ID   W5N3G5_LEPOC            Unreviewed;      1300 AA.
AC   W5N3G5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015174.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000015174.1}
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 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; AHAT01023064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000015174; -.
DR   Ensembl; ENSLOCT00000015203.1; ENSLOCP00000015174.1; ENSLOCG00000012317.1.
DR   eggNOG; KOG3690; Eukaryota.
DR   GeneTree; ENSGT00940000163600; -.
DR   InParanoid; W5N3G5; -.
DR   OMA; DYSDFQD; -.
DR   Proteomes; UP000018468; Linkage group LG15.
DR   Bgee; ENSLOCG00000012317; Expressed in intestine and 13 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06461; M2_ACE; 2.
DR   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR001623; DnaJ_domain.
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   PROSITE; PS50076; DNAJ_2; 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:UP000018468};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   TRANSMEM        1262..1280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          781..867
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
SQ   SEQUENCE   1300 AA;  149977 MW;  3CD2ECB365F9EA48 CRC64;
     LSFPVFAAAA GQTLAGMLWV MWVVPLFGLA HSVFLFELPG DYLANETGAL DFVNDYNTSA
     EQVFFRSTSA SWTYNTDLNE HNQIAQVNAS MEEQAFVEAW GKKAKDLFPT WVTDTFNDIQ
     LRTLIKKISV LGAANLNTTE RKNYNTILSD MDSIYSTANV CPPGENIKCW SLEPDIVDLM
     ATSRNYKKLL YAWEGWHNAS GIPLRKKYPE FVELSNKASQ MDGFVDTGDY WRSWYESPTF
     QEDLETIYQQ LQPLYLHLHA FVRRKLYQRY GPKYINLKGP IPAHLLGNMW AQQWNNIYDM
     MVPFPHKPNL DVTQTMVNLK WNATHMFRVS EEFFTSLGLI AMPQEFWDHS MLEKPTDGRQ
     VVCHASAWDF YNRKDFRIKQ CTTVTMEQLF TVHHEMGHVE YYLQYKDQPV GFRSGANPGF
     HEAVGDVLSL SVSTPKHLKE IGLLKSFVPD NESDINYLLK MALEKIAFLP FGYLIDQWRW
     GVFSGRTPPE RYNADWWYLR TKYQGICPPI ERSEEHFDAG AKFHIPGNTP YIRYFVSFIL
     QFQFHEKLCE AAKHVGPLHQ CDIYRSKEAG AILQKVLSAG SSKPWQDILQ EALGTNRMDA
     GPLMAYFSPI INWLKEQNAN ETLGWPDFEW RPPVPEGYPE DIDKIADEEK AIEFLDQYNS
     TAEVVWNAYT EASWVYNTNI TEENKQTMLQ KNLEMSNHTL TYGLEARKFD YTDFQDESVK
     RILKKLSEIE RAGLPQNELK DYNELLSRME TTYSVATVCQ EGRRCLPLDP DLTEIMAKSR
     DYKELLFAWQ GWRDASGKKI RQDYKTYVEL SNKAARLNGH PDNGAYWRSL YETPTFEQDL
     ERLYQEMQPL YLNLHAYVRK ALYKKYGSEY VNLKGPIPAH LLGNMWAQSW SNIYDLVTPF
     PDAGQVDATP AMVAKGWDAR KMFEQSDHFF QSLGLIPMPP EFWSKSMLEK PSDGRSVVCH
     ASAWDFYNRK DFRIKQCTVV TMDDLITVHH EMGHVQYFLQ YKDQPVPFRD GANPGFHEAI
     GDVLALSVST PKHLHSIGLL DKVENNYDSD INYLMSIALD KIAFLPFGYL MDQWRWKVFD
     GRISEQEYNK EWWNLRLKYQ GLCPPVPRSE EDFDPGAKFH IPANVPYVRY FVSFVIQFQF
     HEALCKAAKH TGPLHMCDIY NSREAGKLLG DVMQLGFSKP WPEAMTLITG QPNMSAQALL
     KYFEPLITWL EKENKKNGDI LGWPEYDWVP GPEKGPEKVT GSAEVSFLGM NLTSDQAAAG
     QWILLVLGLG LLIATICLAY KSKSKKRQKS NSELELSQKD
//