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
//