ID B4GX29_DROPE Unreviewed; 604 AA. AC B4GX29; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144}; DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144}; DE Flags: Fragment; GN Name=Dper\GL21247 {ECO:0000313|EMBL:EDW27356.1}; GN ORFNames=Dper_GL21247 {ECO:0000313|EMBL:EDW27356.1}; OS Drosophila persimilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744}; RN [1] {ECO:0000313|EMBL:EDW27356.1, ECO:0000313|Proteomes:UP000008744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSH-3 / Tucson 14011-0111.49 RC {ECO:0000313|Proteomes:UP000008744}; 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; CH479195; EDW27356.1; -; Genomic_DNA. DR RefSeq; XP_002023228.1; XM_002023192.1. DR AlphaFoldDB; B4GX29; -. DR MEROPS; M02.003; -. DR EnsemblMetazoa; FBtr0186862; FBpp0185354; FBgn0158840. DR GeneID; 6598003; -. DR KEGG; dpe:6598003; -. DR eggNOG; KOG3690; Eukaryota. DR HOGENOM; CLU_014364_3_3_1; -. DR OMA; DQYASNF; -. DR OrthoDB; 2898149at2759; -. DR PhylomeDB; B4GX29; -. DR Proteomes; UP000008744; 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:SF45; 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:UP000008744}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Zinc {ECO:0000256|RuleBase:RU361144}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:EDW27356.1" SQ SEQUENCE 604 AA; 69379 MW; 68B241457E7A75A7 CRC64; IFVGFVLPSS STDSTLTTFL VEANQQLAGI YDQVVLAQLQ NELRGSNDVV ALLEMEIADE KLLNYLKSLM PHLAKFKRLK LGDASQKRQL ERIPRLGYNA LDGMELAQVY ALASNMSDSY RNVLLCAYKQ PGNCTLRLIP EVQAIVQESR DLDEIEYYWY EWRKQTGLAT RDQFVAFMEL YKKTAQLNGY PRAQDYWFRS LEMGGAQTMS LLDRLMAGLR PLFLQFHAHV RGSLRKMHGE RLVPRGRPYP QHLAEVFIGN AFRRVRAEWY VDLPSPLAGL ANITQDLHRR GLSTTQRVFW NVAEYFRGLG LPLLESSLWT NAQVVAADDD DRCWHKVWRY YTLPITNFTY CPLNDEERFL NMFEAQSDLY YNRAASGQPT LLRDEPFPSF GDAIGKCFSL AATSPRYLQK LGLLQEGKWL ELPARLNRLY VHGLRVVFLL PVFYVLDRYR VEVLSGHIRA DDNEAYWRLT EHYTGAAAPR KRSNEQFDVP AKLLMEVDDQ YASNILSTVL QFQLLKHYCT TTLQFGKDNP RKALDLCDIS DQRQIGASLQ RAMALGSSVP YSDVLQELVG EPEINIDGLL AYFKPLHDWL VQQNQLQNLD VGWA //