FAT5_CAEEL
ID FAT5_CAEEL Reviewed; 333 AA.
AC G5ED44;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Delta(9)-fatty-acid desaturase fat-5 {ECO:0000303|PubMed:10872837};
DE EC=1.14.19.- {ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573};
DE AltName: Full=Fatty acid desaturase 5;
DE Short=FAT-5 {ECO:0000303|PubMed:10872837, ECO:0000303|PubMed:16839188};
DE AltName: Full=Palmitoyl-CoA fatty acid desaturase;
GN Name=fat-5; ORFNames=W06D12.3;
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, CATALYTIC ACTIVITY, INDUCTION, TISSUE
RP SPECIFICITY, AND PATHWAY.
RX PubMed=16839188; DOI=10.1371/journal.pgen.0020108;
RA Brock T.J., Browse J., Watts J.L.;
RT "Genetic regulation of unsaturated fatty acid composition in C. elegans.";
RL PLoS Genet. 2:E108-E108(2006).
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, AND CATALYTIC ACTIVITY.
RX PubMed=10872837; DOI=10.1006/bbrc.2000.2772;
RA Watts J.L., Browse J.;
RT "A palmitoyl-CoA-specific delta9 fatty acid desaturase from Caenorhabditis
RT elegans.";
RL Biochem. Biophys. Res. Commun. 272:263-269(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29237573; DOI=10.1016/j.bbalip.2017.12.007;
RA He B., Zhang J., Wang Y., Li Y., Zou X., Liang B.;
RT "Identification of cytochrome b5 CYTB-5.1 and CYTB-5.2 in C. elegans;
RT evidence for differential regulation of SCD.";
RL Biochim. Biophys. Acta 1863:235-246(2018).
CC -!- FUNCTION: Delta(9)-fatty acid desaturase that acts preferentially on
CC palmitoyl-CoA (hexadecanoyl-CoA) producing the monounsaturated
CC palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA), which can be elongated to
CC (11Z)-octadecenoyl-CoA (the most abundant monounsaturated fatty acid in
CC Caenorhabditis elegans phospholipids and triacylglycerols). Also acts
CC on pentadecanoyl-CoA, heptadecanoyl-CoA and myristoyl-CoA
CC (tetradecanoyl-CoA), the monounsaturated fatty acids (MUFAs) produced
CC are further used as substrates to synthesize polyunsaturated fatty
CC acids (PUFAs) by several other desaturases and elongases
CC (PubMed:16839188, PubMed:10872837, PubMed:29237573). Unlike plants,
CC Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as
CC substrates (By similarity). {ECO:0000250|UniProtKB:G5EGA5,
CC ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188,
CC ECO:0000269|PubMed:29237573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36931, 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:57379,
CC ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:10872837,
CC ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188,
CC ECO:0000269|PubMed:29237573};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + tetradecanoyl-CoA =
CC (9Z)-tetradecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36939, 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:57385,
CC ChEBI:CHEBI:65060; Evidence={ECO:0000269|PubMed:10872837};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36940;
CC Evidence={ECO:0000305|PubMed:10872837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + heptadecanoyl-CoA + O2 =
CC (9Z)-heptadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36951, 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:74307,
CC ChEBI:CHEBI:74308; Evidence={ECO:0000269|PubMed:10872837};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36952;
CC Evidence={ECO:0000305|PubMed:10872837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + pentadecanoyl-CoA =
CC (9Z)-pentadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36955, 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:74309,
CC ChEBI:CHEBI:74310; Evidence={ECO:0000269|PubMed:10872837};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36956;
CC Evidence={ECO:0000305|PubMed:10872837};
CC -!- PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis.
CC {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine in adult worms and in
CC all four larval stages. Additional expression in the pharynx and tail
CC cells after hatching and throughout the lifespan.
CC {ECO:0000269|PubMed:16839188}.
CC -!- INDUCTION: Expression is regulated by nhr-80 and nhr-49 in the
CC intestine. {ECO:0000269|PubMed:16839188}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250}.
CC -!- MISCELLANEOUS: Cytochrome b5 CYTB-5.2 is specifically required for the
CC desaturase activity, its knockdown or mutation alters the enzyme
CC activity. {ECO:0000269|PubMed:29237573}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF260242; AAF97548.1; -; mRNA.
DR EMBL; Z82073; CAB04924.1; -; Genomic_DNA.
DR PIR; T26230; T26230.
DR RefSeq; NP_507482.1; NM_075081.4.
DR AlphaFoldDB; G5ED44; -.
DR SMR; G5ED44; -.
DR BioGRID; 45141; 3.
DR STRING; 6239.W06D12.3; -.
DR SwissLipids; SLP:000000269; -.
DR EPD; G5ED44; -.
DR PaxDb; G5ED44; -.
DR PeptideAtlas; G5ED44; -.
DR EnsemblMetazoa; W06D12.3.1; W06D12.3.1; WBGene00001397.
DR GeneID; 180162; -.
DR KEGG; cel:CELE_W06D12.3; -.
DR CTD; 180162; -.
DR WormBase; W06D12.3; CE16551; WBGene00001397; fat-5.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00970000196153; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; G5ED44; -.
DR OMA; FIDCMAS; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; G5ED44; -.
DR Reactome; R-CEL-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA01038; -.
DR PRO; PR:G5ED44; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001397; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; ISS:WormBase.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IGI:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IGI:WormBase.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IBA:GO_Central.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR PRINTS; PR00075; FACDDSATRASE.
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..333
FT /note="Delta(9)-fatty-acid desaturase fat-5"
FT /id="PRO_0000423387"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 333 AA; 38462 MW; 4DA52D619FC40F99 CRC64;
MTQIKVDAII SKQFLAADLN EIRQMQEESK KQVIKMEIVW KNVALFVALH IGALVGLYQL
VFQAKWATVG WVFLLHTLGS MGVTGGAHRL WAHRAYKATL SWRVFLMLIN SIAFQNDIID
WARDHRCHHK WTDTDADPHS TNRGMFFAHM GWLLVKKHDQ LKIQGGKLDL SDLYEDPVLM
FQRKNYLPLV GIFCFALPTF IPVVLWGESA FIAFYTAALF RYCFTLHATW CINSVSHWVG
WQPYDHQASS VDNLWTSIAA VGEGGHNYHH TFPQDYRTSE HAEFLNWTRV LIDFGASIGM
VYDRKTTPEE VIQRQCKKFG CETEREKMLH KLG
