ID   A0A0J7L0B8_LASNI        Unreviewed;       657 AA.
AC   A0A0J7L0B8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   ORFNames=RF55_3507 {ECO:0000313|EMBL:KMQ96227.1};
OS   Lasius niger (Black garden ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Lasius; Lasius.
OX   NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ96227.1, ECO:0000313|Proteomes:UP000036403};
RN   [1] {ECO:0000313|EMBL:KMQ96227.1, ECO:0000313|Proteomes:UP000036403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:KMQ96227.1};
RA   Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT   "Lasius niger genome sequencing.";
RL   Submitted (APR-2015) 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 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361144};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMQ96227.1}.
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; LBMM01001488; KMQ96227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J7L0B8; -.
DR   STRING; 67767.A0A0J7L0B8; -.
DR   PaxDb; 67767-A0A0J7L0B8; -.
DR   OrthoDB; 2898149at2759; -.
DR   Proteomes; UP000036403; Unassembled WGS sequence.
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; -; 2.
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.
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   Metal-binding {ECO:0000256|RuleBase:RU361144};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..657
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005290609"
SQ   SEQUENCE   657 AA;  75828 MW;  20BF2DFAB3D612CE CRC64;
     MLRLVLVAAV VSLAVAKPES TAEDPVDPVQ SSQTAAELLQ NAQDILKRID AEYGKWSNKQ
     SLAEWNYASN LTDENLAEKL NVSAEAARVR KQIAEEVNAF PWKDLKDENI KRQFKSFGIL
     GIAALPEDSY KEFKLTISQM EDIYSTAKIC DYKNKTKCDL ALEPEITEIL MHSRDPEELK
     YIWVEWRKAS GEQVKCLYPK YVELANTAAS LNNFSDYAAY WMKDYEADDF PEQIETLWQQ
     LKPLYLQLHA YVRRELRKKY GENIVSKDGP IPAHLLGNTW AQTWGNIAEF TVPFPGKQLP
     DVSAALVEQG RFTFDSRSSV AGYNATSIFR LAENFFKSIN LSAMPDTFWE KSILLKQKDV
     NMICHASAWD FYDSKDFRIK QCTRVNMEDL LTAHHEMGHV EYFLQYKDQP TIFKEGANPG
     FHEAVGDVIS LSASTPSHLK KIGLLKDDST DREALLNHLY AKSLDKIAFL PFAYMMDRWR
     WNVFQRKVTP DNYNCNWWSL AEEYQGIEPP VDRSEEDFDP GSKYHIIADV EYIRYYVSFV
     IQFQFHKALC TKAKQYDPKN PNANPLHQCD IYDNKDAGNL LKSMLELGSS KPWPDAMEKI
     AGQREMDSAG LLEYFKPLTD WLTEENKRTN EYIGWKSSNR RCVQTREELR IIDEPTE
//