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
//
