FAT7_CAEEL
ID FAT7_CAEEL Reviewed; 338 AA.
AC G5EGH6;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Delta(9)-fatty-acid desaturase fat-7 {ECO:0000303|PubMed:10872837, ECO:0000303|PubMed:16839188};
DE Short=FAT-7 {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 7;
DE AltName: Full=Stearoyl-CoA desaturase fat-7;
GN Name=fat-7; ORFNames=F10D2.9;
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, PATHWAY, TISSUE
RP 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, AND DISRUPTION PHENOTYPE.
RX PubMed=15719061; DOI=10.1371/journal.pbio.0030053;
RA Van Gilst M.R., Hadjivassiliou H., Jolly A., Yamamoto K.R.;
RT "Nuclear hormone receptor NHR-49 controls fat consumption and fatty acid
RT composition in C. elegans.";
RL PLoS Biol. 3:e53-e53(2005).
RN [5]
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 triacylglycerols
CC (PubMed:16839188, PubMed:10872837, PubMed:29237573). Also acts on
CC palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-
CC octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids
CC (MUFAs) produced are further used by several other desaturases and
CC elongases as substrates to synthesize polyunsaturated fatty acids
CC (PUFAs) endogenously (PUFAs are essential for membrane structure and
CC many cellular and physiological processes) (PubMed:16839188,
CC PubMed:10872837, PubMed:29237573). Unlike plants, Caenorhabditis
CC elegans desaturases seem to use fatty acyl-CoAs as substrates (By
CC similarity). Partially inhibits expression of genes involved in beta-
CC oxidation, such as ech-1 and acs-2, perhaps signaling via the actions
CC of one of its fatty acid products (PubMed:15719061). May form part of a
CC negative feedback loop with the transcription factor nhr-49 to limit
CC beta-oxidation, in which nhr-49 stimulates expression of fat-7 and acs-
CC 2, and in turn fat-7 indirectly inhibits acs-2 and other genes also
CC involved in beta-oxidation (PubMed:15719061).
CC {ECO:0000250|UniProtKB:G5EGA5, ECO:0000269|PubMed:10872837,
CC ECO:0000269|PubMed:15719061, ECO:0000269|PubMed:16839188,
CC 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 -!- TISSUE SPECIFICITY: Expressed in the intestine in adult worms and in
CC all four larval 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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a significant
CC increase in the abundance of C18:0 fatty acid, as well as a decrease in
CC the levels of C18:1n9 and C18:2n6 fatty acids (PubMed:15719061). Slight
CC reduction in polyunsaturated fatty acids (PUFAs) (PubMed:15719061).
CC Widespread vacuole formation, germ line necrosis and shortened life-
CC span (PubMed:15719061). {ECO:0000269|PubMed:15719061}.
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; AF260243; AAF97549.1; -; mRNA.
DR EMBL; FO081104; CCD69123.1; -; Genomic_DNA.
DR PIR; T28723; T28723.
DR RefSeq; NP_504814.1; NM_072413.6.
DR AlphaFoldDB; G5EGH6; -.
DR SMR; G5EGH6; -.
DR BioGRID; 44145; 2.
DR STRING; 6239.F10D2.9; -.
DR SwissLipids; SLP:000000271; -.
DR EPD; G5EGH6; -.
DR PaxDb; G5EGH6; -.
DR PeptideAtlas; G5EGH6; -.
DR EnsemblMetazoa; F10D2.9.1; F10D2.9.1; WBGene00001399.
DR GeneID; 179100; -.
DR KEGG; cel:CELE_F10D2.9; -.
DR CTD; 179100; -.
DR WormBase; F10D2.9; CE09320; WBGene00001399; fat-7.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00970000196153; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; G5EGH6; -.
DR OMA; CQHGPID; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; G5EGH6; -.
DR Reactome; R-CEL-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA01038; -.
DR PRO; PR:G5EGH6; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001399; 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; IDA:WormBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:WormBase.
DR GO; GO:0032364; P:oxygen homeostasis; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IGI:WormBase.
DR GO; GO:0001666; P:response to hypoxia; IMP:UniProtKB.
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..338
FT /note="Delta(9)-fatty-acid desaturase fat-7"
FT /id="PRO_0000423389"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 338 AA; 39062 MW; EDC3EEB315B6B30B CRC64;
MTVKTRASIA KKIEKDGLDS QYLFMDPNEV LQVQEESKKI PYKMEIVWRN VALFAALHVA
AAIGLYELVF HAKWQTAVFS FALYVFSGFG ITAGAHRLWS HKSYKATTPM RIFLMLLNNI
ALQNDIIEWA RDHRCHHKWT DTDADPHNTT RGFFFTHMGW LLVRKHPQVK EHGGKLDLSD
LFSDPVLVFQ RKHYFPLVIL FCFILPTIIP VYFWKETAFI AFYVAGTFRY CFTLHATWCI
NSAAHYFGWK PYDTSVSAVE NVFTTVVAVG EGGHNFHHTF PQDYRASEYS LIYNWTRVLI
DTAAVLGLVY DRKTIADEFI SRQVANHGSE ESRKKSIM
