ID B3MN07_DROAN Unreviewed; 615 AA.
AC B3MN07;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN Name=Dana\GF14268 {ECO:0000313|EMBL:EDV31985.1};
GN Synonyms=dana_GLEANR_15030 {ECO:0000313|EMBL:EDV31985.1};
GN ORFNames=GF14268 {ECO:0000313|EMBL:EDV31985.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV31985.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV31985.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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}.
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DR EMBL; CH902620; EDV31985.1; -; Genomic_DNA.
DR RefSeq; XP_001962764.1; XM_001962728.2.
DR AlphaFoldDB; B3MN07; -.
DR SMR; B3MN07; -.
DR STRING; 7217.B3MN07; -.
DR MEROPS; M02.003; -.
DR EnsemblMetazoa; FBtr0118968; FBpp0117460; FBgn0091295.
DR GeneID; 6497096; -.
DR KEGG; dan:6497096; -.
DR eggNOG; KOG3690; Eukaryota.
DR HOGENOM; CLU_014364_3_3_1; -.
DR InParanoid; B3MN07; -.
DR OMA; KPSKMFE; -.
DR OrthoDB; 2898149at2759; -.
DR PhylomeDB; B3MN07; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:EnsemblMetazoa.
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:EnsemblMetazoa.
DR GO; GO:0007552; P:metamorphosis; IEA:EnsemblMetazoa.
DR GO; GO:0016486; P:peptide hormone processing; IEA:EnsemblMetazoa.
DR GO; GO:0009609; P:response to symbiotic bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0019953; P:sexual reproduction; IEA:EnsemblMetazoa.
DR CDD; cd06461; M2_ACE; 1.
DR Gene3D; 1.10.1370.30; -; 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:EDV31985.1}; Coiled coil {ECO:0000256|SAM:Coils};
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:EDV31985.1};
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:UP000007801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..615
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002793122"
FT COILED 18..75
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 615 AA; 70833 MW; 15F8882A8B3BF40A CRC64;
MKLLLVAFLA MLAVSHALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY ASNINDENEK
KKNEISAELA KFMKEVASDV KKFQWRSYQS DDLKRQFKSL TKLGYAALPE ADYAEFLETV
SAMESNYAKV KVCDYKDATK CDLALEPEIE EVISKSRDAE ELKYYWREFY DKAGTAVRSQ
FERYIELNTK AAHLNNFTSG AESWLDEYED DTFEKQLEDI FAEIRPLYEQ IHGYVRSRLR
KFYGDQVVSE TGPIPMHLLG NMWAQQWSEI ADIVSPFPDK PLVDVSDEME KQGYTPLKMF
QMGDDFFTSM NLTKLPQDFW DKSIIEKPSD GRDLICHASA WDFYLTDDVR IKQCTRVTQD
QLFTVHHELG HIQYFLQYQH LPFVYRTGAN PGFHEAVGDV LSLSVSTPKH LEKIGLLKNY
VSDEEARINQ LFLTALDKIV FLPFAFTMDK YRWSLFRGEV DKANWNCAFW KLREEYSGIE
PPVVRSEKDF DAPAKYHVSA DVEYLRYLVS FIIQFQFYKS ACIKAGQYDA TNPELPLDNC
DIYGSAAAGA AFHNMLSLGA SKPWPDALEA FNGERVMSGK AIAEYFEPLR VWLEADNIKN
NVHIGWTASD KCVAS
//
