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Angiotensin-converting enzyme 2 (EC 3.4.17.23) (ACE-related carboxypeptidase) [Cleaved into: Processed angiotensin-converting enzyme 2]

 ACE2_RAT                Reviewed;         805 AA.
Q5EGZ1;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
23-MAY-2018, entry version 95.
RecName: Full=Angiotensin-converting enzyme 2;
EC=3.4.17.23;
AltName: Full=ACE-related carboxypeptidase;
Contains:
RecName: Full=Processed angiotensin-converting enzyme 2;
Flags: Precursor;
Name=Ace2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND LACK OF INTERACTION WITH SARS-COV
SPIKE GLYCOPROTEIN.
STRAIN=Sprague-Dawley;
PubMed=15452268; DOI=10.1128/JVI.78.20.11429-11433.2004;
Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M.,
Sullivan J.L., Farzan M., Choe H.;
"Efficient replication of severe acute respiratory syndrome
coronavirus in mouse cells is limited by murine angiotensin-converting
enzyme 2.";
J. Virol. 78:11429-11433(2004).
[2]
FUNCTION, AND INDUCTION.
PubMed=12075344; DOI=10.1038/nature00786;
Crackower M.A., Sarao R., Oudit G.Y., Yagil C., Kozieradzki I.,
Scanga S.E., Oliveira-dos-Santos A.J., da Costa J., Zhang L., Pei Y.,
Scholey J., Ferrario C.M., Manoukian A.S., Chappell M.C., Backx P.H.,
Yagil Y., Penninger J.M.;
"Angiotensin-converting enzyme 2 is an essential regulator of heart
function.";
Nature 417:822-828(2002).
[3]
ENZYME REGULATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=15231706; DOI=10.1210/en.2004-0443;
Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A.,
Smith A.I., Lew R.A.;
"The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is
selectively expressed by adult Leydig cells of the testis.";
Endocrinology 145:4703-4711(2004).
[4]
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).
[5]
TISSUE SPECIFICITY.
PubMed=15949646; DOI=10.1016/j.peptides.2005.01.009;
Gembardt F., Sterner-Kock A., Imboden H., Spalteholz M., Reibitz F.,
Schultheiss H.-P., Siems W.-E., Walther T.;
"Organ-specific distribution of ACE2 mRNA and correlating peptidase
activity in rodents.";
Peptides 26:1270-1277(2005).
-!- FUNCTION: Carboxypeptidase which converts angiotensin I to
angiotensin 1-9, a peptide of unknown function, and angiotensin II
to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-
13 and dynorphin-13 with high efficiency. May be an important
regulator of heart function. {ECO:0000269|PubMed:12075344}.
-!- CATALYTIC ACTIVITY: Angiotensin II + H(2)O = angiotensin-(1-7) +
L-phenylalanine.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Activated by chloride and fluoride, but not
bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the
ACE inhibitors linosipril, captopril, enalaprilat.
{ECO:0000269|PubMed:15231706}.
-!- SUBUNIT: Interacts with ITGB1 and the catalytically active form of
TMPRSS2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed angiotensin-converting enzyme 2:
Secreted {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
Note=Detected in both cell membrane and cytoplasm in neurons.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in heart, kidney and forebrain. In
testis, expression is restricted to Leydig cells. In heart,
expressed in endothelial cells from small and large arteries,
arterial smooth muscle cells, and myocytes (at protein level).
Ubiquitously expressed, with highest levels in ileum, bladder and
lung. {ECO:0000269|PubMed:15231706, ECO:0000269|PubMed:15671045,
ECO:0000269|PubMed:15949646}.
-!- INDUCTION: Down-regulated in hypertensive animals. Up-regulated
after myocardial infarction. {ECO:0000269|PubMed:12075344,
ECO:0000269|PubMed:15671045}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:15231706}.
-!- PTM: Proteolytic cleavage by ADAM17 generates a secreted form.
Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and
HPN/TMPRSS1 (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: In contrast to its human and palm-civet orthologs,
does not interact with SARS-CoV spike glycoprotein.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY881244; AAW78017.1; -; mRNA.
RefSeq; NP_001012006.1; NM_001012006.1.
UniGene; Rn.230337; -.
ProteinModelPortal; Q5EGZ1; -.
SMR; Q5EGZ1; -.
STRING; 10116.ENSRNOP00000047913; -.
BindingDB; Q5EGZ1; -.
ChEMBL; CHEMBL2311; -.
MEROPS; M02.006; -.
SwissPalm; Q5EGZ1; -.
PaxDb; Q5EGZ1; -.
PRIDE; Q5EGZ1; -.
GeneID; 302668; -.
KEGG; rno:302668; -.
UCSC; RGD:728890; rat.
CTD; 59272; -.
RGD; 728890; Ace2.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
HOVERGEN; HBG000265; -.
InParanoid; Q5EGZ1; -.
KO; K09708; -.
PhylomeDB; Q5EGZ1; -.
BRENDA; 3.4.17.23; 5301.
PRO; PR:Q5EGZ1; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004180; F:carboxypeptidase activity; IDA:CACAO.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
GO; GO:0001618; F:virus receptor activity; ISS:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
CDD; cd06461; M2_ACE; 1.
InterPro; IPR031588; Collectrin_dom.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 1.
Pfam; PF16959; Collectrin; 1.
Pfam; PF01401; Peptidase_M2; 1.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Carboxypeptidase; Cell membrane; Chloride; Complete proteome;
Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Protease; Reference proteome;
Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 805 Angiotensin-converting enzyme 2.
/FTId=PRO_0000028574.
CHAIN 18 708 Processed angiotensin-converting enzyme
2.
/FTId=PRO_0000292272.
TOPO_DOM 18 740 Extracellular. {ECO:0000255}.
TRANSMEM 741 761 Helical. {ECO:0000255}.
TOPO_DOM 762 805 Cytoplasmic. {ECO:0000255}.
REGION 652 659 Essential for cleavage by ADAM17.
{ECO:0000250}.
REGION 697 716 Essential for cleavage by TMPRSS11D and
TMPRSS2. {ECO:0000250}.
ACT_SITE 375 375 {ECO:0000255|PROSITE-ProRule:PRU10095}.
ACT_SITE 505 505 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 374 374 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 378 378 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 402 402 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
BINDING 169 169 Chloride. {ECO:0000250}.
BINDING 273 273 Substrate. {ECO:0000250}.
BINDING 345 345 Substrate. {ECO:0000250}.
BINDING 346 346 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 371 371 Substrate. {ECO:0000250}.
BINDING 477 477 Chloride. {ECO:0000250}.
BINDING 481 481 Chloride. {ECO:0000250}.
BINDING 515 515 Substrate. {ECO:0000250}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 601 601 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 660 660 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 133 141 {ECO:0000250}.
DISULFID 344 361 {ECO:0000250}.
DISULFID 530 542 {ECO:0000250}.
SEQUENCE 805 AA; 92491 MW; A4079F2407960D28 CRC64;
MSSSCWLLLS LVAVATAQSL IEEKAESFLN KFNQEAEDLS YQSSLASWNY NTNITEENAQ
KMNEAAAKWS AFYEEQSKIA QNFSLQEIQN ATIKRQLKAL QQSGSSALSP DKNKQLNTIL
NTMSTIYSTG KVCNSMNPQE CFLLEPGLDE IMATSTDYNR RLWAWEGWRA EVGKQLRPLY
EEYVVLKNEM ARANNYEDYG DYWRGDYEAE GVEGYNYNRN QLIEDVENTF KEIKPLYEQL
HAYVRTKLME VYPSYISPTG CLPAHLLGDM WGRFWTNLYP LTTPFLQKPN IDVTDAMVNQ
SWDAERIFKE AEKFFVSVGL PQMTPGFWTN SMLTEPGDDR KVVCHPTAWD LGHGDFRIKM
CTKVTMDNFL TAHHEMGHIQ YDMAYAKQPF LLRNGANEGF HEAVGEIMSL SAATPKHLKS
IGLLPSNFQE DNETEINFLL KQALTIVGTL PFTYMLEKWR WMVFQDKIPR EQWTKKWWEM
KREIVGVVEP LPHDETYCDP ASLFHVSNDY SFIRYYTRTI YQFQFQEALC QAAKHDGPLH
KCDISNSTEA GQKLLNMLSL GNSGPWTLAL ENVVGSRNMD VKPLLNYFQP LFVWLKEQNR
NSTVGWSTDW SPYADQSIKV RISLKSALGK NAYEWTDNEM YLFRSSVAYA MREYFSREKN
QTVPFGEADV WVSDLKPRVS FNFFVTSPKN VSDIIPRSEV EEAIRMSRGR INDIFGLNDN
SLEFLGIYPT LKPPYEPPVT IWLIIFGVVM GTVVVGIVIL IVTGIKGRKK KNETKREENP
YDSMDIGKGE SNAGFQNSDD AQTSF


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