ID   I3LC15_PIG              Unreviewed;       752 AA.
AC   I3LC15;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=LOC100515049 {ECO:0000313|Ensembl:ENSSSCP00000021588.2};
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|Ensembl:ENSSSCP00000021588.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000021588.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000021588.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000021588.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; I3LC15; -.
DR   MEROPS; M02.004; -.
DR   PaxDb; 9823-ENSSSCP00000021588; -.
DR   Ensembl; ENSSSCT00000027986.5; ENSSSCP00000021588.2; ENSSSCG00000023612.5.
DR   eggNOG; KOG3690; Eukaryota.
DR   GeneTree; ENSGT00940000163921; -.
DR   HOGENOM; CLU_014364_3_0_1; -.
DR   OMA; QTEASWA; -.
DR   TreeFam; TF312861; -.
DR   Proteomes; UP000008227; Chromosome 12.
DR   Bgee; ENSSSCG00000023612; Expressed in testis and 2 other cell types or tissues.
DR   ExpressionAtlas; I3LC15; baseline.
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:SF41; ANGIOTENSIN-CONVERTING ENZYME-LIKE PROTEIN ACE3; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000008227};
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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..752
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003675159"
FT   TRANSMEM        640..658
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        713..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   752 AA;  87515 MW;  3C3826C488E94301 CRC64;
     MDLPWTFPTC ALLLWAALAM AQGQDELYSE TVAKAFLQFY ERTAQVVWNQ FMEATWNYVT
     NITNKNREEM LRKDVERSQH TLYFGTRARL FKIDDFQDPD VKRMLSKLQN LYKAALPEDE
     LREYNQILAY METTYSMAQV CLNEGPCLPL EPDLEEVMAT SRDQKELLWA WQGWRDAVGR
     QLRMTFERYV QLSNKAAELN GYEDMGAMWR SAYESDTLEQ DVEQLYEELQ PLYLNLHAYV
     RRGLYRFYGP QLIDPRGPIP AHILGNMWAQ SWVSILDLVL PFPEKPPEDI TKIMKGQHWK
     PEKMFQEAEK FFTSLGLLST PPEFWKNSMM ERPTDGREVE CHASAWDFYN GEDFRIKKCT
     EVTIEDLLSI FHQMGHIQYF LQYKNLSVIF RAGANPAFEE AVGSVITLSA SSHKHLLNRG
     LLSHQHQDEE EEVNFLMSMA LEKIAFIPFA YLVDRFRWKV FDGTIRKAVY NQEWWNLRLK
     YQGLCPPVPR TEDDFDPGAK FHISASMPYI RYFLSLMLQF QIHEALCKAS GHVGPLHRCD
     IYNSKKAGKL LADVLKLGSS KPWPEVLQKI TGETKVSTKA LMTYFKPLLN WLVTENVRHG
     EILGWPDFSC SLEQSFDKET DRAAFLGLEL NPDQAKSGQW VLLALSFVML LMVLLLAYKV
     YTLEKKSLAQ DTSAQDTSVQ DTSTRDNSVH VPPPKAYFLG TAMEPHQVVR RQWMLLGLCL
     ILMLCSVGLI IRIFTQHSWK PPWMRDEWWS WD
//