ID B4N7R8_DROWI Unreviewed; 632 AA. AC B4N7R8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144}; DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144}; GN Name=Dwil\GK18674 {ECO:0000313|EMBL:EDW80407.1}; GN ORFNames=Dwil_GK18674 {ECO:0000313|EMBL:EDW80407.1}; OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW80407.1, ECO:0000313|Proteomes:UP000007798}; RN [1] {ECO:0000313|EMBL:EDW80407.1, ECO:0000313|Proteomes:UP000007798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M., RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). 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 --------------------------------------------------------------------------- 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; CH964214; EDW80407.1; -; Genomic_DNA. DR RefSeq; XP_002069421.1; XM_002069385.2. DR AlphaFoldDB; B4N7R8; -. DR SMR; B4N7R8; -. DR MEROPS; M02.002; -. DR EnsemblMetazoa; FBtr0249325; FBpp0247817; FBgn0220672. DR GeneID; 6646754; -. DR KEGG; dwi:6646754; -. DR eggNOG; KOG3690; Eukaryota. DR HOGENOM; CLU_014364_3_3_1; -. DR InParanoid; B4N7R8; -. DR OMA; FYRQIHG; -. DR OrthoDB; 2898149at2759; -. DR PhylomeDB; B4N7R8; -. DR Proteomes; UP000007798; 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 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 ECO:0000313|EMBL:EDW80407.1}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, KW ECO:0000256|RuleBase:RU361144}; KW Hydrolase {ECO:0000256|RuleBase:RU361144, ECO:0000313|EMBL:EDW80407.1}; 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:UP000007798}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|RuleBase:RU361144}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..632 FT /note="Angiotensin-converting enzyme" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002819444" SQ SEQUENCE 632 AA; 73175 MW; F1F6DDC3062BC00A CRC64; MNAFLMLGLV LAVFWAGLPH SALGNSNTCS AAVLDARRFF QHENEQLRQR YNEEFLAAYT YNTNVTEANR EAMITIFAKN AKETKRLAEQ IKSSDYDQSS DADIRRQSRL LSEMGSAALN PEDYLTLKNA ISSMQSNYAT TNVCSYKNRS DCSLTLEPHI QERLSKSRDP DELAWYWREW YDKAGTPQRE NFATYVNLTR KASQLNGYRS YADYWVHFYE DPDFERQLDA TFKAILPFYR QVHGYVRYRL RQHYGEDVVP AEGNIPMHLL GNMWGQAWNE VIDLFTPYPE KPFVDVKSEM QKQEYTVNKL FELGDQFFQS LGMRALPPSF WNLSVLTRPQ DREIVCHASA WDFYQDSDVR IKMCTELDTH YLYVVHHELG HIQYYLQYEQ QPAVYRGAPN PGFHEAVGDV IALSVMSAKH LKSIGLTGSG RLDEKSRINE LFKQALTKIA FLPFGYTMDK YRYAVFRNEL DESQWNCAFW QMRSEFGGIE PPINRSDKNF DPPAKYHIDA DVEYLRYFAA HIFQFQFHKA LCQLAGQYSS TDNRLTLDNC DIFGSKDAGK ALSKFLSLGN SIHWKDALQE FTGETEMNPS ALLEYFEPLY QWLKQENSRL GVPLGWGETN KIPSDCCGPF ST //