FAT6_CAEEL
ID FAT6_CAEEL Reviewed; 339 AA.
AC G5EGN2; D3YT93; D3YT94;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Delta(9)-fatty-acid desaturase fat-6 {ECO:0000303|PubMed:10872837, ECO:0000303|PubMed:16839188};
DE EC=1.14.19.- {ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188};
DE EC=1.14.19.1 {ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573};
DE AltName: Full=Fatty-acid desaturase 6;
DE Short=FAT-6 {ECO:0000303|PubMed:10872837, ECO:0000303|PubMed:16839188};
DE AltName: Full=Stearoyl-CoA desaturase fat-6;
GN Name=fat-6; ORFNames=VZK822L.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, CATALYTIC ACTIVITY,
RP PATHWAY, TISSUE SPECIFICITY, AND INDUCTION.
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 stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-
CC CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated
CC fatty acid in Caenorhabditis elegans phospholipids and
CC triacylglycerols. Also acts on palmitoyl-CoA (hexadecanoyl-CoA),
CC heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the
CC monounsaturated fatty acids (MUFAs) produced are further used as
CC substrates to synthesize polyunsaturated fatty acids (PUFAs) by several
CC other desaturases and elongases (PubMed:16839188, PubMed:10872837,
CC PubMed:29237573). Unlike plants, Caenorhabditis elegans desaturases
CC seem to use fatty acyl-CoAs as substrates (By similarity).
CC {ECO:0000250|UniProtKB:G5EGA5, ECO:0000269|PubMed:10872837,
CC ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, 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:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188,
CC ECO:0000269|PubMed:29237573};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722;
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(+) + 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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC Evidence={ECO:0000269|PubMed:16839188, 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=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (9Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:36935, 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:74296,
CC ChEBI:CHEBI:74297; Evidence={ECO:0000269|PubMed:10872837};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36936;
CC Evidence={ECO:0000305|PubMed:10872837};
CC -!- PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis.
CC {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}.
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=G5EGN2-1; Sequence=Displayed;
CC Name=b;
CC IsoId=G5EGN2-2; Sequence=VSP_047791;
CC Name=c;
CC IsoId=G5EGN2-3; Sequence=VSP_047790;
CC -!- TISSUE SPECIFICITY: Expressed in the intestine in adult worms and in
CC all four larval stages. Additional expression in the hypodermis in all
CC life stages. {ECO:0000269|PubMed:16839188}.
CC -!- INDUCTION: Expression is regulated by nhr-80 and nhr-49.
CC {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-5.1 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; AF260244; AAF97550.1; -; mRNA.
DR EMBL; Z95123; CAB08356.1; -; Genomic_DNA.
DR EMBL; Z95123; CBK19477.1; -; Genomic_DNA.
DR EMBL; Z95123; CBK19478.1; -; Genomic_DNA.
DR PIR; T28019; T28019.
DR RefSeq; NP_001255595.1; NM_001268666.1. [G5EGN2-1]
DR RefSeq; NP_001255596.1; NM_001268667.1. [G5EGN2-2]
DR RefSeq; NP_001255597.1; NM_001268668.1. [G5EGN2-3]
DR AlphaFoldDB; G5EGN2; -.
DR SMR; G5EGN2; -.
DR BioGRID; 43217; 13.
DR STRING; 6239.VZK822L.1a.1; -.
DR SwissLipids; SLP:000000270; -.
DR EPD; G5EGN2; -.
DR PaxDb; G5EGN2; -.
DR PeptideAtlas; G5EGN2; -.
DR EnsemblMetazoa; VZK822L.1a.1; VZK822L.1a.1; WBGene00001398. [G5EGN2-1]
DR EnsemblMetazoa; VZK822L.1b.1; VZK822L.1b.1; WBGene00001398. [G5EGN2-2]
DR EnsemblMetazoa; VZK822L.1c.1; VZK822L.1c.1; WBGene00001398. [G5EGN2-3]
DR GeneID; 178122; -.
DR KEGG; cel:CELE_VZK822L.1; -.
DR CTD; 178122; -.
DR WormBase; VZK822L.1a; CE18302; WBGene00001398; fat-6. [G5EGN2-1]
DR WormBase; VZK822L.1b; CE44710; WBGene00001398; fat-6. [G5EGN2-2]
DR WormBase; VZK822L.1c; CE44565; WBGene00001398; fat-6. [G5EGN2-3]
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00970000196153; -.
DR InParanoid; G5EGN2; -.
DR OMA; SCGESWH; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; G5EGN2; -.
DR Reactome; R-CEL-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA01038; -.
DR PRO; PR:G5EGN2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001398; Expressed in larva and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:WormBase.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IGI:WormBase.
DR GO; GO:0045087; P:innate immune response; IEP: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 Alternative splicing; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..339
FT /note="Delta(9)-fatty-acid desaturase fat-6"
FT /id="PRO_0000423388"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_047790"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_047791"
SQ SEQUENCE 339 AA; 39059 MW; F47A49D1959C2887 CRC64;
MTVKTRSNIA KKIEKDGGPE TQYLAVDPNE IIQLQEESKK IPYKMEIVWR NVALFAALHF
AAAIGLYQLI FEAKWQTVIF TFLLYVFGGF GITAGAHRLW SHKSYKATTP MRIFLMILNN
IALQNDVIEW ARDHRCHHKW TDTDADPHNT TRGFFFAHMG WLLVRKHPQV KEQGAKLDMS
DLLSDPVLVF QRKHYFPLVI LCCFILPTII PVYFWKETAF IAFYTAGTFR YCFTLHATWC
INSAAHYFGW KPYDSSITPV ENVFTTIAAV GEGGHNFHHT FPQDYRTSEY SLKYNWTRVL
IDTAAALGLV YDRKTACDEI IGRQVSNHGC DIQRGKSIM
