FADS1_HUMAN
ID FADS1_HUMAN Reviewed; 444 AA.
AC O60427; A8K0I7; B2RAI0; Q53GM5; Q8N3A6; Q8NCC7; Q8NCG0; Q96I39; Q96SV3;
AC Q96T10; Q9NRP8; Q9NYX1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Acyl-CoA (8-3)-desaturase {ECO:0000305};
DE EC=1.14.19.44 {ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175};
DE AltName: Full=Delta(5) fatty acid desaturase;
DE Short=D5D {ECO:0000250|UniProtKB:Q920L1};
DE Short=Delta(5) desaturase {ECO:0000250|UniProtKB:Q920L1};
DE Short=Delta-5 desaturase {ECO:0000303|PubMed:10601301, ECO:0000303|PubMed:10769175};
DE AltName: Full=Fatty acid desaturase 1 {ECO:0000303|PubMed:10860662};
GN Name=FADS1 {ECO:0000303|PubMed:10860662, ECO:0000312|HGNC:HGNC:3574};
GN Synonyms=FADSD5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RX PubMed=10601301; DOI=10.1074/jbc.274.52.37335;
RA Cho H.P., Nakamura M., Clarke S.D.;
RT "Cloning, expression, and fatty acid regulation of the human Delta-5
RT desaturase.";
RL J. Biol. Chem. 274:37335-37339(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=10769175; DOI=10.1042/bj3470719;
RA Leonard A.E., Kelder B., Bobik E.G., Chuang L.-T., Parker-Barnes J.M.,
RA Thurmond J.M., Kroeger P.E., Kopchick J.J., Huang Y.-S., Mukerji P.;
RT "cDNA cloning and characterization of human Delta5-desaturase involved in
RT the biosynthesis of arachidonic acid.";
RL Biochem. J. 347:719-724(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10860662; DOI=10.1006/geno.2000.6196;
RA Marquardt A., Stoehr H., White K., Weber B.H.;
RT "cDNA cloning, genomic structure, and chromosomal localization of three
RT members of the human fatty acid desaturase family.";
RL Genomics 66:175-183(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, Neuroblastoma, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney epithelium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-272.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP SUBCELLULAR LOCATION (ISOFORM 1), AND INDUCTION.
RX PubMed=22619218; DOI=10.1194/jlr.m025312;
RA Park W.J., Kothapalli K.S., Reardon H.T., Lawrence P., Qian S.B.,
RA Brenna J.T.;
RT "A novel FADS1 isoform potentiates FADS2-mediated production of eicosanoid
RT precursor fatty acids.";
RL J. Lipid Res. 53:1502-1512(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP ACETYLATION AT MET-1.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
CC -!- FUNCTION: [Isoform 1]: Acts as a front-end fatty acyl-coenzyme A (CoA)
CC desaturase that introduces a cis double bond at carbon 5 located
CC between a preexisting double bond and the carboxyl end of the fatty
CC acyl chain. Involved in biosynthesis of highly unsaturated fatty acids
CC (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic
CC acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3)
CC precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA)
CC (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate
CC arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3),
CC respectively (PubMed:10601301, PubMed:10769175). As a rate limiting
CC enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid
CC biosynthesis, controls the metabolism of inflammatory lipids like
CC prostaglandin E2, critical for efficient acute inflammatory response
CC and maintenance of epithelium homeostasis. Contributes to membrane
CC phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl
CC chain esterified into phospholipids. In particular, regulates
CC phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory
CC cytokine production in T-cells (By similarity). Also desaturates (11E)-
CC octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the
CC biohydrogenation pathway of LA (18:2n-6) (By similarity).
CC {ECO:0000250|UniProtKB:Q920L1, ECO:0000250|UniProtKB:Q920R3,
CC ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175}.
CC -!- FUNCTION: [Isoform 2]: Does not exhibit any catalytic activity toward
CC 20:3n-6, but it may enhance FADS2 activity.
CC {ECO:0000250|UniProtKB:A4UVI1}.
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:10601301, ECO:0000269|PubMed:10769175};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46425;
CC Evidence={ECO:0000305|PubMed:10601301};
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:10769175};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421;
CC Evidence={ECO:0000305|PubMed:10769175};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (5Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:46060, 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:85651; Evidence={ECO:0000250|UniProtKB:Q920R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46061;
CC Evidence={ECO:0000250|UniProtKB:Q920R3};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:A4UVI1}. Mitochondrion
CC {ECO:0000269|PubMed:22619218}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:A4UVI1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=FADS1CS;
CC IsoId=O60427-1; Sequence=Displayed;
CC Name=2; Synonyms=FADS1AT1;
CC IsoId=O60427-2; Sequence=VSP_047521;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in liver,
CC brain, adrenal gland and heart. Highly expressed in fetal liver and
CC brain. {ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175,
CC ECO:0000269|PubMed:10860662}.
CC -!- INDUCTION: Strongly down-regulated upon differentiation in a
CC neuroblastoma cell line (at protein level).
CC {ECO:0000269|PubMed:22619218}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11182.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11229.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK027427; BAB55103.1; -; mRNA.
DR EMBL; AK027522; BAB55173.1; -; mRNA.
DR EMBL; AK074754; BAC11182.1; ALT_INIT; mRNA.
DR EMBL; AK074819; BAC11229.1; ALT_INIT; mRNA.
DR EMBL; AK096275; BAG53244.1; -; mRNA.
DR EMBL; AK289552; BAF82241.1; -; mRNA.
DR EMBL; AK314199; BAG36877.1; -; mRNA.
DR EMBL; AC004770; AAC23397.1; -; Genomic_DNA.
DR EMBL; AP002380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF084558; AAG23120.1; -; mRNA.
DR EMBL; AL512760; CAC21679.1; -; mRNA.
DR EMBL; AL834479; CAD39138.1; -; mRNA.
DR EMBL; AK222906; BAD96626.1; -; mRNA.
DR EMBL; BC007846; AAH07846.1; -; mRNA.
DR EMBL; AF199596; AAF29378.1; -; mRNA.
DR EMBL; AF226273; AAF70457.1; -; mRNA.
DR RefSeq; NP_037534.3; NM_013402.4.
DR AlphaFoldDB; O60427; -.
DR SMR; O60427; -.
DR BioGRID; 110180; 88.
DR IntAct; O60427; 19.
DR MINT; O60427; -.
DR STRING; 9606.ENSP00000322229; -.
DR BindingDB; O60427; -.
DR ChEMBL; CHEMBL5840; -.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR DrugBank; DB11358; Evening primrose oil.
DR DrugBank; DB00159; Icosapent.
DR DrugBank; DB13168; Omega-6 fatty acids.
DR DrugBank; DB09328; Vayarin.
DR SwissLipids; SLP:000000368; -.
DR iPTMnet; O60427; -.
DR PhosphoSitePlus; O60427; -.
DR BioMuta; FADS1; -.
DR EPD; O60427; -.
DR jPOST; O60427; -.
DR MassIVE; O60427; -.
DR MaxQB; O60427; -.
DR PaxDb; O60427; -.
DR PeptideAtlas; O60427; -.
DR PRIDE; O60427; -.
DR ProteomicsDB; 1836; -.
DR ProteomicsDB; 49399; -. [O60427-1]
DR Antibodypedia; 21596; 276 antibodies from 36 providers.
DR DNASU; 3992; -.
DR Ensembl; ENST00000433932.5; ENSP00000405087.1; ENSG00000149485.19. [O60427-2]
DR Ensembl; ENST00000542506.5; ENSP00000441403.1; ENSG00000149485.19. [O60427-2]
DR GeneID; 3992; -.
DR KEGG; hsa:3992; -.
DR UCSC; uc010rln.2; human. [O60427-1]
DR CTD; 3992; -.
DR DisGeNET; 3992; -.
DR GeneCards; FADS1; -.
DR HGNC; HGNC:3574; FADS1.
DR HPA; ENSG00000149485; Low tissue specificity.
DR MIM; 606148; gene.
DR neXtProt; NX_O60427; -.
DR OpenTargets; ENSG00000149485; -.
DR PharmGKB; PA27973; -.
DR VEuPathDB; HostDB:ENSG00000149485; -.
DR eggNOG; KOG4232; Eukaryota.
DR GeneTree; ENSGT00950000182990; -.
DR HOGENOM; CLU_016265_0_0_1; -.
DR InParanoid; O60427; -.
DR OMA; MITFYIR; -.
DR OrthoDB; 1060606at2759; -.
DR PhylomeDB; O60427; -.
DR TreeFam; TF313604; -.
DR BioCyc; MetaCyc:HS07617-MON; -.
DR BRENDA; 1.14.19.30; 2681.
DR PathwayCommons; O60427; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR SignaLink; O60427; -.
DR SIGNOR; O60427; -.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 3992; 19 hits in 1083 CRISPR screens.
DR ChiTaRS; FADS1; human.
DR GeneWiki; FADS1; -.
DR GenomeRNAi; 3992; -.
DR Pharos; O60427; Tchem.
DR PRO; PR:O60427; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O60427; protein.
DR Bgee; ENSG00000149485; Expressed in upper leg skin and 203 other tissues.
DR ExpressionAtlas; O60427; baseline and differential.
DR Genevisible; O60427; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0062076; F:acyl-CoA delta5-desaturase activity; IDA:UniProtKB.
DR GO; GO:0000248; F:C-5 sterol desaturase activity; TAS:ProtInc.
DR GO; GO:0016213; F:linoleoyl-CoA desaturase activity; IDA:MGI.
DR GO; GO:0045485; F:omega-6 fatty acid desaturase activity; TAS:Reactome.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
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:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
DR GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0046456; P:icosanoid biosynthetic process; TAS:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; TAS:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
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; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Electron transport;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..444
FT /note="Acyl-CoA (8-3)-desaturase"
FT /id="PRO_0000307096"
FT TOPO_DOM 1..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..145
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..305
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..94
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 179..183
FT /note="Histidine box-1"
FT MOTIF 216..220
FT /note="Histidine box-2"
FT MOTIF 382..386
FT /note="Histidine box-3"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:25732826,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047521"
FT VARIANT 272
FT /note="P -> S (in dbSNP:rs17856235)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035340"
FT CONFLICT 6
FT /note="V -> L (in Ref. 7; AAF29378)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="E -> G (in Ref. 1; BAB55103)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="P -> L (in Ref. 7; AAF29378)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="F -> L (in Ref. 1; BAC11182)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="D -> E (in Ref. 1; BAC11182)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="D -> G (in Ref. 5; BAD96626)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="W -> R (in Ref. 1; BAB55173)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="N -> S (in Ref. 1; BAC11182)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="K -> N (in Ref. 7; AAF29378)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="F -> L (in Ref. 1; BAB55103)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="Q -> L (in Ref. 8; AAF70457)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="F -> S (in Ref. 1; BAC11229)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="H -> R (in Ref. 8; AAF70457)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="K -> E (in Ref. 1; BAC11229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 51964 MW; CC3C28D82AA49BF2 CRC64;
MAPDPVAAET AAQGPTPRYF TWDEVAQRSG CEERWLVIDR KVYNISEFTR RHPGGSRVIS
HYAGQDATDP FVAFHINKGL VKKYMNSLLI GELSPEQPSF EPTKNKELTD EFRELRATVE
RMGLMKANHV FFLLYLLHIL LLDGAAWLTL WVFGTSFLPF LLCAVLLSAV QAQAGWLQHD
FGHLSVFSTS KWNHLLHHFV IGHLKGAPAS WWNHMHFQHH AKPNCFRKDP DINMHPFFFA
LGKILSVELG KQKKKYMPYN HQHKYFFLIG PPALLPLYFQ WYIFYFVIQR KKWVDLAWMI
TFYVRFFLTY VPLLGLKAFL GLFFIVRFLE SNWFVWVTQM NHIPMHIDHD RNMDWVSTQL
QATCNVHKSA FNDWFSGHLN FQIEHHLFPT MPRHNYHKVA PLVQSLCAKH GIEYQSKPLL
SAFADIIHSL KESGQLWLDA YLHQ
