ID   A0A182JRU2_9DIPT        Unreviewed;       577 AA.
AC   A0A182JRU2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
OS   Anopheles christyi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR001224-PA, ECO:0000313|Proteomes:UP000075881};
RN   [1] {ECO:0000313|Proteomes:UP000075881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACHR001224-PA}
RP   IDENTIFICATION.
RC   STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR001224-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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}.
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DR   AlphaFoldDB; A0A182JRU2; -.
DR   STRING; 43041.A0A182JRU2; -.
DR   EnsemblMetazoa; ACHR001224-RA; ACHR001224-PA; ACHR001224.
DR   VEuPathDB; VectorBase:ACHR001224; -.
DR   OrthoDB; 2898149at2759; -.
DR   Proteomes; UP000075881; 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:SF45; 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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..577
FT                   /note="Angiotensin-converting enzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008124533"
SQ   SEQUENCE   577 AA;  66125 MW;  705CF8DBDD7858EC CRC64;
     MMRVWFCGAL LVVLVSGQIS DLRYTETSND KLSEAIQFLR EYDREAAEMC NRVANAEWRF
     STNGTEYNKR RMREQQNLAS KLECISWRRA VSFDSSRIID TSIRRQLGRI VQQGRCGLGD
     AKYAELQHVL MLLKDNYNGA KVCPFRRGGS EATDLGTFSS TGGIAYPSSS YVSAYTGYCD
     LKINPDLTRI METSRSESEL RYYWVAWREK TGPPVRNTFM RYLNLANQAA EQHGFHDAGE
     QMRSVYEDGD FFFTVNDLWG QLQPLYKQLF TFVRKGLIRQ YGEHVVRRDG PLPAHLLGNM
     WAQNWRHIMD IIKPGPLETP DVSGEMVRQG YTPMKIFQTA EEFFTSIGLS PMAPEFWRNS
     VLQKPNDGAS QCSASAWDFC NKVDFRIKQC TQVSLDDFVG AHHEMTHIQY YMQYAGQPFL
     YREGPNPAFH EALANAITLS VGGPAHLQKI GLLTSPVTVA NGNSMINIEY LLNLALDKLP
     FMAFSLALEK WRWYVFEKGP IGMNARWWEL RLRYQGVIPP TGRGFEHFDA GAKYHVVSDQ
     DYIKYFVATV LQFQIYSELC QAAQHYGPLH TYLGHVH
//