ID C7BBB5_9MUSC Unreviewed; 356 AA. AC C7BBB5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-APR-2021, entry version 32. DE SubName: Full=Desaturase {ECO:0000313|EMBL:ACT76161.1}; GN Name=desatF {ECO:0000313|EMBL:ACT76161.1}; OS Drosophila trilutea. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=94114 {ECO:0000313|EMBL:ACT76161.1}; RN [1] {ECO:0000313|EMBL:ACT76161.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19652700; DOI=10.1371/journal.pbio.1000168; RA Shirangi T.R., Dufour H.D., Williams T.M., Carroll S.B.; RT "Rapid evolution of sex pheromone-producing enzyme expression in RT Drosophila."; RL PLoS Biol. 7:e1000168-e1000168(2009). CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; 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 may contain the active site and/or be CC involved in metal ion binding. {ECO:0000256|RuleBase:RU000581}. CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. CC {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|RuleBase:RU000581}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FJ869337; ACT76161.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 InterPro; IPR005804; FA_desaturase_dom. DR InterPro; IPR001522; FADS-1_CS. DR PANTHER; PTHR11351; PTHR11351; 1. DR Pfam; PF00487; FA_desaturase; 1. DR PRINTS; PR00075; FACDDSATRASE. DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1. PE 3: Inferred from homology; KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581}; KW Fatty acid metabolism {ECO:0000256|RuleBase:RU000581}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000581}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000581, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 42..66 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 73..96 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 189..210 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 216..236 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 69..279 FT /note="FA_desaturase" FT /evidence="ECO:0000259|Pfam:PF00487" SQ SEQUENCE 356 AA; 40955 MW; 25876972D05433F4 CRC64; MPPNSRDTAT GVLFESDVET VDGGLTKDVT HLKTTDGSRL QLVWLNIVLF VILHTASLYG VWLLFAEATW TTFLLFIPAV VMTILGVSGG AHRLWAHRTF KANSPLKLIF LFLNTLAFQD AVYYWARDHR VHHKYTETDG DPYNSQRGWF FSHIGWLCCR KHPEVVEKGK QIDLSDLEXD PLVMFQKKYY LLLMPLICFV LPTAVPMYLW GESLNTSXHV MALLRWCLSL NLIWLVNSSA HMFGMKPYDK NISPVDQGFL ITCRVGEGYH NYHHVFPWDY KSAELGKYSQ DVTTKFIDFF AYLGWAYDLK SVSLDLVRRR AERTGDGSHP VWGWGDRDQL MEDIGDTTIS HQRKGK //