ID   A0NFU8_ANOGA            Unreviewed;       698 AA.
AC   A0NFU8;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE   Flags: Fragment;
GN   Name=ANCE2 {ECO:0000313|EMBL:EAU76037.2};
GN   ORFNames=AgaP_AGAP009751 {ECO:0000313|EMBL:EAU76037.2};
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:EAU76037.2};
RN   [1] {ECO:0000313|EMBL:EAU76037.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAU76037.2};
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:EAU76037.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAU76037.2};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAU76037.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAU76037.2};
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:EAU76037.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAU76037.2};
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:EAU76037.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAU76037.2};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 87-698, AND DISULFIDE BONDS.
RX   PubMed=31682720; DOI=10.1042/BCJ20190635;
RA   Cashman J.S., Cozier G.E., Harrison C., Isaac R.E., Acharya K.R.;
RT   "Crystal structures of angiotensin-converting enzyme from Anopheles gambiae
RT   in its native form and with a bound inhibitor.";
RL   Biochem. J. 476:3505-3520(2019).
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:EAU76037.2}.
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DR   EMBL; AAAB01008980; EAU76037.2; -; Genomic_DNA.
DR   RefSeq; XP_001238053.2; XM_001238052.2.
DR   PDB; 6S1Y; X-ray; 2.20 A; A=87-698.
DR   PDB; 6S1Z; X-ray; 2.50 A; A=87-698.
DR   PDBsum; 6S1Y; -.
DR   PDBsum; 6S1Z; -.
DR   AlphaFoldDB; A0NFU8; -.
DR   SMR; A0NFU8; -.
DR   STRING; 7165.A0NFU8; -.
DR   MEROPS; M02.003; -.
DR   PaxDb; 7165-AGAP009751-PA; -.
DR   GeneID; 4578020; -.
DR   KEGG; aga:AgaP_AGAP009751; -.
DR   CTD; 4578020; -.
DR   VEuPathDB; VectorBase:AGAP009751; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   HOGENOM; CLU_014364_3_0_1; -.
DR   InParanoid; A0NFU8; -.
DR   OMA; WPEYNDS; -.
DR   OrthoDB; 2898149at2759; -.
DR   PhylomeDB; A0NFU8; -.
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:0070573; F:metallodipeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z};
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, ECO:0007829|PDB:6S1Y};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW   Protease {ECO:0000256|RuleBase:RU361144};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361144, ECO:0007829|PDB:6S1Y}.
FT   BINDING         443
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z"
FT   BINDING         471
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z"
FT   DISULFID        209..217
FT                   /evidence="ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z"
FT   DISULFID        412..430
FT                   /evidence="ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z"
FT   DISULFID        543..688
FT                   /evidence="ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z"
FT   DISULFID        598..616
FT                   /evidence="ECO:0007829|PDB:6S1Y, ECO:0007829|PDB:6S1Z"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EAU76037.2"
SQ   SEQUENCE   698 AA;  80352 MW;  3C065DAB2F956C5B CRC64;
     NRFGITCKGL FIPSVQQYVS DGDSANSSSR PVFPVQVLIN GLAETIQWDW NVRRDSEKHI
     MASNIQWRSV WLMLLFASTI AAGPVKRRST ESEKAPSETE ISQIVEWIEQ RYQQTKAHQT
     LAAWEYGSNL TEFNLSKKTK AAADFAEVAK AVAEELQQFK TDQLTNATLK RRIKKLAKLG
     YAALPADQFK ELLGAIASME SNYAKAKFCA YGDATKCDLS LDPELTEIFA NHREPEELKY
     YWVQWYNATG APVRESFQKY VELNRQAALR NNFSSGAAVW LNEYDDSTFE QQVDDVIEQI
     RPLYEQLHAY VRYKLRQKYG DKLVSPTGPI PMHLLGNLWA QTWDNIADFT TPFPEKKLLD
     VTDEMIRQGY TPIKMFQMGD DFFTSLNMTK LPQTFWDKSI LEKPTDGRDL VCHASAWDFF
     AIDDVRIKQC TRVNMREFFV VHHELGHIQY YLQYQHQPVE FRGGANPGFH EAVGDVLSLS
     VSTPKHLKKV GLLKDYEEDE QVKINQFYRA GVTKLVFLPF AYTLDKYRWG VFRGDIKPRE
     YNCKFWEMRS RYSGVEPPVV RTEQDFDPPA KYHVSADVEY LRYFVSYVIQ FQFHRAACAL
     AGEYVKGDPE KTLNNCDIYQ STAAGNQLKE MLALGSSKPW PDAMEVLTGE RKMSADAILE
     YFDPLYQWLL EENKRLGAHV GWTDSQKCVS HPIDFMAA
//