi H.R., Schwager S.L.U., Nchinda A.T., Sturrock E.D.,
RA   Acharya K.R.;
RT   "Crystal structure of the N domain of human somatic angiotensin I-
RT   converting enzyme provides a structural basis for domain-specific
RT   inhibitor design.";
RL   J. Mol. Biol. 357:964-974(2006).
RN   [29]
RP   INVOLVEMENT IN MVCD3.
RX   PubMed=10099885;
RA   Vleming L.J., van der Pijl J.W., Lemkes H.H.P.J., Westendorp R.G.J.,
RA   Maassen J.A., Daha M.R., van Es L.A., van Kooten C.;
RT   "The DD genotype of the ACE gene polymorphism is associated with
RT   progression of diabetic nephropathy to end stage renal failure in
RT   IDDM.";
RL   Clin. Nephrol. 51:133-140(1999).
RN   [30]
RP   VARIANTS THR-1018; VAL-1051; GLN-1279; SER-1286 AND PRO-1296.
RX   PubMed=10391210; DOI=10.1038/10297;
RA   Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
RA   Cooper R., Lipshutz R., Chakravarti A.;
RT   "Patterns of single-nucleotide polymorphisms in candidate genes for
RT   blood-pressure homeostasis.";
RL   Nat. Genet. 22:239-247(1999).
RN   [31]
RP   VARIANT LEU-1228, AND ASSOCIATION WITH BENIGN SERUM INCREASE OF
RP   ANGIOTENSIN-CONVERTING ENZYME.
RX   PubMed=11551873; DOI=10.1161/hc3601.095932;
RA   Kramers C., Danilov S.M., Deinum J., Balyasnikova I.V.,
RA   Scharenborg N., Looman M., Boomsma F., de Keijzer M.H., van Duijn C.,
RA   Martin S., Soubrier F., Adema G.J.;
RT   "Point mutation in the stalk of angiotensin-converting enzyme causes a
RT   dramatic increase in serum angiotensin-converting enzyme but no
RT   cardiovascular disease.";
RL   Circulation 104:1236-1240(2001).
RN   [32]
RP   VARIANT LEU-1228, AND ASSOCIATION WITH BENIGN SERUM INCREASE OF
RP   ANGIOTENSIN-CONVERTING ENZYME.
RX   PubMed=14694062; DOI=10.1212/01.WNL.0000098990.12845.DA;
RA   Linnebank M., Kesper K., Jeub M., Urbach H., Wuellner U.,
RA   Klockgether T., Schmidt S.;
RT   "Hereditary elevation of angiotensin converting enzyme suggesting
RT   neurosarcoidosis.";
RL   Neurology 61:1819-1820(2003).
RN   [33]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.
RX   PubMed=15534175; DOI=10.1001/archneur.61.11.1652;
RA   Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
RT   "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes
RT   involving approximately 18,000 cases and 58,000 controls.";
RL   Arch. Neurol. 61:1652-1661(2004).
RN   [34]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO ICH.
RX   PubMed=15277638; DOI=10.1212/01.WNL.0000130200.12993.0C;
RA   Slowik A., Turaj W., Dziedzic T., Haefele A., Pera J., Malecki M.T.,
RA   Glodzik-Sobanska L., Szermer P., Figlewicz D.A., Szczudlik A.;
RT   "DD genotype of ACE gene is a risk factor for intracerebral
RT   hemorrhage.";
RL   Neurology 63:359-361(2004).
RN   [35]
RP   INVOLVEMENT IN RTD, AND VARIANT ARG-354.
RX   PubMed=16116425; DOI=10.1038/ng1623;
RA   Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N.,
RA   Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G.,
RA   Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J.,
RA   Joubert M., Antignac C., Gubler M.-C.;
RT   "Mutations in genes in the renin-angiotensin system are associated
RT   with autosomal recessive renal tubular dysgenesis.";
RL   Nat. Genet. 37:964-968(2005).
RN   [36]
RP   VARIANT ASN-295.
RX   PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA   Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA   Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D.,
RA   Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
RA   Bjoerklund P., Lifton R.P.;
RT   "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT   insulin-producing adenomas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
CC   -!- FUNCTION: Converts angiotensin I to angiotensin II by release of
CC       the terminal His-Leu, this results in an increase of the
CC       vasoconstrictor activity of angiotensin. Also able to inactivate
CC       bradykinin, a potent vasodilator. Has also a glycosidase activity
CC       which releases GPI-anchored proteins from the membrane by cleaving
CC       the mannose linkage in the GPI moiety.
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
CC       oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither
CC       Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II,
CC       with increase in vasoconstrictor activity, but no action on
CC       angiotensin II.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- COFACTOR: Isoform Testis-specific:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Isoform Testis-specific only binds 1 Zn(2+) ion per subunit.;
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC       Note=Binds 3 chloride ions per subunit.;
CC   -!- ENZYME REGULATION: Strongly activated by chloride. Specifically
CC       inhibited by lisinopril, captopril and enalaprilat.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.51 mM for Hip-His-Leu {ECO:0000269|PubMed:11076943,
CC         ECO:0000269|PubMed:12542396};
CC   -!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
CC       Secreted.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cytoplasm {ECO:0000250}. Note=Detected in both cell
CC       membrane and cytoplasm in neurons. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Somatic-1;
CC         IsoId=P12821-1; Sequence=Displayed;
CC       Name=Somatic-2; Synonyms=Soluble;
CC         IsoId=P12821-2; Sequence=VSP_029932, VSP_029933;
CC         Note=Incomplete sequence.;
CC       Name=Testis-specific; Synonyms=ACE-T;
CC         IsoId=P12821-3, P22966-1;
CC         Sequence=VSP_035120, VSP_035121;
CC         Note=Variant in position: 32:S->P (in dbSNP:rs4317). Variant in
CC         position: 49:S->G (in dbSNP:rs4318).;
CC       Name=4;
CC         IsoId=P12821-4; Sequence=VSP_054836, VSP_054837;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       lung, kidney, heart, gastrointestinal system and prostate. Isoform
CC       Testis-specific is expressed in spermatocytes and adult testis.
CC       {ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042,
CC       ECO:0000269|PubMed:12459472, ECO:0000269|PubMed:15671045}.
CC   -!- INDUCTION: Up-regulated in failing heart.
CC       {ECO:0000269|PubMed:15151696, ECO:0000269|PubMed:15671045}.
CC   -!- PTM: Phosphorylated by CK2 on Ser-1299; which allows membrane
CC       retention. {ECO:0000269|PubMed:12386153}.
CC   -!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an
CC       acute neurologic event leading to death of neural tissue of the
CC       brain and resulting in loss of motor, sensory and/or cognitive
CC       function. Ischemic strokes, resulting from vascular occlusion, is
CC       considered to be a highly complex disease consisting of a group of
CC       heterogeneous disorders with multiple genetic and environmental
CC       risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease
CC       susceptibility is associated with variations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal
CC       recessive severe disorder of renal tubular development
CC       characterized by persistent fetal anuria and perinatal death,
CC       probably due to pulmonary hypoplasia from early-onset
CC       oligohydramnios (the Potter phenotype).
CC       {ECO:0000269|PubMed:16116425}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Microvascular complications of diabetes 3 (MVCD3)
CC       [MIM:612624]: Pathological conditions that develop in numerous
CC       tissues and organs as a consequence of diabetes mellitus. They
CC       include diabetic retinopathy, diabetic nephropathy leading to end-
CC       stage renal disease, and diabetic neuropathy. Diabetic retinopathy
CC       remains the major cause of new-onset blindness among diabetic
CC       adults. It is characterized by vascular permeability and increased
CC       tissue ischemia and angiogenesis. {ECO:0000269|PubMed:10099885}.
CC       Note=Disease susceptibility is associated with variations
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A
CC       pathological condition characterized by bleeding into one or both
CC       cerebral hemispheres including the basal ganglia and the cerebral
CC       cortex. It is often associated with hypertension and
CC       craniocerebral trauma. Intracerebral bleeding is a common cause of
CC       stroke. {ECO:0000269|PubMed:15277638}. Note=Disease susceptibility
CC       is associated with variations affecting the gene represented in
CC       this entry.
CC   -!- MISCELLANEOUS: Inhibitors of ACE are commonly used to treat
CC       hypertension and some types of renal and cardiac dysfunction.
CC   -!- MISCELLANEOUS: The glycosidase activity probably uses different
CC       active site residues than the metalloprotease activity.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92208.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ACE";
DR   EMBL; J04144; AAA51684.1; -; mRNA.
DR   EMBL; M26657; AAA60611.1; -; mRNA.
DR   EMBL; X16295; CAA34362.1; -; mRNA.
DR   EMBL; AF118569; AAD28560.1; -; Genomic_DNA.
DR   EMBL; AY436326; AAR03504.1; -; Genomic_DNA.
DR   EMBL; AK301988; BAG63395.1; -; mRNA.
DR   EMBL; EU332840; ABY87529.1; -; Genomic_DNA.
DR   EMBL; AB208971; BAD92208.1; ALT_INIT; mRNA.
DR   EMBL; AC113554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS11637.1; -. [P12821-1]
DR   CCDS; CCDS45755.1; -. [P12821-3]
DR   CCDS; CCDS54155.1; -. [P12821-4]
DR   PIR; A31759; A31759.
DR   PIR; PW0053; PW0053.
DR   PIR; S05238; S05238.
DR   RefSeq; NP_000780.1; NM_000789.3. [P12821-1]
DR   RefSeq; NP_001171528.1; NM_001178057.1. [P12821-4]
DR   RefSeq; NP_690043.1; NM_152830.2. [P12821-3]
DR   UniGene; Hs.298469; -.
DR   PDB; 1O86; X-ray; 2.00 A; A=642-1230.
DR   PDB; 1O8A; X-ray; 2.00 A; A=642-1230.
DR   PDB; 1UZE; X-ray; 1.82 A; A=642-1230.
DR   PDB; 1UZF; X-ray; 2.00 A; A=642-1230.
DR   PDB; 2C6F; X-ray; 3.01 A; A/B=30-641.
DR   PDB; 2C6N; X-ray; 3.00 A; A/B=30-641.
DR   PDB; 2IUL; X-ray; 2.01 A; A=642-1232.
DR   PDB; 2IUX; X-ray; 2.80 A; A=642-1232.
DR   PDB; 2OC2; X-ray; 2.25 A; A=642-1232.
DR   PDB; 2XY9; X-ray; 1.97 A; A=645-1228.
DR   PDB; 2XYD; X-ray; 2.15 A; A/B=30-639.
DR   PDB; 2YDM; X-ray; 2.44 A; A=642-1230.
DR   PDB; 3BKK; X-ray; 2.17 A; A=642-1232.
DR   PDB; 3BKL; X-ray; 2.18 A; A=642-1232.
DR   PDB; 3L3N; X-ray; 2.30 A; A=642-1232.
DR   PDB; 3NXQ; X-ray; 1.99 A; A/B=30-658.
DR   PDB; 4APH; X-ray; 1.99 A; A=642-1230.
DR   PDB; 4APJ; X-ray; 2.60 A; A=642-1230.
DR   PDB; 4BXK; X-ray; 2.20 A; A/B=30-657.
DR   PDB; 4BZR; X-ray; 1.84 A; A=642-1230.
DR   PDB; 4BZS; X-ray; 2.10 A; A/B=30-657.
DR   PDB; 4C2N; X-ray; 2.59 A; A=642-1230.
DR   PDB; 4C2O; X-ray; 1.80 A; A=642-1230.
DR   PDB; 4C2P; X-ray; 1.99 A; A=642-1230.
DR   PDB; 4C2Q; X-ray; 2.40 A; A=642-1230.
DR   PDB; 4C2R; X-ray; 2.30 A; A=642-1230.
DR   PDB; 4CA5; X-ray; 1.85 A; A=642-1230.
DR   PDB; 4CA6; X-ray; 1.91 A; A/B=30-639.
DR   PDB; 4UFA; X-ray; 1.80 A; A/B=30-657.
DR   PDB; 4UFB; X-ray; 1.80 A; A/B/C/D=30-657.
DR   PDB; 5AM8; X-ray; 1.90 A; A/B/C/D=30-658.
DR   PDB; 5AM9; X-ray; 1.80 A; A/B/C/D=30-658.
DR   PDB; 5AMA; X-ray; 1.80 A; A/B/C/D=30-658.
DR   PDB; 5AMB; X-ray; 1.55 A; A/B=30-658.
DR   PDB; 5AMC; X-ray; 1.65 A; A/B=30-658.
DR   PDBsum; 1O86; -.
DR   PDBsum; 1O8A; -.
DR   PDBsum; 1UZE; -.
DR   PDBsum; 1UZF; -.
DR   PDBsum; 2C6F; -.
DR   PDBsum; 2C6N; -.
DR   PDBsum; 2IUL; -.
DR   PDBsum; 2IUX; -.
DR   PDBsum; 2OC2; -.
DR   PDBsum; 2XY9; -.
DR   PDBsum; 2XYD; -.
DR   PDBsum; 2YDM; -.
DR   PDBsum; 3BKK; -.
DR   PDBsum; 3BKL; -.
DR   PDBsum; 3L3N; -.
DR   PDBsum; 3NXQ; -.
DR   PDBsum; 4APH; -.
DR   PDBsum; 4APJ; -.
DR   PDBsum; 4BXK; -.
DR   PDBsum; 4BZR; -.
DR   PDBsum; 4BZS; -.
DR   PDBsum; 4C2N; -.
DR   PDBsum; 4C2O; -.
DR   PDBsum; 4C2P; -.
DR   PDBsum; 4C2Q; -.
DR   PDBsum; 4C2R; -.
DR   PDBsum; 4CA5; -.
DR   PDBsum; 4CA6; -.
DR   PDBsum; 4UFA; -.
DR   PDBsum; 4UFB; -.
DR   PDBsum; 5AM8; -.
DR   PDBsum; 5AM9; -.
DR   PDBsum; 5AMA; -.
DR   PDBsum; 5AMB; -.
DR   PDBsum; 5AMC; -.
DR   ProteinModelPortal; P12821; -.
DR   SMR; P12821; -.
DR   BioGrid; 108004; 8.
DR   IntAct; P12821; 1.
DR   MINT; MINT-127316; -.
DR   STRING; 9606.ENSP00000290866; -.
DR   BindingDB; P12821; -.
DR   ChEMBL; CHEMBL1808; -.
DR   DrugBank; DB02032; 1-(3-Mercapto-2-Methyl-Propionyl)-Pyrrolidine-2-Carboxylic Acid.
DR   DrugBank; DB00542; Benazepril.
DR   DrugBank; DB00616; Candoxatril.
DR   DrugBank; DB01197; Captopril.
DR   DrugBank; DB01340; Cilazapril.
DR   DrugBank; DB00584; Enalapril.
DR   DrugBank; DB09477; Enalaprilat.
DR   DrugBank; DB00492; Fosinopril.
DR   DrugBank; DB00722; Lisinopril.
DR   DrugBank; DB00691; Moexipril.
DR   DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DR   DrugBank; DB00886; Omapatrilat.
DR   DrugBank; DB00790; Perindopril.
DR   DrugBank; DB00881; Quinapril.
DR   DrugBank; DB00178; Ramipril.
DR   DrugBank; DB01180; Rescinnamine.
DR   DrugBank; DB01348; Spirapril.
DR   DrugBank; DB08836; Temocapril.
DR   DrugBank; DB00519; Trandolapril.
DR   DrugBank; DB13166; Zofenopril.
DR   GuidetoPHARMACOLOGY; 1613; -.
DR   MEROPS; M02.001; -.
DR   iPTMnet; P12821; -.
DR   PhosphoSitePlus; P12821; -.
DR   BioMuta; ACE; -.
DR   DMDM; 113045; -.
DR   EPD; P12821; -.
DR   MaxQB; P12821; -.
DR   PaxDb; P12821; -.
DR   PeptideAtlas; P12821; -.
DR   PRIDE; P12821; -.
DR   Ensembl; ENST00000290863; ENSP00000290863; ENSG00000159640. [P12821-3]
DR   Ensembl; ENST00000290866; ENSP00000290866; ENSG00000159640. [P12821-1]
DR   Ensembl; ENST00000413513; ENSP00000392247; ENSG00000159640. [P12821-4]
DR   GeneID; 1636; -.
DR   KEGG; hsa:1636; -.
DR   UCSC; uc002jau.3; human. [P12821-1]
DR   CTD; 1636; -.
DR   DisGeNET; 1636; -.
DR   GeneCards; ACE; -.
DR   HGNC; HGNC:2707; ACE.
DR   HPA; CAB002426; -.
DR   HPA; CAB002921; -.
DR   HPA; HPA029298; -.
DR   HPA; HPA069790; -.
DR   MalaCards; ACE; -.
DR   MIM; 106180; gene+phenotype.
DR   MIM; 267430; phenotype.
DR   MIM; 601367; phenotype.
DR   MIM; 612624; phenotype.
DR   MIM; 614519; phenotype.
DR   neXtProt; NX_P12821; -.
DR   OpenTargets; ENSG00000159640; -.
DR   Orphanet; 97369; Renal tubular dysgenesis of genetic origin.
DR   PharmGKB; PA139; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   eggNOG; ENOG410XPJ3; LUCA.
DR   GeneTree; ENSGT00520000055576; -.
DR   HOGENOM; HOG000007838; -.
DR   HOVERGEN; HBG000264; -.
DR   InParanoid; P12821; -.
DR   KO; K01283; -.
DR   OMA; VTMEQLF; -.
DR   OrthoDB; EOG091G033S; -.
DR   PhylomeDB; P12821; -.
DR   TreeFam; TF312861; -.
DR   BioCyc; MetaCyc:HS08412-MONOMER; -.
DR   BRENDA; 3.4.15.1; 2681.
DR   Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   SABIO-RK; P12821; -.
DR   SignaLink; P12821; -.
DR   SIGNOR; P12821; -.
DR   EvolutionaryTrace; P12821; -.
DR   GeneWiki; Angiotensin-converting_enzyme; -.
DR   GenomeRNAi; 1636; -.
DR   PMAP-CutDB; P12821; -.
DR   PRO; PR:P12821; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000159640; -.
DR   CleanEx; HS_ACE; -.
DR   ExpressionAtlas; P12821; baseline and differential.
DR   Genevisible; P12821; HS.
DR   GO; GO:0005768; C:endosome; IDA:BHF-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR   GO; GO:0031711; F:bradykinin receptor binding; IPI:BHF-UCL.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031404; F:chloride ion binding; IDA:BHF-UCL.
DR   GO; GO:0008144; F:drug binding; IDA:BHF-UCL.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008238; F:exopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0070573; F:metallodipeptidase activity; EXP:Reactome.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:BHF-UCL.
DR   GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:BHF-UCL.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IDA:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; IDA:BHF-UCL.
DR   GO; GO:0002005; P:angiotensin catabolic process in blood; IC:UniProtKB.
DR   GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:BHF-UCL.
DR   GO; GO:0050482; P:arachidonic acid secretion; IDA:BHF-UCL.
DR   GO; GO:0001974; P:blood vessel remodeling; IC:BHF-UCL.
DR   GO; GO:0071838; P:cell proliferation in bone marrow; ISS:BHF-UCL.
DR   GO; GO:0060047; P:heart contraction; ISS:BHF-UCL.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IC:BHF-UCL.
DR   GO; GO:0042447; P:hormone catabolic process; IDA:BHF-UCL.
DR   GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
DR   GO; GO:0032943; P:mononuclear cell proliferation; IC:BHF-UCL.
DR   GO; GO:1903597; P:negative regulation of gap junction assembly; ISS:BHF-UCL.
DR   GO; GO:0002446; P:neutrophil mediated immunity; ISS:BHF-UCL.
DR   GO; GO:0043171; P:peptide catabolic process; IDA:BHF-UCL.
DR   GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
DR   GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; ISS:BHF-UCL.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:BHF-UCL.
DR   GO; GO:0006508; P:proteolysis; TAS:UniProtKB.
DR   GO; GO:0060177; P:regulation of angiotensin metabolic process; IDA:BHF-UCL.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:BHF-UCL.
DR   GO; GO:0097746; P:regulation of blood vessel diameter; IC:BHF-UCL.
DR   GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; ISS:BHF-UCL.
DR   GO; GO:0002019; P:regulation of renal output by angiotensin; IC:BHF-UCL.
DR   GO; GO:0014910; P:regulation of smooth muscle cell migration; ISS:BHF-UCL.
DR   GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IMP:BHF-UCL.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IC:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
DR   CDD; cd06461; M2_ACE; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 1.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   PROSITE; PS00142; ZINC_PROTEASE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Phosphoprotein; Polymorphism; Protease;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   SIGNAL        1     29       {ECO:0000269|PubMed:2558109}.
FT   CHAIN        30   1306       Angiotensin-converting enzyme.
FT                                /FTId=PRO_0000028530.
FT   CHAIN        30   1232       Angiotensin-converting enzyme, soluble
FT                                form.
FT                                /FTId=PRO_0000028531.
FT   PROPEP     1233   1306       Removed in soluble form.
FT                                /FTId=PRO_0000028532.
FT   TOPO_DOM     30   1256       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1257   1277       Helical. {ECO:0000255}.
FT   TOPO_DOM   1278   1306       Cytoplasmic. {ECO:0000255}.
FT   REGION       30    630       Peptidase M2 1.
FT   REGION      631   1232       Peptidase M2 2.
FT   ACT_SITE    391    391       1.
FT   ACT_SITE    989    989       2.
FT   METAL       390    390       Zinc 1; catalytic.
FT                                {ECO:0000269|PubMed:16476442}.
FT   METAL       394    394       Zinc 1; catalytic.
FT                                {ECO:0000269|PubMed:16476442}.
FT   METAL       418    418       Zinc 1; catalytic.
FT                                {ECO:0000269|PubMed:16476442}.
FT   METAL       988    988       Zinc 2; catalytic.
FT                                {ECO:0000269|PubMed:16476442}.
FT   METAL       992    992       Zinc 2; catalytic.
FT                                {ECO:0000269|PubMed:16476442}.
FT   METAL      1016   1016       Zinc 2; catalytic.
FT                                {ECO:0000269|PubMed:16476442}.
FT   BINDING     231    231       Chloride 1.
FT   BINDING     529    529       Chloride 1.
FT   BINDING     791    791       Chloride 2.
FT   BINDING     829    829       Chloride 3.
FT   BINDING    1090   1090       Chloride 2.
FT   BINDING    1094   1094       Chloride 2.
FT   BINDING    1127   1127       Chloride 3.
FT   SITE       1225   1225       Not glycosylated.
FT                                {ECO:0000269|PubMed:9013598}.
FT   MOD_RES    1299   1299       Phosphoserine.
FT                                {ECO:0000269|PubMed:12386153}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000305|PubMed:9013598}.
FT   CARBOHYD     54     54       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16476442,
FT                                ECO:0000269|PubMed:9013598}.
FT   CARBOHYD     74     74       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16476442}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:9013598}.
FT   CARBOHYD    146    146       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16476442,
FT                                ECO:0000269|PubMed:9013598}.
FT   CARBOHYD    160    160       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    318    318       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16476442}.
FT   CARBOHYD    445    445       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    509    509       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:16476442,
FT                                ECO:0000269|PubMed:9013598}.
FT   CARBOHYD    677    677       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    695    695       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:9013598}.
FT   CARBOHYD    714    714       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:9013598}.
FT   CARBOHYD    760    760       N-linked (GlcNAc...) asparagine; partial.
FT                                {ECO:0000269|PubMed:9013598}.
FT   CARBOHYD    942    942       N-linked (GlcNAc...) asparagine; partial.
FT                                {ECO:0000269|PubMed:9013598}.
FT   CARBOHYD   1191   1191       N-linked (GlcNAc...) asparagine; partial.
FT                                {ECO:0000269|PubMed:9013598}.
FT   DISULFID    157    165       {ECO:0000269|PubMed:8755737}.
FT   DISULFID    757    763       {ECO:0000269|PubMed:8755737}.
FT   DISULFID    957    975       {ECO:0000269|PubMed:8755737}.
FT   DISULFID   1143   1155       {ECO:0000269|PubMed:8755737}.
FT   VAR_SEQ       1    641       MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSA
FT                                DEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARR
FT                                QEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRIIGA
FT                                VRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTAT
FT                                CWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYE
FT                                DFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQ
FT                                LEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWA
FT                                QSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEE
FT                                FFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNR
FT                                KDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRR
FT                                GANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTESDI
FT                                NYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDW
FT                                WYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVS
FT                                FVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQ
FT                                AGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQ
FT                                QNGEVLGWPEYQWHPPLPDNYPEGID -> MGQGWATAGLP
FT                                SLLFLLLCYGHPLLVPSQEASQQVTVTHGTSSQATTSSQTT
FT                                THQATAHQTSAQSPN (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054836.
FT   VAR_SEQ       1    574       Missing (in isoform Testis-specific).
FT                                {ECO:0000303|PubMed:2547653,
FT                                ECO:0000303|PubMed:2554286}.
FT                                /FTId=VSP_035120.
FT   VAR_SEQ     575    641       AGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQ
FT                                QNGEVLGWPEYQWHPPLPDNYPEGID -> MGQGWATAGLP
FT                                SLLFLLLCYGHPLLVPSQEASQQVTVTHGTSSQATTSSQTT
FT                                THQATAHQTSAQSPN (in isoform Testis-
FT                                specific). {ECO:0000303|PubMed:2547653,
FT                                ECO:0000303|PubMed:2554286}.
FT                                /FTId=VSP_035121.
FT   VAR_SEQ    1128   1168       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054837.
FT   VAR_SEQ    1137   1145       QFHEALCQA -> HPFSQHTAA (in isoform
FT                                Somatic-2). {ECO:0000303|PubMed:9642152}.
FT                                /FTId=VSP_029932.
FT   VAR_SEQ    1146   1306       Missing (in isoform Somatic-2).
FT                                {ECO:0000303|PubMed:9642152}.
FT                                /FTId=VSP_029933.
FT   VARIANT     154    154       A -> T (in dbSNP:rs13306087).
FT                                /FTId=VAR_029139.
FT   VARIANT     183    183       A -> T (in dbSNP:rs12720754).
FT                                /FTId=VAR_029140.
FT   VARIANT     244    244       Y -> C (in dbSNP:rs3730025).
FT                                /FTId=VAR_023430.
FT   VARIANT     260    260       R -> C (in dbSNP:rs4302).
FT                                /FTId=VAR_054000.
FT   VARIANT     260    260       R -> L (in dbSNP:rs4303).
FT                                /FTId=VAR_054001.
FT   VARIANT     261    261       A -> S (in dbSNP:rs4303).
FT                                {ECO:0000269|PubMed:10319862}.
FT                                /FTId=VAR_011707.
FT   VARIANT     295    295       D -> N. {ECO:0000269|PubMed:25787250}.
FT                                /FTId=VAR_074173.
FT   VARIANT     351    351       P -> L (in dbSNP:rs2229839).
FT                                /FTId=VAR_023431.
FT   VARIANT     354    354       G -> R (in dbSNP:rs56394458).
FT                                {ECO:0000269|PubMed:16116425}.
FT                                /FTId=VAR_035434.
FT   VARIANT     379    379       R -> Q (in dbSNP:rs13306085).
FT                                /FTId=VAR_029141.
FT   VARIANT     524    524       V -> A (in dbSNP:rs12720746).
FT                                /FTId=VAR_029142.
FT   VARIANT     561    561       R -> W (in dbSNP:rs4314).
FT                                {ECO:0000269|PubMed:10319862}.
FT                                /FTId=VAR_011708.
FT   VARIANT     592    592       D -> G (in dbSNP:rs12709426).
FT                                /FTId=VAR_020053.
FT   VARIANT     828    828       M -> T (in dbSNP:rs13306091).
FT                                /FTId=VAR_034602.
FT   VARIANT     916    916       T -> M (in dbSNP:rs3730043).
FT                                /FTId=VAR_023432.
FT   VARIANT    1018   1018       I -> T (in dbSNP:rs4976).
FT                                {ECO:0000269|PubMed:10391210}.
FT                                /FTId=VAR_014189.
FT   VARIANT    1051   1051       F -> V (in dbSNP:rs4977).
FT                                {ECO:0000269|PubMed:10391210}.
FT                                /FTId=VAR_014190.
FT   VARIANT    1187   1187       T -> M (in dbSNP:rs12709442).
FT                                /FTId=VAR_023433.
FT   VARIANT    1228   1228       P -> L (no effect on activity; increases
FT                                secretion; rate of solubilization is 2.5-
FT                                fold higher than wild-type;
FT                                dbSNP:rs121912703).
FT                                {ECO:0000269|PubMed:11076943,
FT                                ECO:0000269|PubMed:11551873,
FT                                ECO:0000269|PubMed:14694062}.
FT                                /FTId=VAR_023434.
FT   VARIANT    1279   1279       R -> Q (in dbSNP:rs4980).
FT                                {ECO:0000269|PubMed:10391210}.
FT                                /FTId=VAR_014191.
FT   VARIANT    1286   1286       R -> S (in dbSNP:rs4364).
FT                                {ECO:0000269|PubMed:10319862,
FT                                ECO:0000269|PubMed:10391210}.
FT                                /FTId=VAR_011709.
FT   VARIANT    1296   1296       Q -> P (in dbSNP:rs4981).
FT                                {ECO:0000269|PubMed:10391210}.
FT                                /FTId=VAR_014192.
FT   MUTAGEN    1299   1299       S->A: Abolishes phosphorylation and
FT                                decreases membrane retention.
FT                                {ECO:0000269|PubMed:12386153}.
FT   CONFLICT     35     35       Q -> E (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     42     42       D -> R (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX        32     34       {ECO:0000244|PDB:5AMB}.
FT   HELIX        43     72       {ECO:0000244|PDB:5AMB}.
FT   HELIX        77    105       {ECO:0000244|PDB:5AMB}.
FT   TURN        106    108       {ECO:0000244|PDB:5AMB}.
FT   HELIX       109    111       {ECO:0000244|PDB:5AMB}.
FT   HELIX       115    124       {ECO:0000244|PDB:5AMB}.
FT   HELIX       128    131       {ECO:0000244|PDB:5AMB}.
FT   HELIX       134    153       {ECO:0000244|PDB:5AMB}.
FT   STRAND      155    157       {ECO:0000244|PDB:5AMB}.
FT   STRAND      159    161       {ECO:0000244|PDB:4BZS}.
FT   STRAND      165    167       {ECO:0000244|PDB:5AMB}.
FT   TURN        168    170       {ECO:0000244|PDB:5AMB}.
FT   HELIX       171    178       {ECO:0000244|PDB:5AMB}.
FT   HELIX       182    216       {ECO:0000244|PDB:5AMB}.
FT   TURN        217    219       {ECO:0000244|PDB:5AMB}.
FT   HELIX       223    229       {ECO:0000244|PDB:5AMB}.
FT   HELIX       236    266       {ECO:0000244|PDB:5AMB}.
FT   TURN        268    270       {ECO:0000244|PDB:5AMB}.
FT   STRAND      281    284       {ECO:0000244|PDB:5AMB}.
FT   HELIX       291    293       {ECO:0000244|PDB:5AMB}.
FT   HELIX       294    297       {ECO:0000244|PDB:5AMB}.
FT   HELIX       309    314       {ECO:0000244|PDB:5AMB}.
FT   HELIX       319    332       {ECO:0000244|PDB:5AMB}.
FT   HELIX       340    345       {ECO:0000244|PDB:5AMB}.
FT   STRAND      352    354       {ECO:0000244|PDB:5AM9}.
FT   STRAND      362    365       {ECO:0000244|PDB:5AMB}.
FT   STRAND      367    370       {ECO:0000244|PDB:5AMB}.
FT   STRAND      372    375       {ECO:0000244|PDB:5AMB}.
FT   HELIX       382    401       {ECO:0000244|PDB:5AMB}.
FT   HELIX       406    408       {ECO:0000244|PDB:5AMB}.
FT   HELIX       414    428       {ECO:0000244|PDB:5AMB}.
FT   HELIX       431    436       {ECO:0000244|PDB:5AMB}.
FT   HELIX       447    461       {ECO:0000244|PDB:5AMB}.
FT   HELIX       464    479       {ECO:0000244|PDB:5AMB}.
FT   HELIX       485    487       {ECO:0000244|PDB:5AMB}.
FT   HELIX       488    500       {ECO:0000244|PDB:5AMB}.
FT   HELIX       514    517       {ECO:0000244|PDB:5AMB}.
FT   TURN        519    524       {ECO:0000244|PDB:5AMB}.
FT   HELIX       528    547       {ECO:0000244|PDB:5AMB}.
FT   HELIX       554    556       {ECO:0000244|PDB:5AMB}.
FT   HELIX       563    575       {ECO:0000244|PDB:5AMB}.
FT   HELIX       581    589       {ECO:0000244|PDB:5AMB}.
FT   HELIX       597    617       {ECO:0000244|PDB:5AMB}.
FT   TURN        634    638       {ECO:0000244|PDB:5AMC}.
FT   HELIX       641    643       {ECO:0000244|PDB:5AM9}.
FT   HELIX       646    675       {ECO:0000244|PDB:4C2O}.
FT   HELIX       680    704       {ECO:0000244|PDB:4C2O}.
FT   HELIX       709    711       {ECO:0000244|PDB:4C2O}.
FT   HELIX       715    724       {ECO:0000244|PDB:4C2O}.
FT   HELIX       728    731       {ECO:0000244|PDB:4C2O}.
FT   HELIX       734    753       {ECO:0000244|PDB:4C2O}.
FT   STRAND      755    757       {ECO:0000244|PDB:4C2O}.
FT   STRAND      759    761       {ECO:0000244|PDB:1UZE}.
FT   STRAND      763    765       {ECO:0000244|PDB:4C2O}.
FT   TURN        766    768       {ECO:0000244|PDB:4C2O}.
FT   HELIX       769    776       {ECO:0000244|PDB:4C2O}.
FT   HELIX       780    793       {ECO:0000244|PDB:4C2O}.
FT   HELIX       795    799       {ECO:0000244|PDB:4C2O}.
FT   HELIX       802    815       {ECO:0000244|PDB:4C2O}.
FT   HELIX       821    827       {ECO:0000244|PDB:4C2O}.
FT   HELIX       834    844       {ECO:0000244|PDB:4C2O}.
FT   HELIX       846    864       {ECO:0000244|PDB:4C2O}.
FT   HELIX       866    868       {ECO:0000244|PDB:4C2O}.
FT   STRAND      879    882       {ECO:0000244|PDB:4C2O}.
FT   HELIX       889    891       {ECO:0000244|PDB:4C2O}.
FT   HELIX       892    895       {ECO:0000244|PDB:4C2O}.
FT   HELIX       906    912       {ECO:0000244|PDB:4C2O}.
FT   HELIX       917    930       {ECO:0000244|PDB:4C2O}.
FT   HELIX       938    943       {ECO:0000244|PDB:4C2O}.
FT   STRAND      945    947       {ECO:0000244|PDB:4APJ}.
FT   STRAND      950    952       {ECO:0000244|PDB:4BZR}.
FT   STRAND      960    963       {ECO:0000244|PDB:4C2O}.
FT   STRAND      965    968       {ECO:0000244|PDB:4C2O}.
FT   STRAND      970    973       {ECO:0000244|PDB:4C2O}.
FT   HELIX       980    998       {ECO:0000244|PDB:4C2O}.
FT   TURN        999   1001       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1004   1006       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1012   1026       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1029   1034       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1045   1077       {ECO:0000244|PDB:4C2O}.
FT   TURN       1083   1085       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1086   1098       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1112   1115       {ECO:0000244|PDB:4C2O}.
FT   TURN       1117   1122       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1126   1145       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1152   1154       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1161   1171       {ECO:0000244|PDB:4C2O}.
FT   TURN       1172   1175       {ECO:0000244|PDB:4C2O}.
FT   HELIX      1179   1187       {ECO:0000244|PDB:4C2O}.
FT   STRAND     1188   1191       {ECO:0000244|PDB:3BKL}.
FT   HELIX      1195   1215       {ECO:0000244|PDB:4C2O}.
SQ   SEQUENCE   1306 AA;  149715 MW;  1B33BCA7301A26AA CRC64;
     MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA QSYNSSAEQV
     LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK AKELYEPIWQ NFTDPQLRRI
     IGAVRTLGSA NLPLAKRQQY NALLSNMSRI YSTAKVCLPN KTATCWSLDP DLTNILASSR
     SYAMLLFAWE GWHNAAGIPL KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL
     EHLYQQLEPL YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF
     PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK PADGREVVCH
     ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ YKDLPVSLRR GANPGFHEAI
     GDVLALSVST PEHLHKIGLL DRVTNDTESD INYLLKMALE KIAFLPFGYL VDQWRWGVFS
     GRTPPSRYNF DWWYLRTKYQ GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF
     HEALCKEAGY EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL
     KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS KFVEEYDRTS
     QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY GTQARKFDVN QLQNTTIKRI
     IKKVQDLERA ALPAQELEEY NKILLDMETT YSVATVCHPN GSCLQLEPDL TNVMATSRKY
     EDLLWAWEGW RDKAGRAILQ FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER
     LFQELQPLYL NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS
     APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT DGREVVCHAS
     AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK DLPVALREGA NPGFHEAIGD
     VLALSVSTPK HLHSLNLLSS EGGSDEHDIN FLMKMALDKI AFIPFSYLVD QWRWRVFDGS
     ITKENYNQEW WSLRLKYQGL CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE
     ALCQAAGHTG PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY
     FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL DAQQARVGQW
     LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE VELRHS
//
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Ontology (50)   
   GO (50)   
Disease (5)   
   OMIM (5)   
Drug (21)   
   DrugBank (20)   
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Chemical reaction (2)   
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Gene (12)   
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Protein sequence (12)   
   RefSeq(pep) (3)   
   PMD (9)   
DNA sequence (9)   
   EMBL (9)   
3D Structure (35)   
   PDB (35)   
Protein domain (3)   
   InterPro (1)   
   Pfam (1)   
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Literature (34)   
   PubMed (34)   
Enzyme (1)   
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ID   B4DKH4_HUMAN            Unreviewed;       475 AA.
AC   B4DKH4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   05-JUL-2017, entry version 50.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG59186.1};
RN   [1] {ECO:0000313|EMBL:BAG59186.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cord blood {ECO:0000313|EMBL:BAG59186.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K.,
RA   Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y.,
RA   Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M.,
RA   Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU361144};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; AK296566; BAG59186.1; -; mRNA.
DR   RefSeq; NP_000780.1; NM_000789.3.
DR   UniGene; Hs.298469; -.
DR   ProteinModelPortal; B4DKH4; -.
DR   PaxDb; B4DKH4; -.
DR   PeptideAtlas; B4DKH4; -.
DR   PRIDE; B4DKH4; -.
DR   GeneID; 1636; -.
DR   KEGG; hsa:1636; -.
DR   CTD; 1636; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   eggNOG; ENOG410XPJ3; LUCA.
DR   HOGENOM; HOG000007838; -.
DR   KO; K01283; -.
DR   GenomeRNAi; 1636; -.
DR   Genevisible; B4DKH4; HS.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361144};
KW   Hydrolase {ECO:0000256|RuleBase:RU361144};
KW   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30    475       Angiotensin-converting enzyme.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002803094.
SQ   SEQUENCE   475 AA;  53750 MW;  0474ADD420A70C7F CRC64;
     MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA QSYNSSAEQV
     LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK AKELYEPIWQ NFTDPQLRRI
     IGAVRTLGSA NLPLAKRQQY NALLSNMSRI YSTAKVCLPN KTATCWSLDP DLTNILASSR
     SYAMLLFAWE GWHNAAGIPL KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL
     EHLYQQLEPL YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF
     PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP GFWEGSMLEK PADGREVVCH
     ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ YKDLPVSLRR GANPGFHEAI
     GDVLALSVST PEHLHKIGLL DRVTNDTEPS IRGSVLLLPE TKPTLMLELS FMFQM
//
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Ontology (5)   
   GO (5)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
All databases (13)   

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