FAT1_CAEEL
ID FAT1_CAEEL Reviewed; 402 AA.
AC Q9NEQ0; Q21056;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Omega-3 fatty acid desaturase fat-1;
DE Short=FAT-1 {ECO:0000303|PubMed:11972048, ECO:0000303|PubMed:9037020};
DE EC=1.14.19.- {ECO:0000269|PubMed:14765186, ECO:0000269|PubMed:24391980, ECO:0000269|PubMed:9037020};
DE AltName: Full=FAT-1 N3 desaturase {ECO:0000303|PubMed:11972048};
DE AltName: Full=Fatty acid desaturase 1;
DE AltName: Full=Fatty acid metabolism 1 {ECO:0000303|PubMed:9037020};
GN Name=fat-1; ORFNames=Y67H2A.8;
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=9037020; DOI=10.1073/pnas.94.4.1142;
RA Spychalla J.P., Kinney A.J., Browse J.;
RT "Identification of an animal omega-3 fatty acid desaturase by heterologous
RT expression in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1142-1147(1997).
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, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=14765186; DOI=10.1038/427504a;
RA Kang J.X., Wang J., Wu L., Kang Z.B.;
RT "Transgenic mice: fat-1 mice convert n-6 to n-3 fatty acids.";
RL Nature 427:504-504(2004).
RN [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=24391980; DOI=10.1371/journal.pone.0084871;
RA Zhu G., Ou Q., Zhang T., Jiang X., Sun G., Zhang N., Wang K., Fang H.,
RA Wang M., Sun J., Ge T.;
RT "A more desirable balanced polyunsaturated fatty acid composition achieved
RT by heterologous expression of Delta15/Delta4 desaturases in mammalian
RT cells.";
RL PLoS ONE 8:e84871-e84871(2013).
RN [7]
RP FUNCTION, AND PATHWAY.
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: Omega-3 fatty acid desaturase that recognizes a range of
CC 18- and 20-carbon omega-6 substrates. Introduces a double bond in the
CC fatty acid chain three carbons away from terminal methyl group to
CC biosynthesize n-3 (omega-3) polyunsaturated fatty acids (PUFAs)
CC endogenously (PUFAs are essential for membrane structure and many
CC cellular and physiological processes). Acts on a number of substrates
CC like linoleoyl-CoA ((9Z,12Z)-octadecadienoyl-CoA, 18:2n-6), dihomo-
CC gamma-linolenoyl-CoA ((8Z,11Z,14Z)-eicosatrienoyl-CoA, 20:3n-6), and
CC arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA, 20:4n-6), to
CC generate alpha-linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA,
CC 18:3n-3), (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA (20:4n-3) and
CC (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA (20:5n-3) respectively
CC (PubMed:9037020, PubMed:11972048, PubMed:14765186, PubMed:22041902,
CC PubMed:24391980, PubMed:26806391). Unlike plants, Caenorhabditis
CC elegans desaturases seem to use fatty acyl-CoAs as substrates (By
CC similarity). {ECO:0000250|UniProtKB:G5EGA5,
CC ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:14765186,
CC ECO:0000269|PubMed:22041902, ECO:0000269|PubMed:24391980,
CC ECO:0000269|PubMed:26806391, ECO:0000269|PubMed:9037020}.
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:14765186,
CC ECO:0000269|PubMed:22041902, ECO:0000269|PubMed:24391980,
CC ECO:0000269|PubMed:9037020};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66041;
CC Evidence={ECO:0000269|PubMed:24391980, ECO:0000269|PubMed:9037020,
CC ECO:0000305|PubMed:14765186, ECO:0000305|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36883, 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:74264, ChEBI:CHEBI:74265;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9037020};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36884;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000305|PubMed:9037020};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome
CC b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2
CC Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36867, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57368, ChEBI:CHEBI:73862;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:22041902,
CC ECO:0000269|PubMed:24391980, ECO:0000269|PubMed:9037020};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36868;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000305|PubMed:22041902,
CC ECO:0000305|PubMed:24391980, ECO:0000305|PubMed:9037020};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + 2 Fe(II)-[cytochrome
CC b5] + 2 H(+) + O2 = (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + 2
CC Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:40423, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:73856, ChEBI:CHEBI:73870;
CC Evidence={ECO:0000269|PubMed:24391980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40424;
CC Evidence={ECO:0000305|PubMed:24391980};
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 -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:24391980,
CC ECO:0000305|PubMed:14765186, ECO:0000305|PubMed:26806391}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: The fat-1 mutant displays a reduction in the n-3
CC PUFAs, the homozygous strain is incapable of producing the normal
CC levels of C18 or C20 PUFAs. {ECO:0000269|PubMed:11972048}.
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-1 desaturase activity. Although FAT-1 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; L41807; AAA67369.1; -; mRNA.
DR EMBL; AL132951; CAC44309.1; -; Genomic_DNA.
DR RefSeq; NP_001023560.1; NM_001028389.4.
DR AlphaFoldDB; Q9NEQ0; -.
DR IntAct; Q9NEQ0; 1.
DR STRING; 6239.Y67H2A.8; -.
DR SwissLipids; SLP:000000265; -.
DR EPD; Q9NEQ0; -.
DR PaxDb; Q9NEQ0; -.
DR PeptideAtlas; Q9NEQ0; -.
DR EnsemblMetazoa; Y67H2A.8.1; Y67H2A.8.1; WBGene00001393.
DR GeneID; 178291; -.
DR KEGG; cel:CELE_Y67H2A.8; -.
DR CTD; 178291; -.
DR WormBase; Y67H2A.8; CE22790; WBGene00001393; fat-1.
DR eggNOG; ENOG502QQNB; Eukaryota.
DR GeneTree; ENSGT00970000196583; -.
DR HOGENOM; CLU_033094_1_0_1; -.
DR InParanoid; Q9NEQ0; -.
DR OMA; DTVFVPW; -.
DR OrthoDB; 577374at2759; -.
DR PhylomeDB; Q9NEQ0; -.
DR SignaLink; Q9NEQ0; -.
DR UniPathway; UPA00658; -.
DR PRO; PR:Q9NEQ0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001393; Expressed in adult organism and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042389; F:omega-3 fatty acid desaturase activity; IMP:WormBase.
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:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:WormBase.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 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..402
FT /note="Omega-3 fatty acid desaturase fat-1"
FT /id="PRO_0000423383"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 231
FT /note="E -> D (in Ref. 1; AAA67369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 46559 MW; BE1B1CD794EA98C5 CRC64;
MVAHSSEGLS ATAPVTGGDV LVDARASLEE KEAPRDVNAN TKQATTEEPR IQLPTVDAFR
RAIPAHCFER DLVKSIRYLV QDFAALTILY FALPAFEYFG LFGYLVWNIF MGVFGFALFV
VGHDCLHGSF SDNQNLNDFI GHIAFSPLFS PYFPWQKSHK LHHAFTNHID KDHGHVWIQD
KDWEAMPSWK RWFNPIPFSG WLKWFPVYTL FGFCDGSHFW PYSSLFVRNS ERVQCVISGI
CCCVCAYIAL TIAGSYSNWF WYYWVPLSFF GLMLVIVTYL QHVDDVAEVY EADEWSFVRG
QTQTIDRYYG LGLDTTMHHI TDGHVAHHFF NKIPHYHLIE ATEGVKKVLE PLSDTQYGYK
SQVNYDFFAR FLWFNYKLDY LVHKTAGIMQ FRTTLEEKAK AK
