FAT3_CAEEL
ID FAT3_CAEEL Reviewed; 443 AA.
AC Q23221; E9P867; E9P868; O61388;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Delta(6)-fatty-acid desaturase fat-3 {ECO:0000303|PubMed:11972048};
DE Short=FAT-3 {ECO:0000303|PubMed:11972048, ECO:0000303|PubMed:26806391};
DE EC=1.14.19.3 {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9480865};
DE AltName: Full=Delta(6)-fatty-acid desaturase {ECO:0000303|PubMed:9480865};
DE Short=Ceeld6 {ECO:0000303|PubMed:9480865};
DE AltName: Full=Fatty acid desaturase 3;
GN Name=fat-3; ORFNames=W08D2.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=9480865; DOI=10.1042/bj3300611;
RA Napier J.A., Hey S.J., Lacey D.J., Shewry P.R.;
RT "Identification of a caenorhabditis elegans Delta6-fatty-acid-desaturase by
RT heterologous expression in saccharomyces cerevisiae.";
RL Biochem. J. 330:611-614(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=11972048; DOI=10.1073/pnas.092064799;
RA Watts J.L., Browse J.;
RT "Genetic dissection of polyunsaturated fatty acid synthesis in
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5854-5859(2002).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-186.
RX PubMed=18094048; DOI=10.1091/mbc.e07-07-0719;
RA Marza E., Long T., Saiardi A., Sumakovic M., Eimer S., Hall D.H.,
RA Lesa G.M.;
RT "Polyunsaturated fatty acids influence synaptojanin localization to
RT regulate synaptic vesicle recycling.";
RL Mol. Biol. Cell 19:833-842(2008).
RN [5]
RP FUNCTION.
RX PubMed=26806391; DOI=10.1016/j.bbalip.2016.01.009;
RA Zhang Y., Wang H., Zhang J., Hu Y., Zhang L., Wu X., Su X., Li T., Zou X.,
RA Liang B.;
RT "The cytochrome b5 reductase HPO-19 is required for biosynthesis of
RT polyunsaturated fatty acids in Caenorhabditis elegans.";
RL Biochim. Biophys. Acta 1861:310-319(2016).
CC -!- FUNCTION: Can function as a Delta(6) fatty acid desaturase. Introduces
CC a double bond in the fatty acid chain 6 carbons away from carboxy
CC terminal to biosynthesize polyunsaturated fatty acids (PUFAs)
CC endogenously (PUFAs are essential for membrane structure and many
CC cellular and physiological processes). Acts on a variety of substrates
CC such as linoleoyl-CoA ((9Z,12Z)-octadecadienoyl-CoA, C18:2n-6) and
CC alpha-linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA, C18:3n-3) to
CC produce gamma-linolenoyl-CoA ((6Z,9Z,12Z)-octadecatrienoyl-CoA, C18:3n-
CC 6) and (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA (18:4n-3) respectively
CC (PubMed:9480865, PubMed:11972048). Unlike plants, Caenorhabditis
CC elegans desaturases seem to use fatty acyl-CoAs as substrates (By
CC similarity). Plays a role in synaptic vesicle recycling by regulating
CC synaptojanin unc-26 localization at synapses (PubMed:18094048).
CC {ECO:0000250|UniProtKB:G5EGA5, ECO:0000269|PubMed:11972048,
CC ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:9480865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:47140, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57363,
CC ChEBI:CHEBI:57383; EC=1.14.19.3;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9480865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47141;
CC Evidence={ECO:0000269|PubMed:11972048};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:47144, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:71489, ChEBI:CHEBI:74034; EC=1.14.19.3;
CC Evidence={ECO:0000269|PubMed:11972048};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47145;
CC Evidence={ECO:0000269|PubMed:11972048};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9480865}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q23221-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q23221-2; Sequence=VSP_047787;
CC Name=c;
CC IsoId=Q23221-3; Sequence=VSP_047786;
CC -!- DISRUPTION PHENOTYPE: The fat-3 mutants lack detectable Delta6-
CC unsaturated fatty acids and have decreased C20 fatty acids levels,
CC these animals require an additional day of development before
CC commencing egg laying (PubMed:11972048). Impaired synaptic vesicle (SV)
CC recycling characterized by the presence of enlarged SV and the
CC formation of abnormal endocytic membrane-bound structures at synapses.
CC The number of SVs is reduced by 37 percent although SV production in
CC neuron cell body and their transport to release sites are normal
CC (PubMed:18094048). {ECO:0000269|PubMed:11972048,
CC ECO:0000269|PubMed:18094048}.
CC -!- MISCELLANEOUS: HPO-19 and T05H4.4 are cytochrome b5 reductases required
CC for PUFA desaturation in Caenorhabditis elegans. HPO-19 and T05H4.4
CC knockdown or mutation alter FAT-3 desaturase activity.
CC {ECO:0000269|PubMed:26806391}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF031477; AAC15586.1; -; mRNA.
DR EMBL; Z70271; CAA94233.2; -; Genomic_DNA.
DR EMBL; Z70271; CBZ01799.1; -; Genomic_DNA.
DR EMBL; Z70271; CBZ01800.1; -; Genomic_DNA.
DR PIR; T26280; T26280.
DR RefSeq; NP_001255426.1; NM_001268497.1. [Q23221-1]
DR RefSeq; NP_001255427.1; NM_001268498.1. [Q23221-2]
DR RefSeq; NP_001255428.1; NM_001268499.1. [Q23221-3]
DR AlphaFoldDB; Q23221; -.
DR BioGRID; 42924; 1.
DR DIP; DIP-27071N; -.
DR IntAct; Q23221; 1.
DR STRING; 6239.W08D2.4a; -.
DR SwissLipids; SLP:000000267; -.
DR EPD; Q23221; -.
DR PaxDb; Q23221; -.
DR PeptideAtlas; Q23221; -.
DR EnsemblMetazoa; W08D2.4a.1; W08D2.4a.1; WBGene00001395. [Q23221-1]
DR EnsemblMetazoa; W08D2.4b.1; W08D2.4b.1; WBGene00001395. [Q23221-2]
DR EnsemblMetazoa; W08D2.4c.1; W08D2.4c.1; WBGene00001395. [Q23221-3]
DR GeneID; 177820; -.
DR KEGG; cel:CELE_W08D2.4; -.
DR CTD; 177820; -.
DR WormBase; W08D2.4a; CE25153; WBGene00001395; fat-3. [Q23221-1]
DR WormBase; W08D2.4b; CE45719; WBGene00001395; fat-3. [Q23221-2]
DR WormBase; W08D2.4c; CE45812; WBGene00001395; fat-3. [Q23221-3]
DR eggNOG; KOG4232; Eukaryota.
DR GeneTree; ENSGT00950000182990; -.
DR HOGENOM; CLU_016265_1_1_1; -.
DR InParanoid; Q23221; -.
DR OMA; QWWKNKH; -.
DR OrthoDB; 1060606at2759; -.
DR PhylomeDB; Q23221; -.
DR SignaLink; Q23221; -.
DR UniPathway; UPA00658; -.
DR PRO; PR:Q23221; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001395; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; Q23221; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IC:WormBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0016213; F:linoleoyl-CoA desaturase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:WormBase.
DR GO; GO:0014055; P:acetylcholine secretion, neurotransmission; IMP:WormBase.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0032456; P:endocytic recycling; IMP:WormBase.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0035264; P:multicellular organism growth; IMP:WormBase.
DR GO; GO:0006936; P:muscle contraction; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:WormBase.
DR GO; GO:0001820; P:serotonin secretion; IMP:WormBase.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:WormBase.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..443
FT /note="Delta(6)-fatty-acid desaturase fat-3"
FT /id="PRO_0000423385"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..71
FT /note="Cytochrome b5 heme-binding"
FT VAR_SEQ 1..366
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_047786"
FT VAR_SEQ 1..258
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_047787"
FT MUTAGEN 186
FT /note="S->F: In wa22; Impaired synaptic vesicle recycling
FT characterized by a partially diffused localization of
FT synaptic vesicle protein snb-1 along the dorsal nerve cord
FT and the formation of enlarged synaptic vesicles. snb-1
FT diffused localization is increased in a unc-57 (ok310)
FT mutant background but not in a unc-26 (s1710) mutant
FT background. Severe depletion of unc-26 at release sites in
FT the dorsal nerve cord and increased phosphatidylinositol
FT 4,5-bisphosphate levels at release sites and at the axonal
FT plasma membrane. Impaired locomotion."
FT /evidence="ECO:0000269|PubMed:18094048"
FT CONFLICT 401
FT /note="M -> V (in Ref. 1; AAC15586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 51773 MW; 9513D611ECB99A06 CRC64;
MVVDKNASGL RMKVDGKWLY LSEELVKKHP GGAVIEQYRN SDATHIFHAF HEGSSQAYKQ
LDLLKKHGEH DEFLEKQLEK RLDKVDINVS AYDVSVAQEK KMVESFEKLR QKLHDDGLMK
ANETYFLFKA ISTLSIMAFA FYLQYLGWYI TSACLLALAW QQFGWLTHEF CHQQPTKNRP
LNDTISLFFG NFLQGFSRDW WKDKHNTHHA ATNVIDHDGD IDLAPLFAFI PGDLCKYKAS
FEKAILKIVP YQHLYFTAML PMLRFSWTGQ SVQWVFKENQ MEYKVYQRNA FWEQATIVGH
WAWVFYQLFL LPTWPLRVAY FIISQMGGGL LIAHVVTFNH NSVDKYPANS RILNNFAALQ
ILTTRNMTPS PFIDWLWGGL NYQIEHHLFP TMPRCNLNAC MKYVKEWCKE NNLPYLVDDY
FDGYAMNLQQ LKNMAEHIQA KAA
