ID Q17EY8_AEDAE Unreviewed; 335 AA.
AC Q17EY8;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=AAEL003622-PB {ECO:0000313|EMBL:EAT45072.1};
GN ORFNames=AAEL003622 {ECO:0000313|EMBL:EAT45072.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT45072.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT45072.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT45072.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT45072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT45072.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT45072.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT45072.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU000581};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000256|RuleBase:RU000581}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|RuleBase:RU000581}.
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DR EMBL; CH477278; EAT45072.1; -; Genomic_DNA.
DR RefSeq; XP_001657079.1; XM_001657029.1.
DR AlphaFoldDB; Q17EY8; -.
DR VEuPathDB; VectorBase:AAEL003622; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF21; GH07782P; 1.
DR PRINTS; PR00075; FACDDSATRASE.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU000581};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Lipid metabolism {ECO:0000256|RuleBase:RU000581};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000581};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000581};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 335 AA; 38325 MW; DEA354D11B10E828 CRC64;
MATKMASSFQ FLGGNSTMDI NGNGKGYGKG VSVISDANNN ETVLDDDHSI SEKDVNAYLQ
HYNKWKQSVL GHRLTEILRD YFGYEFDAEI KWNNVLMIGI FHVIAIIAFS KLIWIATPIS
YLWGFFVGGC AGFGVTAGVH RLWCHKAYKA KLPLRIILMC CYSIAGQNTI YDWVRDHRIH
HKYSETDGDP HNSNRGFLYA HVGWLMLRKH PECIKKGRLI DMTDITSDPV VQFHHKRIQP
VENKAVSIVA MGEGWHNYHH VFPWDYKAAE LGNYSVNVTT FWLDLFAKIG WAYDLKEPSK
ELVRRTIEKY GDGTHLAIST KDRIEVPDPE ESKKL
//
