FAT4_CAEEL
ID FAT4_CAEEL Reviewed; 447 AA.
AC G5EG11; D5MCT8; E9P887;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Delta(5) fatty acid desaturase fat-4;
DE Short=FAT-4 {ECO:0000303|PubMed:11972048, ECO:0000303|PubMed:9845325};
DE EC=1.14.19.37 {ECO:0000269|PubMed:9917342};
DE EC=1.14.19.44 {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9917342};
DE AltName: Full=FAT-4 Delta(5) desaturase {ECO:0000303|PubMed:11972048};
DE AltName: Full=Fatty acid desaturase 4;
GN Name=fat-4; Synonyms=des-5; ORFNames=T13F2.1;
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] (ISOFORM A), FUNCTION, AND PATHWAY.
RX PubMed=9845325; DOI=10.1016/s0014-5793(98)01385-4;
RA Michaelson L.V., Napier J.A., Lewis M., Griffiths G., Lazarus C.M.,
RA Stobart A.K.;
RT "Functional identification of a fatty acid delta5 desaturase gene from
RT Caenorhabditis elegans.";
RL FEBS Lett. 439:215-218(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=9917342; DOI=10.1006/abbi.1998.1024;
RA Watts J.L., Browse J.;
RT "Isolation and characterization of a Delta 5-fatty acid desaturase from
RT Caenorhabditis elegans.";
RL Arch. Biochem. Biophys. 362:175-182(1999).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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(5) fatty acid desaturase and behaves
CC as a (8-3) desaturase. Introduces a double bond in the fatty acid chain
CC 5 carbons away from carboxy terminal to biosynthesize polyunsaturated
CC fatty acids (PUFAs) endogenously (PUFAs are essential for membrane
CC structure and many cellular and physiological processes). Acts on a
CC variety of substrates such as dihomo-gamma-linoleoyl-CoA ((8Z,11Z,14Z)-
CC eicosatrienoyl-CoA, 20:3n-6) to generate arachidonoyl-CoA
CC ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA, 20:4n-6). Also acts on a number
CC of other substrates, including fatty acids that do not contain a double
CC bond at the 8 position like (11Z,14Z,17Z)-eicosatrienoyl-CoA (20:3n-3)
CC to produce (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA (20:4n-3)
CC (PubMed:9845325, PubMed:9917342, PubMed:11972048, PubMed:26806391).
CC Unlike plants, Caenorhabditis elegans desaturases seem to use fatty
CC acyl-CoAs as substrates (By similarity). {ECO:0000250|UniProtKB:G5EGA5,
CC ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:26806391,
CC ECO:0000269|PubMed:9845325, ECO:0000269|PubMed:9917342}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (5Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:46524, 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:76410,
CC ChEBI:CHEBI:78663; EC=1.14.19.37;
CC Evidence={ECO:0000269|PubMed:9917342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46525;
CC Evidence={ECO:0000305|PubMed:9917342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z,17Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46528, 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:74328, ChEBI:CHEBI:78664; EC=1.14.19.37;
CC Evidence={ECO:0000269|PubMed:9917342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46529;
CC Evidence={ECO:0000305|PubMed:9917342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z,17Z)-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:46420, 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:73862, ChEBI:CHEBI:74265;
CC EC=1.14.19.44; Evidence={ECO:0000269|PubMed:11972048,
CC ECO:0000305|PubMed:26806391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000305|PubMed:26806391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46424, 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:57368, ChEBI:CHEBI:74264; EC=1.14.19.44;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9917342,
CC ECO:0000305|PubMed:26806391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46425;
CC Evidence={ECO:0000269|PubMed:11972048, ECO:0000305|PubMed:26806391,
CC ECO:0000305|PubMed:9917342};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9845325,
CC ECO:0000269|PubMed:9917342}.
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=G5EG11-1; Sequence=Displayed;
CC Name=b;
CC IsoId=G5EG11-2; Sequence=VSP_047789;
CC Name=c;
CC IsoId=G5EG11-3; Sequence=VSP_047788;
CC -!- DISRUPTION PHENOTYPE: The fat-4 mutants lack detectable Delta(5)-
CC unsaturated fatty acids. {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-4 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; AF078796; AAC95143.1; -; mRNA.
DR EMBL; AF114440; AAD13294.1; -; mRNA.
DR EMBL; Z81122; CAB61031.1; -; Genomic_DNA.
DR EMBL; Z81122; CBL43456.1; -; Genomic_DNA.
DR EMBL; Z81122; CBZ01822.1; -; Genomic_DNA.
DR PIR; T43319; T43319.
DR RefSeq; NP_001255423.1; NM_001268494.1. [G5EG11-1]
DR RefSeq; NP_001255424.1; NM_001268495.1. [G5EG11-2]
DR RefSeq; NP_001255425.1; NM_001268496.1. [G5EG11-3]
DR AlphaFoldDB; G5EG11; -.
DR BioGRID; 42923; 1.
DR STRING; 6239.T13F2.1a.1; -.
DR SwissLipids; SLP:000000268; -.
DR EPD; G5EG11; -.
DR PaxDb; G5EG11; -.
DR PeptideAtlas; G5EG11; -.
DR EnsemblMetazoa; T13F2.1a.1; T13F2.1a.1; WBGene00001396. [G5EG11-1]
DR EnsemblMetazoa; T13F2.1b.1; T13F2.1b.1; WBGene00001396. [G5EG11-2]
DR EnsemblMetazoa; T13F2.1c.1; T13F2.1c.1; WBGene00001396. [G5EG11-3]
DR GeneID; 177819; -.
DR KEGG; cel:CELE_T13F2.1; -.
DR CTD; 177819; -.
DR WormBase; T13F2.1a; CE25113; WBGene00001396; fat-4. [G5EG11-1]
DR WormBase; T13F2.1b; CE44752; WBGene00001396; fat-4. [G5EG11-2]
DR WormBase; T13F2.1c; CE45810; WBGene00001396; fat-4. [G5EG11-3]
DR eggNOG; KOG4232; Eukaryota.
DR GeneTree; ENSGT00950000182990; -.
DR HOGENOM; CLU_016265_1_1_1; -.
DR InParanoid; G5EG11; -.
DR OMA; YAKQEAN; -.
DR OrthoDB; 1060606at2759; -.
DR PhylomeDB; G5EG11; -.
DR UniPathway; UPA00658; -.
DR PRO; PR:G5EG11; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001396; Expressed in adult organism and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0062076; F:acyl-CoA delta5-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:0006629; P:lipid metabolic process; IBA:GO_Central.
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..447
FT /note="Delta(5) fatty acid desaturase fat-4"
FT /id="PRO_0000423386"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..80
FT /note="Cytochrome b5 heme-binding"
FT VAR_SEQ 1..392
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_047788"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_047789"
SQ SEQUENCE 447 AA; 52348 MW; D7E09CE0E2975015 CRC64;
MVLREQEHEP FFIKIDGKWC QIDDAVLRSH PGGSAITTYK NMDATTVFHT FHTGSKEAYQ
WLTELKKECP TQEPEIPDIK DDPIKGIDDV NMGTFNISEK RSAQINKSFT DLRMRVRAEG
LMDGSPLFYI RKILETIFTI LFAFYLQYHT YYLPSAILMG VAWQQLGWLI HEFAHHQLFK
NRYYNDLASY FVGNFLQGFS SGGWKEQHNV HHAATNVVGR DGDLDLVPFY ATVAEHLNNY
SQDSWVMTLF RWQHVHWTFM LPFLRLSWLL QSIIFVSQMP THYYDYYRNT AIYEQVGLSL
HWAWSLGQLY FLPDWSTRIM FFLVSHLVGG FLLSHVVTFN HYSVEKFALS SNIMSNYACL
QIMTTRNMRP GRFIDWLWGG LNYQIEHHLF PTMPRHNLNT VMPLVKEFAA ANGLPYMVDD
YFTGFWLEIE QFRNIANVAA KLTKKIA
