ID   Q4ACT8_PIG              Unreviewed;       745 AA.
AC   Q4ACT8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=tACE {ECO:0000313|EMBL:BAE16967.2};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:BAE16967.2};
RN   [1] {ECO:0000313|EMBL:BAE16967.2}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis {ECO:0000313|EMBL:BAE16967.2};
RX   PubMed=17145192; DOI=10.1016/j.cbpb.2006.10.108;
RA   Takeuchi K., Araki H., Sakaue T., Yamamoto Y., Fujiwara M., Nishi K.,
RA   Ohkubo I.;
RT   "Porcine germinal angiotensin I-converting enzyme: isolation,
RT   characterization and molecular cloning.";
RL   Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 146:215-226(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361144};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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DR   EMBL; AB231334; BAE16967.2; -; mRNA.
DR   AlphaFoldDB; Q4ACT8; -.
DR   BindingDB; Q4ACT8; -.
DR   ChEMBL; CHEMBL3432; -.
DR   MEROPS; M02.004; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Genevisible; Q4ACT8; SS.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU361144}; Hydrolase {ECO:0000256|RuleBase:RU361144};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..745
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004235419"
FT   TRANSMEM        699..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          31..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   745 AA;  84801 MW;  98C5784DAB9FC4B2 CRC64;
     MGQGWAAPGL PCLLLLLLLC CGRPLLVPGQ GTTSQVTDIQ RTTSQATTSG QATTSSQATT
     SSQTTTSHST TSSLKTQSPN LVSDEAEASK FVEEYDRRSQ VVLNEYAEAN WDYNTNITAE
     GSKRVLEKST QMANHTVKYG IWARKFDVAN IQNFTLKRMI KKIQDLERAA LPFKELEEYN
     QILLDMETAY SVASVCHANS TCLQLEPDLT NLMDTSRSYE ELLWAWKGWR DKVGRAILPL
     FPKYVELTNK AARLNGYEDG GDAWRAAYEM PFLEQELEQL FQELQPLYLN LHAYVRRALH
     HHYGPEHINL EGPIPAHLLG NMWAQTWSNI YDLVVPFPSA SKMDASEAMI NQGWTPQKMF
     KEADNFFTSL GLLPVPPEFW NKSMLEKPTD GREVVCHASA WDFFNGKDFR IKQCTTVNME
     DLVVAHHEMG HIQYFMQYKD LPVTFREGAN PGFHEAIGDV LALSVSTPKH LRSINLLKSE
     DDGYEEDINF LMKMALDKVA FVPFSYLVDQ WRWRVFDRSI TKENYNQEWW SLRLKYQGLC
     PPVARSQGDF DPGAKFHIPS SVPYIRYFVS FIIQFQFHEA LCQAAGHKGP LHKCDIYQSK
     EAGRRLADAM KLGLSKPWPE AMQLITGQPN VSASAMMTYF KPLLDWLVTE NGRHGEKLGW
     PQYNWTPNSA RLEGSFAGTG RVNFLGLNLE EQQARVGQWV LLFLGVTLLV ATMGLTQRLF
     SIRHQILRRT HRGPQFGSEV ELRHS
//