ID   B0WR90_CULQU            Unreviewed;       621 AA.
AC   B0WR90;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 93.
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};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176 {ECO:0000313|EnsemblMetazoa:CPIJ009107-PA, ECO:0000313|Proteomes:UP000002320};
RN   [1] {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|PROSITE-ProRule:PRU01355,
CC       ECO:0000256|RuleBase:RU361144}.
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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   OMA; WPEYNDS; -.
DR   OrthoDB; 10029630at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF44; ANGIOTENSIN-CONVERTING ENZYME-RELATED; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS52011; PEPTIDASE_M2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601548-4};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR601548-
KW   10}; Hydrolase {ECO:0000256|RuleBase:RU361144};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601548-3,
KW   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|PIRSR:PIRSR601548-3, 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"
FT   ACT_SITE        372
FT                   /note="Proton acceptor 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-1"
FT   ACT_SITE        372
FT                   /note="Proton acceptor 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-11"
FT   ACT_SITE        501
FT                   /note="Proton donor 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-1"
FT   ACT_SITE        501
FT                   /note="Proton donor 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-11"
FT   BINDING         212
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-2"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-3"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-8"
FT   BINDING         375
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-3"
FT   BINDING         375
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-8"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-3"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-8"
FT   BINDING         510
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-2"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-10"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-10"
FT   DISULFID        137..145
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01355"
FT   DISULFID        340..358
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-4,
FT                   ECO:0000256|PROSITE-ProRule:PRU01355"
FT   DISULFID        526..544
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-4,
FT                   ECO:0000256|PROSITE-ProRule:PRU01355"
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
//