ID   ACE_THETS               Reviewed;         616 AA.
AC   Q6Q4G4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Angiotensin-converting enzyme;
DE            EC=3.4.15.1;
DE   AltName: Full=Dipeptidyl carboxypeptidase I;
DE   AltName: Full=Kininase II;
DE   AltName: Full=TtACE;
DE   Flags: Precursor;
GN   Name=ACE;
OS   Theromyzon tessulatum (Duck leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Theromyzon.
OX   NCBI_TaxID=13286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, ACTIVITY REGULATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=15175004; DOI=10.1042/bj20040522;
RA   Riviere G., Michaud A., Deloffre L., Vandenbulcke F., Levoye A., Breton C.,
RA   Corvol P., Salzet M., Vieau D.;
RT   "Characterization of the first non-insect invertebrate functional
RT   angiotensin-converting enzyme (ACE): leech TtACE resembles the N-domain of
RT   mammalian ACE.";
RL   Biochem. J. 382:565-573(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa,
CC         when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion
CC         of angiotensin I to angiotensin II, with increase in vasoconstrictor
CC         activity, but no action on angiotensin II.; EC=3.4.15.1;
CC         Evidence={ECO:0000269|PubMed:15175004};
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=Chloride. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by chloride. Inhibited by captopril and
CC       lisinopril, and to a lesser extent by delaprilat.
CC       {ECO:0000269|PubMed:15175004}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Epithelial cells of the midgut.
CC       {ECO:0000269|PubMed:15175004}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at stages 1 and 2.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
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DR   EMBL; AY560004; AAS57725.1; -; mRNA.
DR   AlphaFoldDB; Q6Q4G4; -.
DR   SMR; Q6Q4G4; -.
DR   MEROPS; M02.005; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06461; M2_ACE; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..616
FT                   /note="Angiotensin-converting enzyme"
FT                   /id="PRO_0000028566"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         380
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        535
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   616 AA;  71481 MW;  70171D38354349FC CRC64;
     MNLINFSYLN LLFGAGLFSV LESATILNTE SDAKKWLTTY NDEAGKYIYD ATEAEWNYNT
     NLTDHNLGIS IKKSNDLATF TEQKAIEANK KFVWKNFTDP LLKREFSKIT DIGTASLSDE
     DFQKMSGLNS DLTKIYSTAK VCNKPNDPSG KCYPLDPDLS DIISKSNDLE ELTWAWKGWR
     DASGKHMPDK YDEFVQLLNK AANINGYEDN GDYWRSWYES PTFRKDCEDL WQEIKPFYEQ
     LHAYVRRKLQ KKYPQIAFPK EGHIPAHLLG NMWAQSWENI EYLLRPAPDL PSMDITEELV
     KQNYTALKLF QLSDTFFKSL GLIQMPQPFW EKSMIEKPAD RDVVCHASAW DFYNRKDFRI
     KQCTVVDMHW FMTTHHEMGH IEYYLHYKDQ PISFRSGANP GFHEAIADIA SLSVATPEYM
     QSVSLLPNFT DDPNGDLNFL MNQALTKVAF LPFGYLIDQW RWDVFSGDTP RPKYNSKWWH
     NRCKYQGVYP PVIRSEQDFD AGSKFHVPNN TPYIRYFVAH IIQFQFHEAL CKAANNSRPL
     HRCNIANSKE AGKKLAELMK SGSSIPWPKV LENLTGSEKM SAKSLMAYYK PLIDWPEKRK
     PRAENWMGGK MSSWIV