ID ACE2_MOUSE Reviewed; 805 AA.
AC Q8R0I0; Q99N70; Q99N71;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Angiotensin-converting enzyme 2;
DE EC=3.4.17.23 {ECO:0000250|UniProtKB:Q9BYF1};
DE AltName: Full=ACE-related carboxypeptidase;
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q9BYF1};
DE Contains:
DE RecName: Full=Processed angiotensin-converting enzyme 2;
DE Flags: Precursor;
GN Name=Ace2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=12487024; DOI=10.1080/1042517021000021608;
RA Komatsu T., Suzuki Y., Imai J., Sugano S., Hida M., Tanigami A., Muroi S.,
RA Yamada Y., Hanaoka K.;
RT "Molecular cloning, mRNA expression, and chromosomal localization of mouse
RT angiotensin-converting enzyme-related carboxypeptidase (mACE2).";
RL DNA Seq. 13:217-220(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12075344; DOI=10.1038/nature00786;
RA Crackower M.A., Sarao R., Oudit G.Y., Yagil C., Kozieradzki I.,
RA Scanga S.E., Oliveira-dos-Santos A.J., da Costa J., Zhang L., Pei Y.,
RA Scholey J., Ferrario C.M., Manoukian A.S., Chappell M.C., Backx P.H.,
RA Yagil Y., Penninger J.M.;
RT "Angiotensin-converting enzyme 2 is an essential regulator of heart
RT function.";
RL Nature 417:822-828(2002).
RN [4]
RP FUNCTION.
RX PubMed=12967627; DOI=10.1016/s0022-2828(03)00177-9;
RA Donoghue M., Wakimoto H., Maguire C.T., Acton S., Hales P., Stagliano N.,
RA Fairchild-Huntress V., Xu J., Lorenz J.N., Kadambi V., Berul C.I.,
RA Breitbart R.E.;
RT "Heart block, ventricular tachycardia, and sudden death in ACE2 transgenic
RT mice with downregulated connexins.";
RL J. Mol. Cell. Cardiol. 35:1043-1053(2003).
RN [5]
RP INTERACTION WITH SARS-COV S PROTEIN.
RX PubMed=15452268; DOI=10.1128/jvi.78.20.11429-11433.2004;
RA Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M.,
RA Sullivan J.L., Farzan M., Choe H.;
RT "Efficient replication of severe acute respiratory syndrome coronavirus in
RT mouse cells is limited by murine angiotensin-converting enzyme 2.";
RL J. Virol. 78:11429-11433(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16001071; DOI=10.1038/nature03712;
RA Imai Y., Kuba K., Rao S., Huan Y., Guo F., Guan B., Yang P., Sarao R.,
RA Wada T., Leong-Poi H., Crackower M.A., Fukamizu A., Hui C.-C., Hein L.,
RA Uhlig S., Slutsky A.S., Jiang C., Penninger J.M.;
RT "Angiotensin-converting enzyme 2 protects from severe acute lung failure.";
RL Nature 436:112-116(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15949646; DOI=10.1016/j.peptides.2005.01.009;
RA Gembardt F., Sterner-Kock A., Imboden H., Spalteholz M., Reibitz F.,
RA Schultheiss H.-P., Siems W.-E., Walther T.;
RT "Organ-specific distribution of ACE2 mRNA and correlating peptidase
RT activity in rodents.";
RL Peptides 26:1270-1277(2005).
RN [8]
RP FUNCTION.
RX PubMed=18424768; DOI=10.1096/fj.08-107300;
RA Kowalczuk S., Broeer A., Tietze N., Vanslambrouck J.M., Rasko J.E.,
RA Broeer S.;
RT "A protein complex in the brush-border membrane explains a Hartnup disorder
RT allele.";
RL FASEB J. 22:2880-2887(2008).
RN [9]
RP FUNCTION, INTERACTION WITH SLC6A19, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19185582; DOI=10.1053/j.gastro.2008.10.055;
RA Camargo S.M., Singer D., Makrides V., Huggel K., Pos K.M., Wagner C.A.,
RA Kuba K., Danilczyk U., Skovby F., Kleta R., Penninger J.M., Verrey F.;
RT "Tissue-specific amino acid transporter partners ACE2 and collectrin
RT differentially interact with hartnup mutations.";
RL Gastroenterology 136:872-882(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22677001; DOI=10.1042/bj20120307;
RA Fairweather S.J., Broeer A., O'Mara M.L., Broeer S.;
RT "Intestinal peptidases form functional complexes with the neutral amino
RT acid transporter B(0)AT1.";
RL Biochem. J. 446:135-148(2012).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=23535237; DOI=10.1152/ajpcell.00364.2012;
RA Xiao L., Haack K.K., Zucker I.H.;
RT "Angiotensin II regulates ACE and ACE2 in neurons through p38 mitogen-
RT activated protein kinase and extracellular signal-regulated kinase 1/2
RT signaling.";
RL Am. J. Physiol. 304:C1073-C1079(2013).
RN [13]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=32425701; DOI=10.1016/j.devcel.2020.05.012;
RA Smith J.C., Sausville E.L., Girish V., Yuan M.L., Vasudevan A., John K.M.,
RA Sheltzer J.M.;
RT "Cigarette smoke exposure and inflammatory signaling increase the
RT expression of the SARS-CoV-2 receptor ACE2 in the respiratory tract.";
RL Dev. Cell 0:0-0(2020).
CC -!- FUNCTION: Essential counter-regulatory carboxypeptidase of the renin-
CC angiotensin hormone system that is a critical regulator of blood
CC volume, systemic vascular resistance, and thus cardiovascular
CC homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino
CC acid peptide with anti-hypertrophic effects in cardiomyocytes, and
CC angiotensin II to angiotensin 1-7, which then acts as a beneficial
CC vasodilator and anti-proliferation agent, counterbalancing the actions
CC of the vasoconstrictor angiotensin II. Also removes the C-terminal
CC residue from three other vasoactive peptides, neurotensin, kinetensin,
CC and des-Arg bradykinin, but is not active on bradykinin. Also cleaves
CC other biological peptides, such as apelins, casomorphins and dynorphin
CC A (By similarity). By cleavage of angiotensin II, may be an important
CC regulator of heart function (PubMed:12075344, PubMed:12967627). By
CC cleavage of angiotensin II, may also have a protective role in acute
CC lung injury (PubMed:16001071). Plays an important role in amino acid
CC transport by acting as binding partner of amino acid transporter
CC SLC6A19, regulating its trafficking on the cell surface and its
CC activity (PubMed:19185582, PubMed:18424768, PubMed:22677001).
CC {ECO:0000250|UniProtKB:Q9BYF1, ECO:0000269|PubMed:12075344,
CC ECO:0000269|PubMed:12967627, ECO:0000269|PubMed:16001071,
CC ECO:0000269|PubMed:18424768, ECO:0000269|PubMed:19185582,
CC ECO:0000269|PubMed:22677001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine;
CC Xref=Rhea:RHEA:26554, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58506, ChEBI:CHEBI:58922; EC=3.4.17.23;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26555;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin I + H2O = angiotensin-(1-9) + L-leucine;
CC Xref=Rhea:RHEA:63532, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:147350, ChEBI:CHEBI:147351;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63533;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bradykinin(1-8) + H2O = bradykinin(1-7) + L-phenylalanine;
CC Xref=Rhea:RHEA:63536, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:133069, ChEBI:CHEBI:147352;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63537;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-leucine + neurotensin-(1-12);
CC Xref=Rhea:RHEA:63540, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:147362, ChEBI:CHEBI:147363;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63541;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + kinetensin = kinetensin-(1-8) + L-leucine;
CC Xref=Rhea:RHEA:63544, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:147364, ChEBI:CHEBI:147365;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63545;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dynorphin A-(1-13) + H2O = dynorphin A-(1-12) + L-lysine;
CC Xref=Rhea:RHEA:63556, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:147381, ChEBI:CHEBI:147383;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63557;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apelin-13 + H2O = apelin-12 + L-phenylalanine;
CC Xref=Rhea:RHEA:63564, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:147395, ChEBI:CHEBI:147396;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63565;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[Pyr1]apelin-13 + H2O = [Pyr1]apelin-12 + L-phenylalanine;
CC Xref=Rhea:RHEA:63604, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:147415, ChEBI:CHEBI:147416;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63605;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apelin-17 + H2O = apelin-16 + L-phenylalanine;
CC Xref=Rhea:RHEA:63608, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:147421, ChEBI:CHEBI:147422;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63609;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Interacts with the catalytically active form of
CC TMPRSS2 (By similarity). Interacts with SLC6A19; this interaction is
CC essential for expression and function of SLC6A19 in intestine
CC (PubMed:19185582). Interacts with ITGA5:ITGB1 (By similarity). Probably
CC interacts (via endocytic sorting signal motif) with AP2M1; the
CC interaction is inhibited by phosphorylation of Tyr-781 (By similarity).
CC Interacts (via PDZ-binding motif) with NHERF1 (via PDZ domains); the
CC interaction may enhance ACE2 membrane residence (By similarity).
CC {ECO:0000250|UniProtKB:Q9BYF1, ECO:0000269|PubMed:19185582}.
CC -!- SUBUNIT: (Microbial infection) Weakly interacts with SARS-CoV S
CC protein. {ECO:0000269|PubMed:15452268}.
CC -!- INTERACTION:
CC Q8R0I0; A0A6G6A1M4: S; Xeno; NbExp=2; IntAct=EBI-8365920, EBI-26997256;
CC Q8R0I0; A0A6M3G9R1: S; Xeno; NbExp=2; IntAct=EBI-8365920, EBI-26997195;
CC Q8R0I0; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-8365920, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: [Processed angiotensin-converting enzyme 2]:
CC Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23535237};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:23535237}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9BYF1}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9BYF1}. Note=Detected in both cell membrane and
CC cytoplasm in neurons. {ECO:0000269|PubMed:23535237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0I0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R0I0-2; Sequence=VSP_014903;
CC -!- TISSUE SPECIFICITY: Expressed in heart, kidney and forebrain (at
CC protein level). Expressed in the small intestine, with expression in
CC the intestinal brush border (at protein level) (PubMed:19185582,
CC PubMed:22677001). Ubiquitously expressed, with highest levels in ileum,
CC kidney and lung. In lung, expressed on vascular endothelial and airway
CC epithelial cells. Also expressed at high levels in lung secretory club
CC and goblet cells as well as in alveolar type 2 cells (PubMed:32425701).
CC {ECO:0000269|PubMed:12487024, ECO:0000269|PubMed:15949646,
CC ECO:0000269|PubMed:16001071, ECO:0000269|PubMed:19185582,
CC ECO:0000269|PubMed:22677001, ECO:0000269|PubMed:32425701}.
CC -!- INDUCTION: Down-regulated in lung after acute injury. Exposure to
CC cigarette smoke increases ACE2 expression up to 80% more in lungs
CC (PubMed:32425701). {ECO:0000269|PubMed:16001071,
CC ECO:0000269|PubMed:32425701}.
CC -!- DOMAIN: The cytoplasmic tail contains several linear motifs such as
CC LIR, PDZ-binding, PTB and endocytic sorting signal motifs that would
CC allow interaction with proteins that mediate endocytic trafficking and
CC autophagy. {ECO:0000250|UniProtKB:Q9BYF1}.
CC -!- PTM: Proteolytic cleavage by ADAM17 generates a secreted form. Also
CC cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-781 probably inhibits
CC interaction with AP2M1 and enables interactions with proteins
CC containing SH2 domains. {ECO:0000250|UniProtKB:Q9BYF1}.
CC -!- PTM: Ubiquitinated. Ubiquitinated on Lys-788 via 'Lys-48'-linked
CC ubiquitin. 'Lys-48'-linked deubiquitinated by USP50 on the Lys-788;
CC leading to its stabilization. {ECO:0000250|UniProtKB:Q9BYF1}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, exhibit normal
CC kidney and lung function, but show a severe reduction in cardiac
CC contractility, and are highly sensitive to severe acute lung failure
CC (PubMed:12075344). Mutant males exhibit an absence of SLC6A19 in small
CC intestine brush border membranes, but normal SLC6A19 expression in
CC kidney (PubMed:19185582). Abolished sodium-dependent transport of
CC isoleucine in intestinal rings (PubMed:19185582). Transgenic mice
CC overexpressing ACE2 in the heart appear healthy but show conduction
CC disturbances and ventricular arrhythmias which leads to sudden death
CC (PubMed:12075344). {ECO:0000269|PubMed:12075344,
CC ECO:0000269|PubMed:19185582}.
CC -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB40431.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB053181; BAB40431.1; ALT_FRAME; mRNA.
DR EMBL; AB053182; BAB40432.1; -; mRNA.
DR EMBL; BC026801; AAH26801.1; -; mRNA.
DR CCDS; CCDS30518.1; -. [Q8R0I0-1]
DR RefSeq; NP_001123985.1; NM_001130513.1. [Q8R0I0-1]
DR RefSeq; NP_081562.2; NM_027286.4. [Q8R0I0-1]
DR PDB; 7FDK; EM; 3.69 A; A=1-615.
DR PDB; 7WRH; EM; 2.66 A; D=18-615.
DR PDB; 7WRI; EM; 3.03 A; A=18-615.
DR PDB; 7XO4; EM; 3.24 A; D/E=1-805.
DR PDB; 7XO5; EM; 3.13 A; D=1-805.
DR PDB; 7XO6; EM; 2.60 A; D=1-805.
DR PDB; 7XOA; EM; 3.20 A; D=1-805.
DR PDB; 7XOB; EM; 3.30 A; D/E=1-805.
DR PDB; 7XOC; EM; 3.00 A; D=1-805.
DR PDB; 7YVU; EM; 3.20 A; A=19-614.
DR PDB; 8AQT; EM; 4.40 A; A=19-615.
DR PDB; 8AQU; EM; 3.22 A; A=19-615.
DR PDB; 8AQV; EM; 2.96 A; A=19-615.
DR PDB; 8AQW; EM; 3.30 A; A=19-615.
DR PDB; 8DM7; EM; 2.49 A; D/E=1-615.
DR PDB; 8DM8; EM; 2.68 A; D=1-615.
DR PDB; 8DM9; EM; 2.56 A; D=1-615.
DR PDB; 8DMA; EM; 2.79 A; D=1-615.
DR PDBsum; 7FDK; -.
DR PDBsum; 7WRH; -.
DR PDBsum; 7WRI; -.
DR PDBsum; 7XO4; -.
DR PDBsum; 7XO5; -.
DR PDBsum; 7XO6; -.
DR PDBsum; 7XOA; -.
DR PDBsum; 7XOB; -.
DR PDBsum; 7XOC; -.
DR PDBsum; 7YVU; -.
DR PDBsum; 8AQT; -.
DR PDBsum; 8AQU; -.
DR PDBsum; 8AQV; -.
DR PDBsum; 8AQW; -.
DR PDBsum; 8DM7; -.
DR PDBsum; 8DM8; -.
DR PDBsum; 8DM9; -.
DR PDBsum; 8DMA; -.
DR AlphaFoldDB; Q8R0I0; -.
DR EMDB; EMD-27529; -.
DR EMDB; EMD-27530; -.
DR EMDB; EMD-27531; -.
DR EMDB; EMD-27532; -.
DR EMDB; EMD-31546; -.
DR EMDB; EMD-32727; -.
DR EMDB; EMD-33336; -.
DR EMDB; EMD-33337; -.
DR EMDB; EMD-33338; -.
DR EMDB; EMD-33342; -.
DR EMDB; EMD-33343; -.
DR EMDB; EMD-33344; -.
DR EMDB; EMD-34138; -.
DR SMR; Q8R0I0; -.
DR BioGRID; 213814; 2.
DR IntAct; Q8R0I0; 3.
DR STRING; 10090.ENSMUSP00000107890; -.
DR GuidetoPHARMACOLOGY; 1614; -.
DR MEROPS; M02.006; -.
DR GlyCosmos; Q8R0I0; 5 sites, No reported glycans.
DR GlyGen; Q8R0I0; 5 sites.
DR iPTMnet; Q8R0I0; -.
DR PhosphoSitePlus; Q8R0I0; -.
DR jPOST; Q8R0I0; -.
DR MaxQB; Q8R0I0; -.
DR PaxDb; 10090-ENSMUSP00000107890; -.
DR PeptideAtlas; Q8R0I0; -.
DR ProteomicsDB; 285640; -. [Q8R0I0-1]
DR ProteomicsDB; 285641; -. [Q8R0I0-2]
DR Antibodypedia; 344; 1469 antibodies from 47 providers.
DR DNASU; 70008; -.
DR Ensembl; ENSMUST00000073973.11; ENSMUSP00000073626.5; ENSMUSG00000015405.16. [Q8R0I0-1]
DR Ensembl; ENSMUST00000112271.10; ENSMUSP00000107890.4; ENSMUSG00000015405.16. [Q8R0I0-1]
DR GeneID; 70008; -.
DR KEGG; mmu:70008; -.
DR UCSC; uc009uvf.2; mouse. [Q8R0I0-1]
DR AGR; MGI:1917258; -.
DR CTD; 59272; -.
DR MGI; MGI:1917258; Ace2.
DR VEuPathDB; HostDB:ENSMUSG00000015405; -.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000158077; -.
DR HOGENOM; CLU_014364_3_0_1; -.
DR InParanoid; Q8R0I0; -.
DR OMA; FTVIHHE; -.
DR OrthoDB; 2898149at2759; -.
DR PhylomeDB; Q8R0I0; -.
DR TreeFam; TF312861; -.
DR BRENDA; 3.4.17.23; 3474.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR SABIO-RK; Q8R0I0; -.
DR BioGRID-ORCS; 70008; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Ace2; mouse.
DR PRO; PR:Q8R0I0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8R0I0; Protein.
DR Bgee; ENSMUSG00000015405; Expressed in small intestine Peyer's patch and 125 other cell types or tissues.
DR ExpressionAtlas; Q8R0I0; baseline and differential.
DR Genevisible; Q8R0I0; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004180; F:carboxypeptidase activity; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISO:MGI.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; ISO:MGI.
DR GO; GO:0001618; F:virus receptor activity; ISS:UniProtKB.
DR GO; GO:0003051; P:angiotensin-mediated drinking behavior; ISO:MGI.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; ISO:MGI.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0051957; P:positive regulation of amino acid transport; ISO:MGI.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:MGI.
DR GO; GO:1905737; P:positive regulation of L-proline import across plasma membrane; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; ISO:MGI.
DR GO; GO:1903779; P:regulation of cardiac conduction; ISO:MGI.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISO:MGI.
DR GO; GO:0015827; P:tryptophan transport; IMP:CACAO.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR CDD; cd06461; M2_ACE; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR031588; Collectrin_dom.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR PANTHER; PTHR10514:SF24; ANGIOTENSIN-CONVERTING ENZYME 2; 1.
DR Pfam; PF16959; Collectrin; 1.
DR Pfam; PF01401; Peptidase_M2; 1.
DR PRINTS; PR00791; PEPDIPTASEA.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS52010; COLLECTRIN_LIKE; 1.
DR PROSITE; PS52011; PEPTIDASE_M2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane;
KW Cell projection; Chloride; Cytoplasm; Disulfide bond; Glycoprotein;
KW Hydrolase; Isopeptide bond; Membrane; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..805
FT /note="Angiotensin-converting enzyme 2"
FT /id="PRO_0000028571"
FT CHAIN 18..708
FT /note="Processed angiotensin-converting enzyme 2"
FT /id="PRO_0000292269"
FT TOPO_DOM 18..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01354"
FT TOPO_DOM 762..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..607
FT /note="Peptidase M2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT DOMAIN 614..805
FT /note="Collectrin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01354"
FT REGION 652..659
FT /note="Essential for cleavage by ADAM17"
FT /evidence="ECO:0000250"
FT REGION 697..716
FT /note="Essential for cleavage by TMPRSS11D and TMPRSS2"
FT /evidence="ECO:0000250"
FT REGION 771..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 778..786
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 781..785
FT /note="SH2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 781..784
FT /note="Endocytic sorting signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 792..795
FT /note="PTB"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 803..805
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT COMPBIAS 790..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT BINDING 169
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT BINDING 477
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT BINDING 481
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOD_RES 781
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT DISULFID 344..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT DISULFID 530..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT CROSSLNK 788
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT VAR_SEQ 354..805
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12487024"
FT /id="VSP_014903"
FT CONFLICT 167
FT /note="G -> S (in Ref. 1; BAB40432)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="G -> E (in Ref. 1; BAB40432)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="N -> S (in Ref. 1; BAB40431)"
FT /evidence="ECO:0000305"
FT HELIX 23..52
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 56..80
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 110..128
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:7XO6"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 158..193
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:7XO6"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:7XO6"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 222..249
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:8AQV"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:7XO6"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:8AQU"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:8AQV"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:7XOC"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7XOC"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 366..384
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:7XO5"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 415..420
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:8AQU"
FT HELIX 432..445
FT /evidence="ECO:0007829|PDB:7XO6"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 449..464
FT /evidence="ECO:0007829|PDB:7XO6"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:7WRI"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 514..532
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 548..558
FT /evidence="ECO:0007829|PDB:7XO6"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 566..571
FT /evidence="ECO:0007829|PDB:7XO6"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:7XOC"
FT HELIX 582..587
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 589..598
FT /evidence="ECO:0007829|PDB:7XO6"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:7XO6"
SQ SEQUENCE 805 AA; 92368 MW; D8B883AAC966A8D9 CRC64;
MSSSSWLLLS LVAVTTAQSL TEENAKTFLN NFNQEAEDLS YQSSLASWNY NTNITEENAQ
KMSEAAAKWS AFYEEQSKTA QSFSLQEIQT PIIKRQLQAL QQSGSSALSA DKNKQLNTIL
NTMSTIYSTG KVCNPKNPQE CLLLEPGLDE IMATSTDYNS RLWAWEGWRA EVGKQLRPLY
EEYVVLKNEM ARANNYNDYG DYWRGDYEAE GADGYNYNRN QLIEDVERTF AEIKPLYEHL
HAYVRRKLMD TYPSYISPTG CLPAHLLGDM WGRFWTNLYP LTVPFAQKPN IDVTDAMMNQ
GWDAERIFQE AEKFFVSVGL PHMTQGFWAN SMLTEPADGR KVVCHPTAWD LGHGDFRIKM
CTKVTMDNFL TAHHEMGHIQ YDMAYARQPF LLRNGANEGF HEAVGEIMSL SAATPKHLKS
IGLLPSDFQE DSETEINFLL KQALTIVGTL PFTYMLEKWR WMVFRGEIPK EQWMKKWWEM
KREIVGVVEP LPHDETYCDP ASLFHVSNDY SFIRYYTRTI YQFQFQEALC QAAKYNGSLH
KCDISNSTEA GQKLLKMLSL GNSEPWTKAL ENVVGARNMD VKPLLNYFQP LFDWLKEQNR
NSFVGWNTEW SPYADQSIKV RISLKSALGA NAYEWTNNEM FLFRSSVAYA MRKYFSIIKN
QTVPFLEEDV RVSDLKPRVS FYFFVTSPQN VSDVIPRSEV EDAIRMSRGR INDVFGLNDN
SLEFLGIHPT LEPPYQPPVT IWLIIFGVVM ALVVVGIIIL IVTGIKGRKK KNETKREENP
YDSMDIGKGE SNAGFQNSDD AQTSF
//
