FAT2_CAEEL
ID FAT2_CAEEL Reviewed; 376 AA.
AC G5EGA5;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Delta(12) fatty acid desaturase fat-2 {ECO:0000303|PubMed:11972048};
DE Short=FAT-2 {ECO:0000303|PubMed:11972048};
DE EC=1.14.19.- {ECO:0000269|PubMed:22041902};
DE EC=1.14.19.6 {ECO:0000269|PubMed:10775428, ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:22041902};
DE AltName: Full=Fatty acid desaturase 2;
GN Name=fat-2; ORFNames=W02A2.1;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10775428; DOI=10.1006/abbi.2000.1733;
RA Peyou-Ndi M.M., Watts J.L., Browse J.;
RT "Identification and characterization of an animal delta(12) fatty acid
RT desaturase gene by heterologous expression in Saccharomyces cerevisiae.";
RL Arch. Biochem. Biophys. 376:399-408(2000).
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, AND PATHWAY.
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, AND CATALYTIC ACTIVITY.
RX PubMed=22041902; DOI=10.1074/jbc.m111.266114;
RA Zhou X.-R., Green A.G., Singh S.P.;
RT "Caenorhabditis elegans Delta12-desaturase FAT-2 is a bifunctional
RT desaturase able to desaturate a diverse range of fatty acid substrates at
RT the Delta12 and Delta15 positions.";
RL J. Biol. Chem. 286:43644-43650(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
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(12)/Delta(15) bifunctional desaturase
CC and behaves as a nu +3' desaturase. Introduces a double bond in the
CC fatty acid chain three carbons away from an existing double bond to
CC biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs
CC are essential for membrane structure and many cellular and
CC physiological processes). Acts on a number of substrates like oleoyl-
CC CoA ((9Z)-octadecenoyl-CoA, 18:1n-9), palmitoleoyl-CoA ((9Z)-
CC hexadecenoyl-CoA, 16:1n-7), and gamma-linolenoyl-CoA ((6Z,9Z,12Z)-
CC octadecatrienoyl-CoA, 18:3n-6), to generate linoleoyl-CoA ((9Z,12Z)-
CC octadecadienoyl-CoA, 18:2n-6), (9Z,12Z)-hexadecadienoyl-CoA (16:2n-4)
CC and (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA (18:4n-3) respectively
CC (PubMed:10775428, PubMed:11972048, PubMed:22041902, PubMed:26806391).
CC Unlike plants, Caenorhabditis elegans desaturases seem to use fatty
CC acyl-CoAs as substrates (Probable). {ECO:0000269|PubMed:10775428,
CC ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:22041902,
CC ECO:0000269|PubMed:26806391, ECO:0000305|PubMed:10775428}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:25856, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57387; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:10775428, ECO:0000269|PubMed:11972048,
CC ECO:0000269|PubMed:22041902, ECO:0000269|PubMed:26806391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25857;
CC Evidence={ECO:0000269|PubMed:26806391, ECO:0000305|PubMed:10775428,
CC ECO:0000305|PubMed:11972048, ECO:0000305|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:45096, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:61540,
CC ChEBI:CHEBI:76552; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:10775428, ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45097;
CC Evidence={ECO:0000305|PubMed:10775428, ECO:0000305|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:66040, 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:57383,
CC ChEBI:CHEBI:74034; Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66041;
CC Evidence={ECO:0000305|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-heptadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (9Z,12Z)-heptadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:42196, 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:74308,
CC ChEBI:CHEBI:78690; Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42197;
CC Evidence={ECO:0000305|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-pentadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (9Z,12Z)-pentadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:42192, 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:74310,
CC ChEBI:CHEBI:78684; Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42193;
CC Evidence={ECO:0000305|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-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:42180, 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:57363, ChEBI:CHEBI:71489;
CC Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42181;
CC Evidence={ECO:0000305|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (9Z,12Z)-tetradecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:42176, 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:65060,
CC ChEBI:CHEBI:78680; Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42177;
CC Evidence={ECO:0000305|PubMed:22041902};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:26806391}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: The fat-2(wa17) mutant leads to high levels of
CC C18:1n-9 and low levels of PUFAs. {ECO:0000269|PubMed:26806391}.
CC -!- MISCELLANEOUS: HPO-19 and T05H4.4 are cytochrome b5 reductases required
CC for PUFA desaturation in Caenorhabditis elegans. HPO-19 knockdown or
CC mutation alters FAT-2 desaturase activity. Although FAT-2 lacks a
CC cytochrome b5 domain, its N-terminal contains a DUF3474 domain that may
CC possess some oxidoreductase activity for electron transfer, obviating
CC the need for an extra cytochrome b5 enzyme, but still requiring
CC cytochrome b5 reductase HPO-19/T05H4.4 to become activated.
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; AF240777; AAF63745.1; -; mRNA.
DR EMBL; Z82286; CAB05304.1; -; Genomic_DNA.
DR PIR; T26075; T26075.
DR RefSeq; NP_502560.1; NM_070159.7.
DR AlphaFoldDB; G5EGA5; -.
DR BioGRID; 43381; 2.
DR STRING; 6239.W02A2.1; -.
DR SwissLipids; SLP:000000266; -.
DR EPD; G5EGA5; -.
DR PaxDb; G5EGA5; -.
DR PeptideAtlas; G5EGA5; -.
DR EnsemblMetazoa; W02A2.1a.1; W02A2.1a.1; WBGene00001394.
DR GeneID; 178293; -.
DR KEGG; cel:CELE_W02A2.1; -.
DR CTD; 178293; -.
DR WormBase; W02A2.1a; CE21231; WBGene00001394; fat-2.
DR eggNOG; ENOG502QQNB; Eukaryota.
DR GeneTree; ENSGT00970000196583; -.
DR HOGENOM; CLU_033094_1_0_1; -.
DR InParanoid; G5EGA5; -.
DR OMA; FYLFHNY; -.
DR OrthoDB; 577374at2759; -.
DR PhylomeDB; G5EGA5; -.
DR BRENDA; 1.14.19.39; 1045.
DR BRENDA; 1.14.19.6; 1045.
DR UniPathway; UPA00658; -.
DR PRO; PR:G5EGA5; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001394; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; G5EGA5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016720; F:delta12-fatty acid dehydrogenase activity; IMP:WormBase.
DR GO; GO:0102985; F:delta12-fatty-acid 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:0102987; F:palmitoleic acid delta 12 desaturase activity; IEA:RHEA.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:WormBase.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0030497; P:fatty acid elongation; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IEP:WormBase.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:WormBase.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="Delta(12) fatty acid desaturase fat-2"
FT /id="PRO_0000423384"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 376 AA; 43463 MW; E3FE314148DA4458 CRC64;
MTIATKVNTN KKDLDTIKVP ELPSVAAVKA AIPEHCFVKD PLTSISYLIK DYVLLAGLYF
AVPYIEHYLG WIGLLGWYWA MGIVGSALFC VGHDCGHGSF SDYEWLNDLC GHLAHAPILA
PFWPWQKSHR QHHQYTSHVE KDKGHPWVTE EDYNNRTAIE KYFAVIPISG WLRWNPIYTI
VGLPDGSHFW PWSRLFETTE DRVKCAVSGV ACAICAYIAF VLCDYSVYTF VKYYYIPLLF
QGLILVIITY LQHQNEDIEV YEADEWGFVR GQTQTIDRHW GFGLDNIMHN ITNGHVAHHF
FFTKIPHYHL LEATPAIKKA LEPLKDTQYG YKREVNYNWF FKYLHYNVTL DYLTHKAKGV
LQYRSGVEAA KAKKAQ
