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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_MESAU               Reviewed;        1314 AA.
Q50JE5;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
25-OCT-2017, entry version 66.
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;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=17343204; DOI=10.1080/10425170600724816;
Uchide T., Fujimori Y., Fukushima U., Uechi M., Sasaki T., Temma K.;
"cDNA cloning of hamster angiotensin-converting enzyme and mRNA
expression.";
DNA Seq. 17:319-325(2006).
-!- 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. {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=Q50JE5-1; Sequence=Displayed;
Name=Testis-specific; Synonyms=ACE-T;
IsoId=Q50JE5-2; Sequence=Not described;
-!- TISSUE SPECIFICITY: Widely expressed with dominant expression in
lung and kidney. {ECO:0000269|PubMed:17343204}.
-!- PTM: Phosphorylated by CK2 on Ser-1307; which allows membrane
retention. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB212958; BAD98304.1; -; mRNA.
RefSeq; NP_001268510.1; NM_001281581.1. [Q50JE5-1]
ProteinModelPortal; Q50JE5; -.
SMR; Q50JE5; -.
MEROPS; M02.001; -.
PRIDE; Q50JE5; -.
GeneID; 101824864; -.
HOVERGEN; HBG000264; -.
OrthoDB; EOG091G033S; -.
BRENDA; 3.4.15.1; 3239.
Proteomes; UP000189706; Genome assembly.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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.
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.
2: Evidence at transcript level;
Alternative splicing; Carboxypeptidase; Cell membrane;
Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 35 {ECO:0000250}.
CHAIN 36 1314 Angiotensin-converting enzyme.
/FTId=PRO_0000028536.
CHAIN 36 1238 Angiotensin-converting enzyme, soluble
form.
/FTId=PRO_0000028537.
PROPEP 1239 1314 Removed in secreted form. {ECO:0000250}.
/FTId=PRO_0000028538.
TOPO_DOM 36 1265 Extracellular. {ECO:0000255}.
TRANSMEM 1266 1282 Helical. {ECO:0000255}.
TOPO_DOM 1283 1314 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 1307 1307 Phosphoserine.
{ECO:0000250|UniProtKB:P12821}.
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 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}.
DISULFID 163 171 {ECO:0000250}.
DISULFID 763 769 {ECO:0000250}.
DISULFID 963 981 {ECO:0000250}.
DISULFID 1149 1161 {ECO:0000250}.
SEQUENCE 1314 AA; 151595 MW; 74E29238E87F157E CRC64;
MGAASGQRGQ GPPSPLLLLW LSLLLLLLPP SPAPALDPGL QPGNFSADEI GAHLFAESYN
SSAEQVIFQS TVASWAYDTN MTEENARLQE EAELIWQEFA EVWGKKAKEL FDAIRQNFTD
SKLRRVIETI RTLGPANLPL ARRQQYNSLQ NNMNRIYSTS KVCLPNKTAT CWSLEPELTN
ILASSRSYAK LLFAWESWHD VVGIPLKPLY QDFTALSNEA YKQDGFSDTG AYWRSAYDSP
SFEETLEHLY HQLEPLYLNL HAYVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWDNIY
DMVVPFPNKP NLDVTNTMVQ KGWNVTHMFR VAEEFFTSMG LSPMPPEFWA ESMLEKPTDG
REVVCHASAW DFFNRKDFRI KQCTRITMEQ LSTVHHEMGH VQYYLQYKDL TVPLRRGANP
GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA NDLESDINYL LKMALEKIAF LPFGYLVDQW
RWGVFSGHTP PSRYNFDWWY FRTKYQGICP PVVRNETHFD AGAKFHIPSG TPYIRYFVSF
ILQFQFHQAL CKEAGHQGPL HQCDIYQSTQ AGAKLQRVLQ AGYSRPWQEV LKEMVGSDTL
DAQALLEYFQ PVIRWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLVT DETEAERFVE
EYDRTARVLW NEYAEANWQY NTNITLEASK ILLQKNKKVA NHTLKYGTLA KKFDVSNFQN
YTIKRIIKKV QNMDRAVLPP KELEEYNQIL MDMETTYSIA NVCYLNGTCL HLEPDLTNVM
ATSRKYEELL WVWKSWRDKV GRAILPLFPK YVELSNKIAH LNGYADGGDS WRSSYESKSL
EQDLEQLYQE LQPLYLNLHA YVRRSLHRHY GSQHINLDGP IPAHLLGNMW AQTWSNIYDL
VAPFPSAPNL DATEAMIKQG WTPRRIFKEA DDFFTSLGLL PVSEEFWNKS MLEKPGDGRE
VVCHASAWDF YNGKDFRIKQ CTSVNMEDLV IAHHEMGHIQ YFMQYKDLPV TFREGANPGF
HEAIGDVLAL SVSTPKHLHS LNLLSSEGGG YEHDINFLMK MALDKIAFIP FSYLIDQWRW
RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRSQDDFDPG SKFHVPANVP YIRYFVSFII
QFQFHEALCR AAGHTGPLHK CDIYQSKEAG KLLADTMKMG YSKPWPEAMK LITGQPNMSA
SAMMNYFKPL TEWLVTENRR HGETLGWPEY NWTPNTARSE GPFPESGRVN FLGMYLEPQQ
ARVGQWVLLF LGVSLLVATL GLTHRLFSIR QHGHSLHRPH RGPQFGSEVE LRHS


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