ID   C3Z9J8_BRAFL            Unreviewed;       667 AA.
AC   C3Z9J8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=LOC118403314 {ECO:0000313|RefSeq:XP_035657902.1};
GN   ORFNames=BRAFLDRAFT_287032 {ECO:0000313|EMBL:EEN50694.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN50694.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN50694.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN50694.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
RN   [2] {ECO:0000313|RefSeq:XP_035657902.1}
RP   IDENTIFICATION.
RC   STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035657902.1};
RC   TISSUE=Testes {ECO:0000313|RefSeq:XP_035657902.1};
RG   RefSeq;
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   EMBL; GG666600; EEN50694.1; -; Genomic_DNA.
DR   RefSeq; XP_002594683.1; XM_002594637.1.
DR   RefSeq; XP_035657902.1; XM_035802009.1.
DR   MEROPS; M02.004; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   InParanoid; C3Z9J8; -.
DR   OMA; QTEASWA; -.
DR   Proteomes; UP000001554; Chromosome 16.
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; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001554};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..667
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041116467"
FT   COILED          30..119
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   667 AA;  76746 MW;  7F45D1788A76B6E4 CRC64;
     MWNVWKIWLC FGAVLLSCSG YTWPLPDQLS AAQQRELKEL QEDVETEISD ICCNNGLKRC
     CVETKKSLAE RKIEEWKELI DSLKELKSTP DEEKAMKWLE EYNEELRQRQ AKSAEANWAQ
     STNITDENAA KVVDVTMELT KWSLKKMEEG KKFDTSGFSD DVKRQFGMIT KSGSSSDEEK
     TRKVAEIGTE LEKIYSTSTA CLPSGTCLKL DPDLEGILAK SRDYDRLTWA WLSWRDAVGP
     PMKDKYAEWV ALMNEGAQEN GYADKGVIWR GAYEMPNDTL EEMVDGVWEK VKPLYTQLHA
     YVRRKLSETY GEDKVLTTGH IPAHLFGNMW AQQWNNIYDI VVPFPDQPAI DVSDTMVEQG
     YDPLRMFKTA EAFFVSIGLR PMPQVFWDKS MIVRPVDREV VCHASAEDFY HDSDVRIKMC
     TKVNQEDLQT IHHEMGHIEY FLTYEDQKTL YRGGANPGFH EAVGDTIALS VNTPGHLKKI
     GLLQNIEGNQ GTEFQINELL KMALSKVAFL PFGLLIDKWR WRVFSGDITP DKFNTEWWNL
     RMKYQGIKPP VERTDEDFDP GAKYHIPSGT PYIRYFFSFV AQFQFQQALC EEAGHDGPLH
     TCDIYQSKKA GAKLKNMLSM GESKPWPEAM KAITGQDKLD PSAILKYFEP LEKWLREQNK
     NEELGWE
//