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Angiotensin-converting enzyme (ACE) (EC 3.2.1.-) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) (CD antigen CD143) [Cleaved into: Angiotensin-converting enzyme, soluble form]

 ACE_HUMAN               Reviewed;        1306 AA.
P12821; B0LPF0; B4DXI3; E7EU16; P22966; Q53YX9; Q59GY8; Q7M4L4;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
27-SEP-2017, entry version 220.
RecName: Full=Angiotensin-converting enzyme;
Short=ACE;
EC=3.2.1.-;
EC=3.4.15.1;
AltName: Full=Dipeptidyl carboxypeptidase I;
AltName: Full=Kininase II;
AltName: CD_antigen=CD143;
Contains:
RecName: Full=Angiotensin-converting enzyme, soluble form;
Flags: Precursor;
Name=ACE; Synonyms=DCP, DCP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC-1).
PubMed=2849100; DOI=10.1073/pnas.85.24.9386;
Soubrier F., Alhenc-Gelas F., Hubert C., Allegrini J., John M.,
Tregear G., Corbol P.;
"Two putative active centers in human angiotensin I-converting enzyme
revealed by molecular cloning.";
Proc. Natl. Acad. Sci. U.S.A. 85:9386-9390(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
PubMed=2547653; DOI=10.1016/0014-5793(89)80897-X;
Lattion A.L., Soubrier F., Allegrini J., Hubert C., Corvol P.,
Alhenc-Gelas F.;
"The testicular transcript of the angiotensin I-converting enzyme
encodes for the ancestral, non-duplicated form of the enzyme.";
FEBS Lett. 252:99-104(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
PubMed=2554286; DOI=10.1073/pnas.86.20.7741;
Ehlers M.R.W., Fox E.A., Strydom D.J., Riordan J.F.;
"Molecular cloning of human testicular angiotensin-converting enzyme:
the testis isozyme is identical to the C-terminal half of endothelial
angiotensin-converting enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 86:7741-7745(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-261; TRP-561 AND
SER-1286.
PubMed=10319862; DOI=10.1038/8760;
Rieder M.J., Taylor S.L., Clark A.G., Nickerson D.A.;
"Sequence variation in the human angiotensin converting enzyme.";
Nat. Genet. 22:59-62(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1239 (ISOFORM SOMATIC-1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
PROTEIN SEQUENCE OF 30-46.
TISSUE=Lung;
PubMed=2558109;
Takeuchi K., Shimizu T., Ohishi N., Seyama Y., Takaku F.,
Yotsumoto H.;
"Purification of human lung angiotensin-converting enzyme by high-
performance liquid chromatography: properties and N-terminal amino
acid sequence.";
J. Biochem. 106:442-445(1989).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1114-1306 (ISOFORM SOMATIC-2), AND
ALTERNATIVE SPLICING.
TISSUE=Umbilical vein endothelial cell;
PubMed=9642152; DOI=10.1006/bbrc.1998.8813;
Sugimura K., Tian X.-L., Hoffmann S., Ganten D., Bader M.;
"Alternative splicing of the mRNA coding for the human endothelial
angiotensin-converting enzyme: a new mechanism for solubilization.";
Biochem. Biophys. Res. Commun. 247:466-472(1998).
[11]
ZINC-BINDING.
PubMed=1649623; DOI=10.1021/bi00243a012;
Ehlers M.R.W., Riordan J.F.;
"Angiotensin-converting enzyme: zinc- and inhibitor-binding
stoichiometries of the somatic and testis isozymes.";
Biochemistry 30:7118-7126(1991).
[12]
DISULFIDE BONDS.
PubMed=8755737; DOI=10.1021/bi960243x;
Sturrock E.D., Yu X.C., Wu Z., Biemann K., Riordan J.F.;
"Assignment of free and disulfide-bonded cysteine residues in testis
angiotensin-converting enzyme: functional implications.";
Biochemistry 35:9560-9566(1996).
[13]
GLYCOSYLATION AT ASN-38; ASN-54; ASN-111; ASN-146; ASN-509; ASN-695;
ASN-714; ASN-760; ASN-942 AND ASN-1191, LACK OF GLYCOSYLATION AT
ASN-1225, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9013598; DOI=10.1074/jbc.272.6.3511;
Yu X.C., Sturrock E.D., Wu Z., Biemann K., Ehlers M.R.W.,
Riordan J.F.;
"Identification of N-linked glycosylation sites in human testis
angiotensin-converting enzyme and expression of an active
deglycosylated form.";
J. Biol. Chem. 272:3511-3519(1997).
[14]
CLEAVAGE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10769174; DOI=10.1042/bj3470711;
Woodman Z.L., Oppong S.Y., Cook S., Hooper N.M., Schwager S.L.U.,
Brandt W.F., Ehlers M.R.W., Sturrock E.D.;
"Shedding of somatic angiotensin-converting enzyme (ACE) is
inefficient compared with testis ACE despite cleavage at identical
stalk sites.";
Biochem. J. 347:711-718(2000).
[15]
TISSUE SPECIFICITY.
PubMed=10969042; DOI=10.1161/01.RES.87.5.e1;
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M.,
Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R.,
Breitbart R.E., Acton S.;
"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2)
converts angiotensin I to angiotensin 1-9.";
Circ. Res. 87:E1-E9(2000).
[16]
TISSUE SPECIFICITY.
PubMed=10924499; DOI=10.1074/jbc.M002615200;
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G.,
Turner A.J.;
"A human homolog of angiotensin-converting enzyme. Cloning and
functional expression as a captopril-insensitive carboxypeptidase.";
J. Biol. Chem. 275:33238-33243(2000).
[17]
BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANT
LEU-1228.
PubMed=11076943; DOI=10.1074/jbc.M007706200;
Eyries M., Michaud A., Deinum J., Agrapart M., Chomilier J.,
Kramers C., Soubrier F.;
"Increased shedding of angiotensin-converting enzyme by a mutation
identified in the stalk region.";
J. Biol. Chem. 276:5525-5532(2001).
[18]
PHOSPHORYLATION AT SER-1299, AND MUTAGENESIS OF SER-1299.
PubMed=12386153; DOI=10.1161/01.RES.0000038114.17939.C8;
Kohlstedt K., Shoghi F., Mueller-Esterl W., Busse R., Fleming I.;
"CK2 phosphorylates the angiotensin-converting enzyme and regulates
its retention in the endothelial cell plasma membrane.";
Circ. Res. 91:749-756(2002).
[19]
TISSUE SPECIFICITY.
PubMed=12459472; DOI=10.1016/S0014-5793(02)03640-2;
Harmer D., Gilbert M., Borman R., Clark K.L.;
"Quantitative mRNA expression profiling of ACE 2, a novel homologue of
angiotensin converting enzyme.";
FEBS Lett. 532:107-110(2002).
[20]
BIOPHYSICOCHEMICAL PROPERTIES, AND CLEAVAGE SITE.
PubMed=12542396; DOI=10.1042/BJ20021842;
Gordon K., Redelinghuys P., Schwager S.L.U., Ehlers M.R.W.,
Papageorgiou A.C., Natesh R., Acharya K.R., Sturrock E.D.;
"Deglycosylation, processing and crystallization of human testis
angiotensin-converting enzyme.";
Biochem. J. 371:437-442(2003).
[21]
INDUCTION.
PubMed=15151696; DOI=10.1186/1741-7015-2-19;
Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.;
"ACE2 gene expression is up-regulated in the human failing heart.";
BMC Med. 2:19-19(2004).
[22]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15671045; DOI=10.1093/eurheartj/ehi114;
Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S.,
Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E.,
Johnston C.I.;
"Myocardial infarction increases ACE2 expression in rat and humans.";
Eur. Heart J. 26:369-375(2005).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509; ASN-695 AND ASN-714.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111; ASN-445 AND ASN-714.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230, AND X-RAY
CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN COMPLEX WITH
LISINOPRIL.
PubMed=12540854; DOI=10.1038/nature01370;
Natesh R., Schwager S.L.U., Sturrock E.D., Acharya K.R.;
"Crystal structure of the human angiotensin-converting enzyme-
lisinopril complex.";
Nature 421:551-554(2003).
[27]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 642-1230 IN COMPLEX WITH
ENALAPRILAT, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN
COMPLEX WITH CAPTOPRIL.
PubMed=15236580; DOI=10.1021/bi049480n;
Natesh R., Schwager S.L.U., Evans H.R., Sturrock E.D., Acharya K.R.;
"Structural details on the binding of antihypertensive drugs captopril
and enalaprilat to human testicular angiotensin I-converting enzyme.";
Biochemistry 43:8718-8724(2004).
[28]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-641 IN COMPLEX WITH
LISINOPRIL; ZINC AND CHLORIDE IONS, AND GLYCOSYLATION AT ASN-54;
ASN-74; ASN-146; ASN-318 AND ASN-509.
PubMed=16476442; DOI=10.1016/j.jmb.2006.01.048;
Corradi H.R., Schwager S.L.U., Nchinda A.T., Sturrock E.D.,
Acharya K.R.;
"Crystal structure of the N domain of human somatic angiotensin I-
converting enzyme provides a structural basis for domain-specific
inhibitor design.";
J. Mol. Biol. 357:964-974(2006).
[29]
INVOLVEMENT IN MVCD3.
PubMed=10099885;
Vleming L.J., van der Pijl J.W., Lemkes H.H.P.J., Westendorp R.G.J.,
Maassen J.A., Daha M.R., van Es L.A., van Kooten C.;
"The DD genotype of the ACE gene polymorphism is associated with
progression of diabetic nephropathy to end stage renal failure in
IDDM.";
Clin. Nephrol. 51:133-140(1999).
[30]
VARIANTS THR-1018; VAL-1051; GLN-1279; SER-1286 AND PRO-1296.
PubMed=10391210; DOI=10.1038/10297;
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
Cooper R., Lipshutz R., Chakravarti A.;
"Patterns of single-nucleotide polymorphisms in candidate genes for
blood-pressure homeostasis.";
Nat. Genet. 22:239-247(1999).
[31]
VARIANT LEU-1228, AND ASSOCIATION WITH BENIGN SERUM INCREASE OF
ANGIOTENSIN-CONVERTING ENZYME.
PubMed=11551873; DOI=10.1161/hc3601.095932;
Kramers C., Danilov S.M., Deinum J., Balyasnikova I.V.,
Scharenborg N., Looman M., Boomsma F., de Keijzer M.H., van Duijn C.,
Martin S., Soubrier F., Adema G.J.;
"Point mutation in the stalk of angiotensin-converting enzyme causes a
dramatic increase in serum angiotensin-converting enzyme but no
cardiovascular disease.";
Circulation 104:1236-1240(2001).
[32]
VARIANT LEU-1228, AND ASSOCIATION WITH BENIGN SERUM INCREASE OF
ANGIOTENSIN-CONVERTING ENZYME.
PubMed=14694062; DOI=10.1212/01.WNL.0000098990.12845.DA;
Linnebank M., Kesper K., Jeub M., Urbach H., Wuellner U.,
Klockgether T., Schmidt S.;
"Hereditary elevation of angiotensin converting enzyme suggesting
neurosarcoidosis.";
Neurology 61:1819-1820(2003).
[33]
INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.
PubMed=15534175; DOI=10.1001/archneur.61.11.1652;
Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes
involving approximately 18,000 cases and 58,000 controls.";
Arch. Neurol. 61:1652-1661(2004).
[34]
INVOLVEMENT IN SUSCEPTIBILITY TO ICH.
PubMed=15277638; DOI=10.1212/01.WNL.0000130200.12993.0C;
Slowik A., Turaj W., Dziedzic T., Haefele A., Pera J., Malecki M.T.,
Glodzik-Sobanska L., Szermer P., Figlewicz D.A., Szczudlik A.;
"DD genotype of ACE gene is a risk factor for intracerebral
hemorrhage.";
Neurology 63:359-361(2004).
[35]
INVOLVEMENT IN RTD, AND VARIANT ARG-354.
PubMed=16116425; DOI=10.1038/ng1623;
Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N.,
Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G.,
Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J.,
Joubert M., Antignac C., Gubler M.-C.;
"Mutations in genes in the renin-angiotensin system are associated
with autosomal recessive renal tubular dysgenesis.";
Nat. Genet. 37:964-968(2005).
[36]
VARIANT ASN-295.
PubMed=25787250; DOI=10.1073/pnas.1503696112;
Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D.,
Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
Bjoerklund P., Lifton R.P.;
"Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
insulin-producing adenomas.";
Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
-!- FUNCTION: 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.
-!- CATALYTIC ACTIVITY: 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.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- COFACTOR: Isoform Testis-specific:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Isoform Testis-specific only binds 1 Zn(2+) ion per subunit.;
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996;
Note=Binds 3 chloride ions per subunit.;
-!- ENZYME REGULATION: Strongly activated by chloride. Specifically
inhibited by lisinopril, captopril and enalaprilat.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.51 mM for Hip-His-Leu {ECO:0000269|PubMed:11076943,
ECO:0000269|PubMed:12542396};
-!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
Secreted.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cytoplasm {ECO:0000250}. Note=Detected in both cell
membrane and cytoplasm in neurons. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Somatic-1;
IsoId=P12821-1; Sequence=Displayed;
Name=Somatic-2; Synonyms=Soluble;
IsoId=P12821-2; Sequence=VSP_029932, VSP_029933;
Note=Incomplete sequence.;
Name=Testis-specific; Synonyms=ACE-T;
IsoId=P12821-3, P22966-1;
Sequence=VSP_035120, VSP_035121;
Note=Variant in position: 32:S->P (in dbSNP:rs4317). Variant in
position: 49:S->G (in dbSNP:rs4318).;
Name=4;
IsoId=P12821-4; Sequence=VSP_054836, VSP_054837;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
lung, kidney, heart, gastrointestinal system and prostate. Isoform
Testis-specific is expressed in spermatocytes and adult testis.
{ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042,
ECO:0000269|PubMed:12459472, ECO:0000269|PubMed:15671045}.
-!- INDUCTION: Up-regulated in failing heart.
{ECO:0000269|PubMed:15151696, ECO:0000269|PubMed:15671045}.
-!- PTM: Phosphorylated by CK2 on Ser-1299; which allows membrane
retention. {ECO:0000269|PubMed:12386153}.
-!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an
acute neurologic event leading to death of neural tissue of the
brain and resulting in loss of motor, sensory and/or cognitive
function. Ischemic strokes, resulting from vascular occlusion, is
considered to be a highly complex disease consisting of a group of
heterogeneous disorders with multiple genetic and environmental
risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal
recessive severe disorder of renal tubular development
characterized by persistent fetal anuria and perinatal death,
probably due to pulmonary hypoplasia from early-onset
oligohydramnios (the Potter phenotype).
{ECO:0000269|PubMed:16116425}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Microvascular complications of diabetes 3 (MVCD3)
[MIM:612624]: Pathological conditions that develop in numerous
tissues and organs as a consequence of diabetes mellitus. They
include diabetic retinopathy, diabetic nephropathy leading to end-
stage renal disease, and diabetic neuropathy. Diabetic retinopathy
remains the major cause of new-onset blindness among diabetic
adults. It is characterized by vascular permeability and increased
tissue ischemia and angiogenesis. {ECO:0000269|PubMed:10099885}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A
pathological condition characterized by bleeding into one or both
cerebral hemispheres including the basal ganglia and the cerebral
cortex. It is often associated with hypertension and
craniocerebral trauma. Intracerebral bleeding is a common cause of
stroke. {ECO:0000269|PubMed:15277638}. Note=Disease susceptibility
is associated with variations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: Inhibitors of ACE are commonly used to treat
hypertension and some types of renal and cardiac dysfunction.
-!- MISCELLANEOUS: The glycosidase activity probably uses different
active site residues than the metalloprotease activity.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92208.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ACE";
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EMBL; J04144; AAA51684.1; -; mRNA.
EMBL; M26657; AAA60611.1; -; mRNA.
EMBL; X16295; CAA34362.1; -; mRNA.
EMBL; AF118569; AAD28560.1; -; Genomic_DNA.
EMBL; AY436326; AAR03504.1; -; Genomic_DNA.
EMBL; AK301988; BAG63395.1; -; mRNA.
EMBL; EU332840; ABY87529.1; -; Genomic_DNA.
EMBL; AB208971; BAD92208.1; ALT_INIT; mRNA.
EMBL; AC113554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS11637.1; -. [P12821-1]
CCDS; CCDS45755.1; -. [P12821-3]
CCDS; CCDS54155.1; -. [P12821-4]
PIR; A31759; A31759.
PIR; PW0053; PW0053.
PIR; S05238; S05238.
RefSeq; NP_000780.1; NM_000789.3. [P12821-1]
RefSeq; NP_001171528.1; NM_001178057.1. [P12821-4]
RefSeq; NP_690043.1; NM_152830.2. [P12821-3]
UniGene; Hs.298469; -.
PDB; 1O86; X-ray; 2.00 A; A=642-1230.
PDB; 1O8A; X-ray; 2.00 A; A=642-1230.
PDB; 1UZE; X-ray; 1.82 A; A=642-1230.
PDB; 1UZF; X-ray; 2.00 A; A=642-1230.
PDB; 2C6F; X-ray; 3.01 A; A/B=30-641.
PDB; 2C6N; X-ray; 3.00 A; A/B=30-641.
PDB; 2IUL; X-ray; 2.01 A; A=642-1232.
PDB; 2IUX; X-ray; 2.80 A; A=642-1232.
PDB; 2OC2; X-ray; 2.25 A; A=642-1232.
PDB; 2XY9; X-ray; 1.97 A; A=645-1228.
PDB; 2XYD; X-ray; 2.15 A; A/B=30-639.
PDB; 2YDM; X-ray; 2.44 A; A=642-1230.
PDB; 3BKK; X-ray; 2.17 A; A=642-1232.
PDB; 3BKL; X-ray; 2.18 A; A=642-1232.
PDB; 3L3N; X-ray; 2.30 A; A=642-1232.
PDB; 3NXQ; X-ray; 1.99 A; A/B=30-658.
PDB; 4APH; X-ray; 1.99 A; A=642-1230.
PDB; 4APJ; X-ray; 2.60 A; A=642-1230.
PDB; 4BXK; X-ray; 2.20 A; A/B=30-657.
PDB; 4BZR; X-ray; 1.84 A; A=642-1230.
PDB; 4BZS; X-ray; 2.10 A; A/B=30-657.
PDB; 4C2N; X-ray; 2.59 A; A=642-1230.
PDB; 4C2O; X-ray; 1.80 A; A=642-1230.
PDB; 4C2P; X-ray; 1.99 A; A=642-1230.
PDB; 4C2Q; X-ray; 2.40 A; A=642-1230.
PDB; 4C2R; X-ray; 2.30 A; A=642-1230.
PDB; 4CA5; X-ray; 1.85 A; A=642-1230.
PDB; 4CA6; X-ray; 1.91 A; A/B=30-639.
PDB; 4UFA; X-ray; 1.80 A; A/B=30-657.
PDB; 4UFB; X-ray; 1.80 A; A/B/C/D=30-657.
PDB; 5AM8; X-ray; 1.90 A; A/B/C/D=30-658.
PDB; 5AM9; X-ray; 1.80 A; A/B/C/D=30-658.
PDB; 5AMA; X-ray; 1.80 A; A/B/C/D=30-658.
PDB; 5AMB; X-ray; 1.55 A; A/B=30-658.
PDB; 5AMC; X-ray; 1.65 A; A/B=30-658.
PDBsum; 1O86; -.
PDBsum; 1O8A; -.
PDBsum; 1UZE; -.
PDBsum; 1UZF; -.
PDBsum; 2C6F; -.
PDBsum; 2C6N; -.
PDBsum; 2IUL; -.
PDBsum; 2IUX; -.
PDBsum; 2OC2; -.
PDBsum; 2XY9; -.
PDBsum; 2XYD; -.
PDBsum; 2YDM; -.
PDBsum; 3BKK; -.
PDBsum; 3BKL; -.
PDBsum; 3L3N; -.
PDBsum; 3NXQ; -.
PDBsum; 4APH; -.
PDBsum; 4APJ; -.
PDBsum; 4BXK; -.
PDBsum; 4BZR; -.
PDBsum; 4BZS; -.
PDBsum; 4C2N; -.
PDBsum; 4C2O; -.
PDBsum; 4C2P; -.
PDBsum; 4C2Q; -.
PDBsum; 4C2R; -.
PDBsum; 4CA5; -.
PDBsum; 4CA6; -.
PDBsum; 4UFA; -.
PDBsum; 4UFB; -.
PDBsum; 5AM8; -.
PDBsum; 5AM9; -.
PDBsum; 5AMA; -.
PDBsum; 5AMB; -.
PDBsum; 5AMC; -.
ProteinModelPortal; P12821; -.
SMR; P12821; -.
BioGrid; 108004; 8.
CORUM; P12821; -.
IntAct; P12821; 1.
MINT; MINT-127316; -.
STRING; 9606.ENSP00000290866; -.
BindingDB; P12821; -.
ChEMBL; CHEMBL1808; -.
DrugBank; DB02032; 1-(3-Mercapto-2-Methyl-Propionyl)-Pyrrolidine-2-Carboxylic Acid.
DrugBank; DB00542; Benazepril.
DrugBank; DB00616; Candoxatril.
DrugBank; DB01197; Captopril.
DrugBank; DB01340; Cilazapril.
DrugBank; DB00584; Enalapril.
DrugBank; DB09477; Enalaprilat.
DrugBank; DB00492; Fosinopril.
DrugBank; DB00722; Lisinopril.
DrugBank; DB00691; Moexipril.
DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DrugBank; DB00886; Omapatrilat.
DrugBank; DB00790; Perindopril.
DrugBank; DB00881; Quinapril.
DrugBank; DB00178; Ramipril.
DrugBank; DB01180; Rescinnamine.
DrugBank; DB01348; Spirapril.
DrugBank; DB08836; Temocapril.
DrugBank; DB00519; Trandolapril.
DrugBank; DB13166; Zofenopril.
GuidetoPHARMACOLOGY; 1613; -.
MEROPS; M02.001; -.
iPTMnet; P12821; -.
PhosphoSitePlus; P12821; -.
BioMuta; ACE; -.
DMDM; 113045; -.
EPD; P12821; -.
MaxQB; P12821; -.
PaxDb; P12821; -.
PeptideAtlas; P12821; -.
PRIDE; P12821; -.
Ensembl; ENST00000290863; ENSP00000290863; ENSG00000159640. [P12821-3]
Ensembl; ENST00000290866; ENSP00000290866; ENSG00000159640. [P12821-1]
Ensembl; ENST00000413513; ENSP00000392247; ENSG00000159640. [P12821-4]
GeneID; 1636; -.
KEGG; hsa:1636; -.
UCSC; uc002jau.3; human. [P12821-1]
CTD; 1636; -.
DisGeNET; 1636; -.
EuPathDB; HostDB:ENSG00000159640.15; -.
GeneCards; ACE; -.
HGNC; HGNC:2707; ACE.
HPA; CAB002426; -.
HPA; CAB002921; -.
HPA; HPA029298; -.
HPA; HPA069790; -.
MalaCards; ACE; -.
MIM; 106180; gene+phenotype.
MIM; 267430; phenotype.
MIM; 601367; phenotype.
MIM; 612624; phenotype.
MIM; 614519; phenotype.
neXtProt; NX_P12821; -.
OpenTargets; ENSG00000159640; -.
Orphanet; 97369; Renal tubular dysgenesis of genetic origin.
PharmGKB; PA139; -.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
GeneTree; ENSGT00520000055576; -.
HOGENOM; HOG000007838; -.
HOVERGEN; HBG000264; -.
InParanoid; P12821; -.
KO; K01283; -.
OMA; VTMEQLF; -.
OrthoDB; EOG091G033S; -.
PhylomeDB; P12821; -.
TreeFam; TF312861; -.
BioCyc; MetaCyc:HS08412-MONOMER; -.
BRENDA; 3.4.15.1; 2681.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
SABIO-RK; P12821; -.
SignaLink; P12821; -.
SIGNOR; P12821; -.
EvolutionaryTrace; P12821; -.
GeneWiki; Angiotensin-converting_enzyme; -.
GenomeRNAi; 1636; -.
PMAP-CutDB; P12821; -.
PRO; PR:P12821; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000159640; -.
CleanEx; HS_ACE; -.
ExpressionAtlas; P12821; baseline and differential.
Genevisible; P12821; HS.
GO; GO:0005768; C:endosome; IDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005764; C:lysosome; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0031711; F:bradykinin receptor binding; IPI:BHF-UCL.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031404; F:chloride ion binding; IDA:BHF-UCL.
GO; GO:0008144; F:drug binding; IDA:BHF-UCL.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0008238; F:exopeptidase activity; IDA:BHF-UCL.
GO; GO:0070573; F:metallodipeptidase activity; EXP:Reactome.
GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:BHF-UCL.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:BHF-UCL.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:UniProtKB.
GO; GO:0008240; F:tripeptidyl-peptidase activity; IDA:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
GO; GO:0050435; P:amyloid-beta metabolic process; IDA:BHF-UCL.
GO; GO:0002005; P:angiotensin catabolic process in blood; IC:UniProtKB.
GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:BHF-UCL.
GO; GO:0050482; P:arachidonic acid secretion; IDA:BHF-UCL.
GO; GO:0001974; P:blood vessel remodeling; IC:BHF-UCL.
GO; GO:0071838; P:cell proliferation in bone marrow; ISS:BHF-UCL.
GO; GO:0060047; P:heart contraction; ISS:BHF-UCL.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IC:BHF-UCL.
GO; GO:0042447; P:hormone catabolic process; IDA:BHF-UCL.
GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
GO; GO:0032943; P:mononuclear cell proliferation; IC:BHF-UCL.
GO; GO:1903597; P:negative regulation of gap junction assembly; ISS:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:0002446; P:neutrophil mediated immunity; ISS:BHF-UCL.
GO; GO:0043171; P:peptide catabolic process; IDA:BHF-UCL.
GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; ISS:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:BHF-UCL.
GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:UniProtKB.
GO; GO:0060177; P:regulation of angiotensin metabolic process; IDA:BHF-UCL.
GO; GO:0008217; P:regulation of blood pressure; ISS:BHF-UCL.
GO; GO:0097746; P:regulation of blood vessel diameter; IC:BHF-UCL.
GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; ISS:BHF-UCL.
GO; GO:0002019; P:regulation of renal output by angiotensin; IC:BHF-UCL.
GO; GO:0014910; P:regulation of smooth muscle cell migration; ISS:BHF-UCL.
GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IMP:BHF-UCL.
GO; GO:0019229; P:regulation of vasoconstriction; IC:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
CDD; cd06461; M2_ACE; 2.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 1.
Pfam; PF01401; Peptidase_M2; 2.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 29 {ECO:0000269|PubMed:2558109}.
CHAIN 30 1306 Angiotensin-converting enzyme.
/FTId=PRO_0000028530.
CHAIN 30 1232 Angiotensin-converting enzyme, soluble
form.
/FTId=PRO_0000028531.
PROPEP 1233 1306 Removed in soluble form.
/FTId=PRO_0000028532.
TOPO_DOM 30 1256 Extracellular. {ECO:0000255}.
TRANSMEM 1257 1277 Helical. {ECO:0000255}.
TOPO_DOM 1278 1306 Cytoplasmic. {ECO:0000255}.
REGION 30 630 Peptidase M2 1.
REGION 631 1232 Peptidase M2 2.
ACT_SITE 391 391 1.
ACT_SITE 989 989 2.
METAL 390 390 Zinc 1; catalytic.
{ECO:0000269|PubMed:16476442}.
METAL 394 394 Zinc 1; catalytic.
{ECO:0000269|PubMed:16476442}.
METAL 418 418 Zinc 1; catalytic.
{ECO:0000269|PubMed:16476442}.
METAL 988 988 Zinc 2; catalytic.
{ECO:0000269|PubMed:16476442}.
METAL 992 992 Zinc 2; catalytic.
{ECO:0000269|PubMed:16476442}.
METAL 1016 1016 Zinc 2; catalytic.
{ECO:0000269|PubMed:16476442}.
BINDING 231 231 Chloride 1.
BINDING 529 529 Chloride 1.
BINDING 791 791 Chloride 2.
BINDING 829 829 Chloride 3.
BINDING 1090 1090 Chloride 2.
BINDING 1094 1094 Chloride 2.
BINDING 1127 1127 Chloride 3.
SITE 1225 1225 Not glycosylated.
{ECO:0000269|PubMed:9013598}.
MOD_RES 1299 1299 Phosphoserine.
{ECO:0000269|PubMed:12386153}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:9013598}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16476442,
ECO:0000269|PubMed:9013598}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16476442}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9013598}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16476442,
ECO:0000269|PubMed:9013598}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16476442}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 509 509 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16476442,
ECO:0000269|PubMed:9013598}.
CARBOHYD 677 677 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 695 695 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:9013598}.
CARBOHYD 714 714 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9013598}.
CARBOHYD 760 760 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:9013598}.
CARBOHYD 942 942 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:9013598}.
CARBOHYD 1191 1191 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:9013598}.
DISULFID 157 165 {ECO:0000269|PubMed:8755737}.
DISULFID 757 763 {ECO:0000269|PubMed:8755737}.
DISULFID 957 975 {ECO:0000269|PubMed:8755737}.
DISULFID 1143 1155 {ECO:0000269|PubMed:8755737}.
VAR_SEQ 1 641 MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSA
DEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARR
QEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRIIGA
VRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTAT
CWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYE
DFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQ
LEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWA
QSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEE
FFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNR
KDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRR
GANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTESDI
NYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDW
WYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVS
FVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQ
AGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQ
QNGEVLGWPEYQWHPPLPDNYPEGID -> MGQGWATAGLP
SLLFLLLCYGHPLLVPSQEASQQVTVTHGTSSQATTSSQTT
THQATAHQTSAQSPN (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054836.
VAR_SEQ 1 574 Missing (in isoform Testis-specific).
{ECO:0000303|PubMed:2547653,
ECO:0000303|PubMed:2554286}.
/FTId=VSP_035120.
VAR_SEQ 575 641 AGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQ
QNGEVLGWPEYQWHPPLPDNYPEGID -> MGQGWATAGLP
SLLFLLLCYGHPLLVPSQEASQQVTVTHGTSSQATTSSQTT
THQATAHQTSAQSPN (in isoform Testis-
specific). {ECO:0000303|PubMed:2547653,
ECO:0000303|PubMed:2554286}.
/FTId=VSP_035121.
VAR_SEQ 1128 1168 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054837.
VAR_SEQ 1137 1145 QFHEALCQA -> HPFSQHTAA (in isoform
Somatic-2). {ECO:0000303|PubMed:9642152}.
/FTId=VSP_029932.
VAR_SEQ 1146 1306 Missing (in isoform Somatic-2).
{ECO:0000303|PubMed:9642152}.
/FTId=VSP_029933.
VARIANT 154 154 A -> T (in dbSNP:rs13306087).
/FTId=VAR_029139.
VARIANT 183 183 A -> T (in dbSNP:rs12720754).
/FTId=VAR_029140.
VARIANT 244 244 Y -> C (in dbSNP:rs3730025).
/FTId=VAR_023430.
VARIANT 260 260 R -> C (in dbSNP:rs4302).
/FTId=VAR_054000.
VARIANT 260 260 R -> L (in dbSNP:rs4303).
/FTId=VAR_054001.
VARIANT 261 261 A -> S (in dbSNP:rs4303).
{ECO:0000269|PubMed:10319862}.
/FTId=VAR_011707.
VARIANT 295 295 D -> N. {ECO:0000269|PubMed:25787250}.
/FTId=VAR_074173.
VARIANT 351 351 P -> L (in dbSNP:rs2229839).
/FTId=VAR_023431.
VARIANT 354 354 G -> R (in dbSNP:rs56394458).
{ECO:0000269|PubMed:16116425}.
/FTId=VAR_035434.
VARIANT 379 379 R -> Q (in dbSNP:rs13306085).
/FTId=VAR_029141.
VARIANT 524 524 V -> A (in dbSNP:rs12720746).
/FTId=VAR_029142.
VARIANT 561 561 R -> W (in dbSNP:rs4314).
{ECO:0000269|PubMed:10319862}.
/FTId=VAR_011708.
VARIANT 592 592 D -> G (in dbSNP:rs12709426).
/FTId=VAR_020053.
VARIANT 828 828 M -> T (in dbSNP:rs13306091).
/FTId=VAR_034602.
VARIANT 916 916 T -> M (in dbSNP:rs3730043).
/FTId=VAR_023432.
VARIANT 1018 1018 I -> T (in dbSNP:rs4976).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014189.
VARIANT 1051 1051 F -> V (in dbSNP:rs4977).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014190.
VARIANT 1187 1187 T -> M (in dbSNP:rs12709442).
/FTId=VAR_023433.
VARIANT 1228 1228 P -> L (no effect on activity; increases
secretion; rate of solubilization is 2.5-
fold higher than wild-type;
dbSNP:rs121912703).
{ECO:0000269|PubMed:11076943,
ECO:0000269|PubMed:11551873,
ECO:0000269|PubMed:14694062}.
/FTId=VAR_023434.
VARIANT 1279 1279 R -> Q (in dbSNP:rs4980).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014191.
VARIANT 1286 1286 R -> S (in dbSNP:rs4364).
{ECO:0000269|PubMed:10319862,
ECO:0000269|PubMed:10391210}.
/FTId=VAR_011709.
VARIANT 1296 1296 Q -> P (in dbSNP:rs4981).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014192.
MUTAGEN 1299 1299 S->A: Abolishes phosphorylation and
decreases membrane retention.
{ECO:0000269|PubMed:12386153}.
CONFLICT 35 35 Q -> E (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 42 42 D -> R (in Ref. 9; AA sequence).
{ECO:0000305}.
HELIX 32 34 {ECO:0000244|PDB:5AMB}.
HELIX 43 72 {ECO:0000244|PDB:5AMB}.
HELIX 77 105 {ECO:0000244|PDB:5AMB}.
TURN 106 108 {ECO:0000244|PDB:5AMB}.
HELIX 109 111 {ECO:0000244|PDB:5AMB}.
HELIX 115 124 {ECO:0000244|PDB:5AMB}.
HELIX 128 131 {ECO:0000244|PDB:5AMB}.
HELIX 134 153 {ECO:0000244|PDB:5AMB}.
STRAND 155 157 {ECO:0000244|PDB:5AMB}.
STRAND 159 161 {ECO:0000244|PDB:4BZS}.
STRAND 165 167 {ECO:0000244|PDB:5AMB}.
TURN 168 170 {ECO:0000244|PDB:5AMB}.
HELIX 171 178 {ECO:0000244|PDB:5AMB}.
HELIX 182 216 {ECO:0000244|PDB:5AMB}.
TURN 217 219 {ECO:0000244|PDB:5AMB}.
HELIX 223 229 {ECO:0000244|PDB:5AMB}.
HELIX 236 266 {ECO:0000244|PDB:5AMB}.
TURN 268 270 {ECO:0000244|PDB:5AMB}.
STRAND 281 284 {ECO:0000244|PDB:5AMB}.
HELIX 291 293 {ECO:0000244|PDB:5AMB}.
HELIX 294 297 {ECO:0000244|PDB:5AMB}.
HELIX 309 314 {ECO:0000244|PDB:5AMB}.
HELIX 319 332 {ECO:0000244|PDB:5AMB}.
HELIX 340 345 {ECO:0000244|PDB:5AMB}.
STRAND 352 354 {ECO:0000244|PDB:5AM9}.
STRAND 362 365 {ECO:0000244|PDB:5AMB}.
STRAND 367 370 {ECO:0000244|PDB:5AMB}.
STRAND 372 375 {ECO:0000244|PDB:5AMB}.
HELIX 382 401 {ECO:0000244|PDB:5AMB}.
HELIX 406 408 {ECO:0000244|PDB:5AMB}.
HELIX 414 428 {ECO:0000244|PDB:5AMB}.
HELIX 431 436 {ECO:0000244|PDB:5AMB}.
HELIX 447 461 {ECO:0000244|PDB:5AMB}.
HELIX 464 479 {ECO:0000244|PDB:5AMB}.
HELIX 485 487 {ECO:0000244|PDB:5AMB}.
HELIX 488 500 {ECO:0000244|PDB:5AMB}.
HELIX 514 517 {ECO:0000244|PDB:5AMB}.
TURN 519 524 {ECO:0000244|PDB:5AMB}.
HELIX 528 547 {ECO:0000244|PDB:5AMB}.
HELIX 554 556 {ECO:0000244|PDB:5AMB}.
HELIX 563 575 {ECO:0000244|PDB:5AMB}.
HELIX 581 589 {ECO:0000244|PDB:5AMB}.
HELIX 597 617 {ECO:0000244|PDB:5AMB}.
TURN 634 638 {ECO:0000244|PDB:5AMC}.
HELIX 641 643 {ECO:0000244|PDB:5AM9}.
HELIX 646 675 {ECO:0000244|PDB:4C2O}.
HELIX 680 704 {ECO:0000244|PDB:4C2O}.
HELIX 709 711 {ECO:0000244|PDB:4C2O}.
HELIX 715 724 {ECO:0000244|PDB:4C2O}.
HELIX 728 731 {ECO:0000244|PDB:4C2O}.
HELIX 734 753 {ECO:0000244|PDB:4C2O}.
STRAND 755 757 {ECO:0000244|PDB:4C2O}.
STRAND 759 761 {ECO:0000244|PDB:1UZE}.
STRAND 763 765 {ECO:0000244|PDB:4C2O}.
TURN 766 768 {ECO:0000244|PDB:4C2O}.
HELIX 769 776 {ECO:0000244|PDB:4C2O}.
HELIX 780 793 {ECO:0000244|PDB:4C2O}.
HELIX 795 799 {ECO:0000244|PDB:4C2O}.
HELIX 802 815 {ECO:0000244|PDB:4C2O}.
HELIX 821 827 {ECO:0000244|PDB:4C2O}.
HELIX 834 844 {ECO:0000244|PDB:4C2O}.
HELIX 846 864 {ECO:0000244|PDB:4C2O}.
HELIX 866 868 {ECO:0000244|PDB:4C2O}.
STRAND 879 882 {ECO:0000244|PDB:4C2O}.
HELIX 889 891 {ECO:0000244|PDB:4C2O}.
HELIX 892 895 {ECO:0000244|PDB:4C2O}.
HELIX 906 912 {ECO:0000244|PDB:4C2O}.
HELIX 917 930 {ECO:0000244|PDB:4C2O}.
HELIX 938 943 {ECO:0000244|PDB:4C2O}.
STRAND 945 947 {ECO:0000244|PDB:4APJ}.
STRAND 950 952 {ECO:0000244|PDB:4BZR}.
STRAND 960 963 {ECO:0000244|PDB:4C2O}.
STRAND 965 968 {ECO:0000244|PDB:4C2O}.
STRAND 970 973 {ECO:0000244|PDB:4C2O}.
HELIX 980 998 {ECO:0000244|PDB:4C2O}.
TURN 999 1001 {ECO:0000244|PDB:4C2O}.
HELIX 1004 1006 {ECO:0000244|PDB:4C2O}.
HELIX 1012 1026 {ECO:0000244|PDB:4C2O}.
HELIX 1029 1034 {ECO:0000244|PDB:4C2O}.
HELIX 1045 1077 {ECO:0000244|PDB:4C2O}.
TURN 1083 1085 {ECO:0000244|PDB:4C2O}.
HELIX 1086 1098 {ECO:0000244|PDB:4C2O}.
HELIX 1112 1115 {ECO:0000244|PDB:4C2O}.
TURN 1117 1122 {ECO:0000244|PDB:4C2O}.
HELIX 1126 1145 {ECO:0000244|PDB:4C2O}.
HELIX 1152 1154 {ECO:0000244|PDB:4C2O}.
HELIX 1161 1171 {ECO:0000244|PDB:4C2O}.
TURN 1172 1175 {ECO:0000244|PDB:4C2O}.
HELIX 1179 1187 {ECO:0000244|PDB:4C2O}.
STRAND 1188 1191 {ECO:0000244|PDB:3BKL}.
HELIX 1195 1215 {ECO:0000244|PDB:4C2O}.
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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