ID   A1YQ85_PIG              Unreviewed;      1309 AA.
AC   A1YQ85;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
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:ABL73884.1};
RN   [1] {ECO:0000313|EMBL:ABL73884.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Kidney {ECO:0000313|EMBL:ABL73884.1};
RA   Yoon J., Yoon J., Hong K.;
RT   "Cloning of porcine kidney cDNA encoding an angiotensin I converting
RT   enzyme.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 2 Zn(2+) ions 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; EF121312; ABL73884.1; -; mRNA.
DR   BindingDB; A1YQ85; -.
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; 2.
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; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR   Genevisible; A1YQ85; 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..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..1309
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002641203"
FT   TRANSMEM        1263..1284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1309 AA;  150543 MW;  09D9ACD74A715D59 CRC64;
     MGAAPGRRWP WPPLLPLLLM LLLPPPPLPV ALALDSALQP GNFTADEAGA EDFAQSFNSS
     SEQVLFQSTA ASWAHDTNIT EENARRQEEA ALISQEFSEV WGQKAKALYD PIWQNFTSRT
     PRRIIGVVRT LGSANLPGKR QQYNSLLSNM TRIYSTARVC FPNKTATCWS LDPELTNILA
     TSRSYTLLLY AWEGWHNAAG IPLKPLYQDF TALSNEAYKQ DGFSDTGAYW RSLYDSPTFT
     EDLERLYHQL EPLYLNLHAY VRRALHRQYG DRFINLRGPI PAHLLGNMWA QSWNNIYDMV
     VPFPGKPSLD VTSAMVQKGW NVTHMFRVAE EFFTSLGLLP MPPEFWAESM LEKPSDRREV
     VCHASAWDFY NRKDFRIKQC TQVTIDQLST VHHEMGHVQY YLQYKDRHVS LRRGANPGFH
     EAIGDVLALS VSTPAHLHKI GLLDHVTSDW ESDINYLLKM ALEKIAFLPF GYLVDQWRWG
     VFSGRTPPSL YNYDWWYLRT KYQGVCPPVV RNETHFDAGA KYHVPNVTPY IRYFVSFILQ
     FQFHQALCKE AGHQGPLHQC DIYQSTRAGA KLRAVLQAGF SRPWQEVLKD MVGSGALDAQ
     PLLDYFQPVT QWLEEQNQRS GDILGWPEYQ WRPPMPDNYP EGIDLVSDEA EASKFVEEYD
     RRSQVVLNEY AEANWDYNTN ITAEGSKRVL EKSTQMANHT VKYGIWARKF DVANIQNFTL
     KRMIKKIQDL ERAALPFKEL EEYNQILLDM ETAYSVASVC HANSTCLQLE PDLTNLMATS
     RSYEELLWAW KGWRDKVGRA ILPYFPKYVE LTNKAARLNG YEDGGDAWRA AYEMPFLEQE
     LEQLFQELQP LYLNLHAYVR RALHHHYGPE HINLEGPIPA HLLGNMWAQT WSNIYDLVVP
     FPSASKMDAS EAMINQGWTP QRMFKEADNF FTSLGLLPVP PEFWNKSMLE KPTDGREVVC
     HASAWDFFNG KDFRIKQCTT VNMEDLVVAH HEMGHIQYFM QYKDLPVTFR EGANPGFHEA
     IGDVLVLSVS TPKHLRSINL LKSEDDGYEE DINFLMKMAL DKVAFVPFSY LVDQWRWRVF
     DRSITKENYN QEWWSLRLKY QGLCPPVARS QGDFDPGAKF HIPSSVPYIR YFVSFIIQFQ
     FHEALCQAAG HKGPLHKCDI YQSKEAGRRL ADAMKLGLSK PWPEAMQLIT GQPNVSASAM
     MTYFKPLLDW LVTENGRHGE KLGWPQYSWT PNSARLEGSF AGTGRVNFLG LNLEEQQARV
     GQWVLLFLGV TLLVATMGLT QRLFSIRHQI LRRTHRGPQF GSEVELRHS
//