ID   E7FFA5_DANRE            Unreviewed;      1324 AA.
AC   E7FFA5; A0A8N7T834;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=ace {ECO:0000313|Ensembl:ENSDARP00000099084,
GN   ECO:0000313|RefSeq:XP_694336.5,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-1826};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000099084};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000099084}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000099084};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000099084, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000099084};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3] {ECO:0000313|RefSeq:XP_694336.5}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_694336.5};
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 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; CT998555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU459092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_694336.5; XM_689244.9.
DR   STRING; 7955.ENSDARP00000099084; -.
DR   MEROPS; M02.004; -.
DR   PaxDb; 7955-ENSDARP00000099084; -.
DR   PeptideAtlas; E7FFA5; -.
DR   Ensembl; ENSDART00000114637; ENSDARP00000099084; ENSDARG00000079166.
DR   Ensembl; ENSDART00000114637.4; ENSDARP00000099084.3; ENSDARG00000079166.4.
DR   GeneID; 565980; -.
DR   KEGG; dre:565980; -.
DR   AGR; ZFIN:ZDB-GENE-030131-1826; -.
DR   CTD; 1636; -.
DR   ZFIN; ZDB-GENE-030131-1826; ace.
DR   eggNOG; KOG3690; Eukaryota.
DR   HOGENOM; CLU_006219_0_0_1; -.
DR   OMA; DYSDFQD; -.
DR   OrthoDB; 2898149at2759; -.
DR   PhylomeDB; E7FFA5; -.
DR   TreeFam; TF312861; -.
DR   Reactome; R-DRE-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Proteomes; UP000000437; Chromosome 12.
DR   Bgee; ENSDARG00000079166; Expressed in intestine and 20 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; 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.
PE   1: Evidence at protein 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   Proteomics identification {ECO:0007829|PeptideAtlas:E7FFA5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
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        1287..1308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1324 AA;  152783 MW;  D19F8E94B5171322 CRC64;
     MNRGKRESRT PIGKQEHPAV NVSRRLLRKL LSQHSASQLR SIMLRAVVLL TLISWSAALK
     PEWMPGDYPP TEQGAERFVS DYNSTAEEVL YLSTEASWNY NTNLTDHNSQ LQIEASLEEQ
     AFTEAWGHKA KATFSESLMD TFTNPDLKKI IKKINVLEAA NLAITDRELY NTILSQMDSI
     YSTAKVCPSP EECWSLEPEL QEIMATSRSY KRLLYAWEGW HNSSGVPLKS LYAEFVKISN
     KASQMDGFKD TGEYWRSWYE SPTFKQDLEN LFKQLEPLYQ NLHAFVRRKL YDYYGPKYIN
     LKGPIPAHLL GNMWSQTWNN IYNMMIPFPN RPNVDVTNTM IAKGYNATHM FRVAEEFFTS
     LGLLEMPPEF WDKSMLEKPT DGREVVCHAS AWDFYNRKDF RIKQCTTVTM EQLFTVHHEM
     GHVEYYLQYK DQPVSFRRGA NPGFHEAIGD VLSLSVSTPK HLHSIDLLDQ LTDDAESDIN
     YLLKMALEKI AFLPFGYLID QWRWSVFSGE TPPDRYNADW WYLRTKYQGI CPPTRRTEEH
     FDAGGKYHIP GNTPYIRYFV SFILQFQFHE KLCKEAGHTG PLHKCDIYKS REAGAVLEKV
     LKAGSSEPWT QVLQEALGTD KMDATPLMSY FLPVTTWLRE QNEKTGETLG WPDFNWVPPI
     PEGYPEDIGK ITDEMQAKQF LDEYNSTAEE VWNAYTESSW TYNTDITEAH KDNMLQKNLE
     MANHTKIYGL EARKYDTSDF QDESVKRILS KLSDLERAAL SAEDLVEYNN LLASMETLYS
     VATVCKDKSN CLPLDPDLNK IMAESRDYDE LLFAWQGWRN ASGREIRDSY KRYVELANSA
     AKSNGHTDNG AFWRSLYETP TFEQDLEALW KDLEPLYLSV HAYVRRALYK KYGPERINLK
     GPIPAHLLGN MWAQTWSGIM DLVNPYPDAT QVDATPAMIA QGWTPKRMFE ESDRFFTSLG
     LLPMPPEFWN KSMLEKPTDG REVVCHASAW DFYNRKDFRI KQCTVVTMDD LITVHHEMGH
     VQYFLQYKDQ PISFRDGANP GFHEAIGDVL ALSVATPKHL QSIGLLDKVE DNAESTINFL
     MSIALDKIAF LPFGYLMDQW RWKVFDGRIS SSEYNKEWWN LRMKYQGLCP PVPRTEKDFD
     PGAKFHIPAN VPYIRYFVSF VIQFQFHKGL CDAAGHKGPL HNCDIYQSKE AGKLLSDVMK
     MGFSKPWPEA MKIITGQPKM SVQPLMEYFK PLIEWLEKEN EKNGDVLGWP EYDWTPYKLS
     TVVEESPKSV NFLGLSVDAA GAAAGQWILL VLSIVFLLAV VFLAYRYSKT KRLQNKSMSQ
     MELK
//