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Database: UniProt
Entry: A0A182XN91_ANOQN
LinkDB: A0A182XN91_ANOQN
Original site: A0A182XN91_ANOQN 
ID   A0A182XN91_ANOQN        Unreviewed;       888 AA.
AC   A0A182XN91;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
OS   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA011341-PA, ECO:0000313|Proteomes:UP000076407};
RN   [1] {ECO:0000313|Proteomes:UP000076407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., 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 quadriannulatus QUAD4_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AQUA011341-PA}
RP   IDENTIFICATION.
RC   STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA011341-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 2 Zn(2+) ions 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   STRING; 34691.A0A182XN91; -.
DR   EnsemblMetazoa; AQUA011341-RA; AQUA011341-PA; AQUA011341.
DR   VEuPathDB; VectorBase:AQUA011341; -.
DR   Proteomes; UP000076407; 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; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
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};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   REGION          149..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   888 AA;  103329 MW;  B87750574F15C558 CRC64;
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXGEYVKG DPEKTLNNCD IYQSVEAGNA
     IKAMLELGSS KPWPDVMEVL TGERRMSADA LIEYFQPLYD WLVVENERIG AHVGWENTTT
     RRYTMLKLLI KCTIGALFAL QSIHCEADPQ LNLPPLAPPG LEGRRPVTFP NGEASPTRVP
     LGVDGVVSGD GSSVHDRSRS ERFGPPYDGD DDEEDERPNY PAQQPEGRAN DYDRRDRQDS
     PYSYNDRNRY GGDRGYDRNQ NRERYPGDRS PNPYVSDVDN PLLYRDGGDR NRNRYVSDVE
     NPLLYRDRTP YNPSRDDDDR NRYNPNARPY NPNDPNFGGR NPPDPNYRGP GQRDPNYRDQ
     GFREPGQRFP GDDRTRYPDD PNYPYRSPEE ERFRIENERR FRAETEKLRA FLTEIDRKSS
     LECSLNVAAQ WNFETNINDA TQVEALAAQQ RYNDFQRLLW DQMRRIDQTK IFDDKLYRQV
     RLMSIIGPSA LPPDQLDRYN RIVNDMLAIF NGATICAYEQ PFECGLRLQP HLKDIMAKSR
     DWNELQYTWL EWRRKSGRNM RDLFEQLVDL TNDAGRVNNF TDAAAYWTFP YESRNFREEM
     EQVWREILPL YEMIHAYVRR KLREFYGPDK INKNAPLPDH ILGDMYGQSW QNILDIVIPY
     PGRSFLEVTP EMQKQGYNPL VMFQIAEEFF VSMNMSAMPP DFWASSILTQ PPDRPILCQP
     SSWDFCTGKD YRVKMCTQVT HKDFITVHHE LAHIQYFLNY RNNPKVFRDG ANPGFHEAIG
     DAISLSVASP KHLQNLGLVQ KSVDDTAHDI NFLFSLAMEK VVFLPFALAL EAWRYDVFSK
     RVRKEQYNCH WWLLREEYGG VKPPVLRSEL DFDPGAKYHV AANIPYIK
//
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