ID B0WR90_CULQU Unreviewed; 621 AA. AC B0WR90; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144}; DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144}; GN Name=6042070 {ECO:0000313|EnsemblMetazoa:CPIJ009107-PA}; GN ORFNames=CpipJ_CPIJ009107 {ECO:0000313|EMBL:EDS33274.1}; OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Culicinae; Culicini; Culex; Culex. OX NCBI_TaxID=7176; RN [1] {ECO:0000313|EMBL:EDS33274.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JHB {ECO:0000313|EMBL:EDS33274.1}; RG The Broad Institute Genome Sequencing Platform; RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C., RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E., RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P., RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F., RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D., RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J., RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E., RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.; RT "Annotation of Culex pipiens quinquefasciatus."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ009107-PA} RP IDENTIFICATION. RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ009107-PA}; RG EnsemblMetazoa; RL Submitted (FEB-2021) to UniProtKB. 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; DS232053; EDS33274.1; -; Genomic_DNA. DR RefSeq; XP_001851224.1; XM_001851172.1. DR AlphaFoldDB; B0WR90; -. DR MEROPS; M02.003; -. DR EnsemblMetazoa; CPIJ009107-RA; CPIJ009107-PA; CPIJ009107. DR KEGG; cqu:CpipJ_CPIJ009107; -. DR VEuPathDB; VectorBase:CPIJ009107; -. DR VEuPathDB; VectorBase:CQUJHB000776; -. DR eggNOG; KOG3690; Eukaryota. DR HOGENOM; CLU_014364_3_3_1; -. DR InParanoid; B0WR90; -. DR OMA; QEWWNFR; -. DR OrthoDB; 2898149at2759; -. DR Proteomes; UP000002320; 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 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:UP000002320}; 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..621 FT /note="Angiotensin-converting enzyme" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5011408410" SQ SEQUENCE 621 AA; 71713 MW; FFDAD2C6E414D065 CRC64; MVTKVLVLAL LASVALAVNP DLEDQELAGQ KYVSDLEADI LARNNEATEA SWAYESDISE AHLKARDEIQ VRNANYFKEV ARELRKYDWQ NFKNGDLKRM FKKMTDLGYA ALPEAKFTEL LDAISSMSEN YATAKVCDYK NREKCDLALE PELTEIFATS RDPEELKYYW TQWYDKAGTP TREAFDKYIK LSNEAAKLNN LSSGAEAWLD AYEDETFEQQ ADAAIEQIRP LYEQIHAYVR HKLRERYGED VVSEKGPIPM HLLGNMWAQS WDNVADFTTP YPNSQLMDVT EEMVKQGYSA KQMFEMGDDF FVSLNMTRLP QSFWEKSILE KPTDGRELVC HASAWDFYKT DDVRIKQCTR INMEDFFTAH HELGHIQYFL QYQHQPSTYR EGANPGFHEA VGDVISLSVS TPKHLEKIGL LKDFVMDEEA KMNQFYRQGL SKLVFLPFAY TLDKYRYGMF RGEIKPDQAN CKFWEMRTKF SGIEPPVVRS EKDFDGPAKY HMSADVEYLR YLVSFIIQFQ FHRSACELAG EYVKGDPVKT LNNCDIYQNA NAGNAIKEML ALGSSKPWPD AMEVLTGQRT MSADALLEYF QPLQDWLVVE NKRLGAYVGW EKSDKTLLLD R //