ID   ACE_HAEIX               Reviewed;         611 AA.
AC   Q10715;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Angiotensin-converting enzyme;
DE            EC=3.4.15.1;
DE   AltName: Full=Dipeptidyl carboxypeptidase I;
DE   AltName: Full=Kininase II;
DE   Flags: Precursor;
GN   Name=ACE;
OS   Haematobia irritans exigua (Buffalo fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Haematobia.
OX   NCBI_TaxID=34678;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8647080; DOI=10.1111/j.1432-1033.1996.0414k.x;
RA   Wijffels G.L., Fitzgerald C., Gough J., Riding G.A., Elvin C., Kemp D.J.,
RA   Willadsen P.;
RT   "Cloning and characterisation of angiotensin-converting enzyme from the
RT   dipteran species, Haematobia irritans exigua, and its expression in the
RT   maturing male reproductive system.";
RL   Eur. J. Biochem. 237:414-423(1996).
CC   -!- FUNCTION: Involved in the specific maturation or degradation of a
CC       number of bioactive peptides.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the compound ganglion and in the
CC       posterior region of the midgut.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L43965; AAA70427.1; -; Genomic_DNA.
DR   PIR; S65472; S65472.
DR   AlphaFoldDB; Q10715; -.
DR   SMR; Q10715; -.
DR   MEROPS; M02.003; -.
DR   GlyCosmos; Q10715; 3 sites, No reported glycans.
DR   GO; GO:0005576; C:extracellular region; 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   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS52011; PEPTIDASE_M2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..611
FT                   /note="Angiotensin-converting enzyme"
FT                   /id="PRO_0000028565"
FT   DOMAIN          19..607
FT                   /note="Peptidase M2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        368
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        497
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        531
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        133..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        336..354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        522..540
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
SQ   SEQUENCE   611 AA;  70506 MW;  A43D6DF5A83ECB53 CRC64;
     MKLLVVTILA GLAVCHGATK EEIVATEYLQ NINKELAKHT NVETEVSWAY ASNITDENER
     LRNEISAENA KFLKEVAKDI QKFNWRTYGS ADVRRQFKSL SKTGYSALPA EDYAELLEVL
     SAMESNFAKV RVCDYKNSAK CDLSLDPEIE EIITKSRDPE ELKYYWTQFY DKAGTPTRSN
     FEKYVELNTK SAKLNNFTDG AEVWLDEYED ATFEDQLEAI FEDIKPLYDQ VHGYVRYRLN
     KFYGDEVVSK TGPLPMHLLG NMWAQQWSSI ADIVSPFPEK PLVDVSDEMV AQGYTPLKMF
     QMGDDFFQSM GLKKLPQEFW DKSILEKPDD GRDLVCHASA WDFYLTDDVR IKQCTRVTQD
     QFFTVHHEMG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV LSLSVSTPKH LERVGLLKNY
     VSDNEARINQ LFLTALDKIV FLPFAFTMDK YRWALFRGQA DKSEWNCAFW KLREEYSGIE
     PPVVRTEKDF DAPAKYHVSA DVEYLRYLVS FIIQFQFYKS ACITAGEYVP NQTEYPLDNC
     DIYGSKEAGK LFENMLSLGA SKPWPDALEA FNGERTMTGK AIAEYFEPLR VWLEAVAVES
     LCHQRYKNVD L
//