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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_RAT                 Reviewed;        1313 AA.
P47820; Q7TMC6; Q8CFN1; Q9EQM9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 154.
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=Dcp1;
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] (ISOFORM SOMATIC), AND VARIANT LYS-207.
TISSUE=Lung;
PubMed=8292044; DOI=10.1006/bbrc.1994.1053;
Koike G., Krieger J.E., Jacob H.J., Mukoyama M., Pratt R.E.,
Dzau V.J.;
"Angiotensin converting enzyme and genetic hypertension: cloning of
rat cDNAs and characterization of the enzyme.";
Biochem. Biophys. Res. Commun. 198:380-386(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
STRAIN=Fischer 344/N, and Lewis/N; TISSUE=Lung;
Jafarian-Tehrani M., Listwak S., Barrientos R.M., Michaud A.,
Corvol P., Sternberg E.M.;
"Characterization of a missense mutation in the angiotensin I-
converting enzyme cDNA in exudative inflammation resistant F344/N
rats.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=12963491; DOI=10.1016/S0006-2952(03)00457-X;
Tian X.-L., Paul M.;
"Species-specific splicing and expression of angiotensin converting
enzyme.";
Biochem. Pharmacol. 66:1037-1044(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SOMATIC).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-1313 (ISOFORM SOMATIC), AND VARIANT
LYS-207.
TISSUE=Kidney;
Tsetsarkin K.A., Dymshits G.M., Markel A.L., Redina O.E.;
"Analysis of the angiotensin converting enzyme (Ace) cDNA sequence and
mRNA level of expression in WAG and ISIAH rats.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. This GPIase activity seems
to be crucial for the egg-binding ability of the sperm (By
similarity). {ECO:0000250}.
-!- 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; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. Isoform Testis-specific only
binds 1 Zn(2+) ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
Note=Binds 3 chloride ions per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Somatic;
IsoId=P47820-1; Sequence=Displayed;
Name=Testis-specific; Synonyms=ACE-T;
IsoId=P47820-2, Q8CFN1-1;
Sequence=VSP_037642, VSP_037643;
-!- TISSUE SPECIFICITY: Testis-specific isoform is expressed in
spermatocytes, adult testis. Also expressed in brain, kidney,
lung, skeletal muscle and heart. {ECO:0000269|PubMed:12963491}.
-!- INDUCTION: Up-regulated after myocardial infarction.
{ECO:0000269|PubMed:15671045}.
-!- PTM: Phosphorylated by CK2 on Ser-1306; which allows membrane
retention. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U03708; AAA82110.1; -; mRNA.
EMBL; U03734; AAA82111.1; -; mRNA.
EMBL; AF201331; AAG35596.1; -; mRNA.
EMBL; AF201332; AAG35597.1; -; mRNA.
EMBL; AF539425; AAN17280.1; -; mRNA.
EMBL; BC085760; AAH85760.1; -; mRNA.
EMBL; AF532783; AAP80808.1; -; mRNA.
EMBL; AF532784; AAP80809.1; -; mRNA.
PIR; JC2038; JC2038.
RefSeq; NP_036676.1; NM_012544.1.
UniGene; Rn.10149; -.
ProteinModelPortal; P47820; -.
SMR; P47820; -.
MINT; MINT-204637; -.
STRING; 10116.ENSRNOP00000010627; -.
BindingDB; P47820; -.
ChEMBL; CHEMBL2625; -.
GuidetoPHARMACOLOGY; 1613; -.
MEROPS; M02.001; -.
iPTMnet; P47820; -.
PhosphoSitePlus; P47820; -.
UniCarbKB; P47820; -.
PaxDb; P47820; -.
PRIDE; P47820; -.
GeneID; 24310; -.
KEGG; rno:24310; -.
UCSC; RGD:2493; rat. [P47820-1]
CTD; 1636; -.
RGD; 2493; Ace.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
HOGENOM; HOG000007838; -.
HOVERGEN; HBG000264; -.
InParanoid; P47820; -.
KO; K01283; -.
PhylomeDB; P47820; -.
TreeFam; TF312861; -.
BRENDA; 3.4.15.1; 5301.
PRO; PR:P47820; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
GO; GO:0031526; C:brush border membrane; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005768; C:endosome; ISO:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005764; C:lysosome; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0097225; C:sperm midpiece; IDA:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0003779; F:actin binding; ISO:RGD.
GO; GO:0031711; F:bradykinin receptor binding; ISO:RGD.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031404; F:chloride ion binding; ISO:RGD.
GO; GO:0008144; F:drug binding; IPI:RGD.
GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
GO; GO:0008238; F:exopeptidase activity; ISO:RGD.
GO; GO:0070573; F:metallodipeptidase activity; ISO:RGD.
GO; GO:0008237; F:metallopeptidase activity; IMP:RGD.
GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:RGD.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:RGD.
GO; GO:0008233; F:peptidase activity; ISO:RGD.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:RGD.
GO; GO:0008240; F:tripeptidyl-peptidase activity; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0050435; P:amyloid-beta metabolic process; ISO:RGD.
GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IMP:RGD.
GO; GO:0031100; P:animal organ regeneration; IMP:RGD.
GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
GO; GO:0010815; P:bradykinin catabolic process; IDA:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0071838; P:cell proliferation in bone marrow; ISO:RGD.
GO; GO:1904045; P:cellular response to aldosterone; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0042755; P:eating behavior; IMP:RGD.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0060047; P:heart contraction; ISO:RGD.
GO; GO:0042447; P:hormone catabolic process; ISO:RGD.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0048286; P:lung alveolus development; IMP:RGD.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0097756; P:negative regulation of blood vessel diameter; IMP:RGD.
GO; GO:0090281; P:negative regulation of calcium ion import; IMP:RGD.
GO; GO:1903597; P:negative regulation of gap junction assembly; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0046325; P:negative regulation of glucose import; IMP:RGD.
GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
GO; GO:0002446; P:neutrophil mediated immunity; ISO:RGD.
GO; GO:0043171; P:peptide catabolic process; IDA:RGD.
GO; GO:0006518; P:peptide metabolic process; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:RGD.
GO; GO:0050769; P:positive regulation of neurogenesis; IMP:RGD.
GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; ISO:RGD.
GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; ISO:RGD.
GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:RGD.
GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:RGD.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; ISO:RGD.
GO; GO:0060177; P:regulation of angiotensin metabolic process; ISO:RGD.
GO; GO:0008217; P:regulation of blood pressure; IDA:BHF-UCL.
GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; ISO:RGD.
GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISO:RGD.
GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
GO; GO:0007283; P:spermatogenesis; ISO:RGD.
GO; GO:0042310; P:vasoconstriction; IMP:RGD.
CDD; cd06461; M2_ACE; 2.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 2.
Pfam; PF01401; Peptidase_M2; 2.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 2.
1: Evidence at protein level;
Alternative splicing; Carboxypeptidase; Cell membrane;
Complete proteome; Cytoplasm; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism;
Protease; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 35 {ECO:0000250}.
CHAIN 36 1313 Angiotensin-converting enzyme.
/FTId=PRO_0000028557.
CHAIN 36 1238 Angiotensin-converting enzyme, soluble
form.
/FTId=PRO_0000028558.
PROPEP 1239 1313 Removed in secreted form. {ECO:0000250}.
/FTId=PRO_0000028559.
TOPO_DOM 36 1265 Extracellular. {ECO:0000255}.
TRANSMEM 1266 1282 Helical. {ECO:0000255}.
TOPO_DOM 1283 1313 Cytoplasmic. {ECO:0000255}.
REGION 36 636 Peptidase M2 1.
REGION 637 1238 Peptidase M2 2.
ACT_SITE 397 397 1. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
ACT_SITE 995 995 2. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 396 396 Zinc 1; catalytic. {ECO:0000250}.
METAL 400 400 Zinc 1; catalytic. {ECO:0000250}.
METAL 424 424 Zinc 1; catalytic. {ECO:0000250}.
METAL 994 994 Zinc 2; catalytic. {ECO:0000250}.
METAL 998 998 Zinc 2; catalytic. {ECO:0000250}.
METAL 1022 1022 Zinc 2; catalytic. {ECO:0000250}.
BINDING 237 237 Chloride 1. {ECO:0000250}.
BINDING 535 535 Chloride 1. {ECO:0000250}.
BINDING 797 797 Chloride 2. {ECO:0000250}.
BINDING 835 835 Chloride 3. {ECO:0000250}.
BINDING 1096 1096 Chloride 2. {ECO:0000250}.
BINDING 1100 1100 Chloride 2. {ECO:0000250}.
BINDING 1133 1133 Chloride 3. {ECO:0000250}.
MOD_RES 1306 1306 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 683 683 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 701 701 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 720 720 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 766 766 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 948 948 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1197 1197 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 581 Missing (in isoform Testis-specific).
{ECO:0000303|PubMed:12963491}.
/FTId=VSP_037642.
VAR_SEQ 582 646 GCSRPWQEVLKDLVGSDALDASALMEYFQPVSQWLQEQNQR
NGEVLGWPEYQWRPPLPDNYPEGI -> MGQGWATPGLPRF
LFLLLCCGHLLPVLSQVAADHVTANQGITNQATTRSQTTHQ
STISQTIQTSNGTPGRGQGHEGARSQGPAGGNSNKTTPCGK
EGEACLFSSSPPT (in isoform Testis-
specific). {ECO:0000303|PubMed:12963491}.
/FTId=VSP_037643.
VARIANT 207 207 R -> K. {ECO:0000269|PubMed:8292044,
ECO:0000269|Ref.5}.
CONFLICT 341 341 L -> F (in Ref. 2; AAG35596).
{ECO:0000305}.
SEQUENCE 1313 AA; 150908 MW; 8CB5D0015F129591 CRC64;
MGAASGQRGR WPLSPPLLML SLLLLLLLPP SPAPALDPGL QPGNFSADEA GAQLFADSYN
SSAEVVMFQS TAASWAHDTN ITEENARLQE EAALINQEFA EVWGKKAKEL YESIWQNFTD
QKLRRIIGSV QTLGPANLPL TQRLQYNSLL SNMSRIYSTG KVCFPNKTAT CWSLDPELTN
ILASSRNYAK VLFAWEGWHD AVGIPLRPLY QDFTALSNEA YRQDGFSDTG AYWRSWYESP
SFEESLEHLY HQVEPLYLNL HAFVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWENIY
DMVVPFPDKP NLDVTSTMVQ KGWNATHMFR VAEEFFTSLG LSPMPPEFWA ESMLEKPADG
REVVCHASAW DFYNRKDFRI KQCTRVTMDQ LSTVHHEMGH VQYYLQYKDL HVSLRRGANP
GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA NDIESDINYL LKMALEKIAF LPFGYLVDQW
RWGVFSGRTP PSRYNYDWWY LRTKYQGICP PVARNETHFD AGAKFHIPSV TPYIRYFVSF
VLQFQFHQAL CKEAGHQGPL HQCDIYQSTK AGAKLQQVLQ AGCSRPWQEV LKDLVGSDAL
DASALMEYFQ PVSQWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLET DEAKANRFVE
EYDRTAKVLW NEYAEANWHY NTNITIEGSK ILLQKNKEVS NHTLKYGTWA KTFDVSNFQN
STIKRIIKKV QNVDRAVLPP NELEEYNQIL LDMETTYSVA NVCYTNGTCL SLEPDLTNIM
ATSRKYEELL WVWKSWRDKV GRAILPFFPK YVDFSNKIAK LNGYSDAGDS WRSSYESDDL
EQDLEKLYQE LQPLYLNLHA YVRRSLHRHY GSEYINLDGP IPAHLLGNMW AQTWSNIYDL
VAPFPSAPSI DATEAMIKQG WTPRRIFKEA DNFFTSLGLL PVPPEFWNKS MLEKPTDGRE
VVCHASAWDF YNGKDFRIKQ CTSVNMEELV IAHHEMGHIQ YFMQYKDLPV TFREGANPGF
HEAIGDVLAL SVSTPKHLHS LNLLSSEGSG YEHDINFLMK MALDKIAFIP FSYLIDQWRW
RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRSQGDFDPG SKFHVPANVP YIRYFISFII
QFQFHEALCR AAGHTGPLYK CDIYQSKEAG KLLADAMKLG YSKQWPEAMK IITGQPNMSA
SAIMNYFKPL TEWLVTENRR HGETLGWPEY TWTPNTARAE GSLPESSRVN FLGMYLEPQQ
ARVGQWVLLF LGVALLVATV GLAHRLYNIH NHHSLRRPHR GPQFGSEVEL RHS


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E0004h ELISA ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
U1886h CLIA kit ACE2,ACEH,ACE-related carboxypeptidase,Angiotensin-converting enzyme 2,Angiotensin-converting enzyme homolog,Homo sapiens,Human,Metalloprotease MPROT15,UNQ868_PRO1885 96T
E1886h ELISA kit ACE2,ACEH,ACE-related carboxypeptidase,Angiotensin-converting enzyme 2,Angiotensin-converting enzyme homolog,Homo sapiens,Human,Metalloprotease MPROT15,UNQ868_PRO1885 96T


 

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