ID A0NFV2_ANOGA Unreviewed; 620 AA. AC A0NFV2; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144}; DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144}; GN Name=ANCE5 {ECO:0000313|EMBL:EAU76041.1}; GN ORFNames=AgaP_AGAP009755 {ECO:0000313|EMBL:EAU76041.1}; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Anophelinae; Anopheles. OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAU76041.1}; RN [1] {ECO:0000313|EMBL:EAU76041.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|EMBL:EAU76041.1}; RX PubMed=12364791; DOI=10.1126/science.1076181; RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W., RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., RA Collins F.H., Hoffman S.L.; RT "The genome sequence of the malaria mosquito Anopheles gambiae."; RL Science 298:129-149(2002). RN [2] {ECO:0000313|EMBL:EAU76041.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAU76041.1}; RG The Anopheles Genome Sequencing Consortium; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EAU76041.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAU76041.1}; RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003; RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.; RT "The Anopheles gambiae genome: an update."; RL Trends Parasitol. 20:49-52(2004). RN [4] {ECO:0000313|EMBL:EAU76041.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAU76041.1}; RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5; RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F., RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.; RT "Update of the Anopheles gambiae PEST genome assembly."; RL Genome Biol. 8:R5.1-R5.13(2007). RN [5] {ECO:0000313|EMBL:EAU76041.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAU76041.1}; RG VectorBase; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAU76041.1}. 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; AAAB01008980; EAU76041.1; -; Genomic_DNA. DR RefSeq; XP_001238057.1; XM_001238056.1. DR AlphaFoldDB; A0NFV2; -. DR STRING; 7165.A0NFV2; -. DR MEROPS; M02.003; -. DR PaxDb; 7165-AGAP009755-PA; -. DR GeneID; 4578342; -. DR KEGG; aga:AgaP_AGAP009755; -. DR CTD; 4578342; -. DR VEuPathDB; VectorBase:AGAP009755; -. DR eggNOG; KOG3690; Eukaryota. DR HOGENOM; CLU_014364_3_3_1; -. DR InParanoid; A0NFV2; -. DR OMA; KPSKMFE; -. DR OrthoDB; 2898149at2759; -. DR PhylomeDB; A0NFV2; -. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. 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; -; 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 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|RuleBase:RU361144}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..620 FT /note="Angiotensin-converting enzyme" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014565135" SQ SEQUENCE 620 AA; 71777 MW; 5BD0EC4CE0FBA8B7 CRC64; MRIFSTVIIA FALVCCVLGG KLVSVSDDEL EARHYVEQVD EEILSRRNVG TEAEWAYESD INEDNLMVKN EVAAANAMFL KEVANTLNKY EYESFSDEDL KRKIRKLTKL GYSVLPEDTF AEMLDAINRM QENYAKVKVC DYRDNSKCDL ALEPELTEIM ATSRDPEELK YYWQQWYDAA GAPTRDDFQK YVDLNGVAAR MNNYSSGAEY WLSAYEDDTF EEQVDAVIEE LRPLYEQIHA NVRYQLRKYY GEDVVSEKGP IPMHLLGNMW AQDWAGVADI ISPFPDRQLL DVTEEMVRQG YNPIQMFEMG DEFFQSMNMT KLPATFWEKS ILEKPDDGRD LVCHASAWEF SKTDDVRIKQ CTRVTMEQFF TVHHELGHVQ YFLQYQHLPS MYRDGANPGF HEAVGDVLSL SVSTPKHLEK IGLLKDYVED EESKLNQFYG SALNKLVFLP FAYTLDKYRW GIFRGDIKPE EYNCKFWEMR SKFSGVEPPV VRSESDLDAP AKYHVSADVE YLRYFVSFII QFQFHRAACE KAGEYVKGDP EKTLNNCDIY QSVEAGNAIK AMLELGSSKP WPDAMEVLTG ERRMSADALI EYFQPLYDWL VVENERIGAH VGWEETESKF //