FADS3_MOUSE
ID FADS3_MOUSE Reviewed; 449 AA.
AC Q9JJE7; Q7TND7; Q8C4Y5; Q8CDZ4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Fatty acid desaturase 3 {ECO:0000250|UniProtKB:Q8K1P9};
DE EC=1.14.19.- {ECO:0000250|UniProtKB:Q8K1P9};
DE AltName: Full=Delta(13) fatty acid desaturase {ECO:0000250|UniProtKB:Q8K1P9};
DE Short=Delta(13) desaturase {ECO:0000250|UniProtKB:Q8K1P9};
GN Name=Fads3 {ECO:0000303|PubMed:19752397, ECO:0000312|MGI:MGI:1928740};
GN ORFNames=MNCb-0629;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-449.
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=19752397; DOI=10.1194/jlr.m000588;
RA Pedrono F., Blanchard H., Kloareg M., D'andrea S., Daval S., Rioux V.,
RA Legrand P.;
RT "The fatty acid desaturase 3 gene encodes for different FADS3 protein
RT isoforms in mammalian tissues.";
RL J. Lipid Res. 51:472-479(2010).
CC -!- FUNCTION: Mammals have different sphingoid bases that differ in their
CC length and/or pattern of desaturation and hydroxyl groups. The
CC predominant sphingoid base in mammalian ceramides is sphing-4-enine
CC (sphingosine or SPH) which has a trans desaturation at carbon 4. FADS3
CC is a ceramide desaturase that introduces a cis double bond between
CC carbon 14 and carbon 15 of the SPH-containing ceramides, producing
CC sphinga-4,14-dienine-containing ceramides (SPD ceramides). SPD
CC ceramides occur widely in mammalian tissues and cells. Due to their
CC unusual structure containing a cis double bond, SPD ceramides may have
CC an opposite, negative role in lipid microdomain formation relative to
CC conventional ceramides (By similarity). FADS3 also acts as a methyl-end
CC fatty acyl coenzyme A (CoA) desaturase that introduces a cis double
CC bond between the preexisting double bond and the terminal methyl group
CC of the fatty acyl chain. Desaturates (11E)-octadecenoate (trans-
CC vaccenoate, the predominant trans fatty acid in human milk) at carbon
CC 13 to generate (11E,13Z)-octadecadienoate (also known as conjugated
CC linoleic acid 11E,13Z-CLA) (By similarity).
CC {ECO:0000250|UniProtKB:Q8K1P9, ECO:0000250|UniProtKB:Q9Y5Q0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = an N-acyl-sphinga-4E,14Z-dienine + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:63928, 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:52639,
CC ChEBI:CHEBI:139573; Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63929;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N-(hexanoyl)sphing-4-enine
CC + O2 = 2 Fe(III)-[cytochrome b5] + 2 H2O + N-hexanoyl-sphinga-4E,14Z-
CC dienine; Xref=Rhea:RHEA:63940, 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:63867,
CC ChEBI:CHEBI:149631; Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63941;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (11E,13Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:46056, 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:85650; Evidence={ECO:0000250|UniProtKB:Q8K1P9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46057;
CC Evidence={ECO:0000250|UniProtKB:Q8K1P9};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q8K1P9}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q9Y5Q0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y5Q0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney (at protein
CC level). {ECO:0000269|PubMed:19752397}.
CC -!- DOMAIN: The protein sequence includes a number of characteristic
CC features of microsomal fatty acid desaturases including the three
CC histidine boxes (these domains may contain the active site and/or be
CC involved in metal ion binding), and the N-terminal cytochrome b5 domain
CC containing the heme-binding motif, HPGG, similar to that of other fatty
CC acid desaturases. {ECO:0000250|UniProtKB:Q9Y5Q0}.
CC -!- MISCELLANEOUS: Two potential isoforms are detected in various tissues.
CC A 75 kDa isoform is expressed in lung. A 37 kDa isoform is expressed in
CC lung, liver and kidney. {ECO:0000269|PubMed:19752397}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB041560; BAA95044.1; -; mRNA.
DR EMBL; AK080414; BAC37908.1; -; mRNA.
DR EMBL; AK029318; BAC26393.1; -; mRNA.
DR EMBL; BC055950; AAH55950.1; -; mRNA.
DR CCDS; CCDS29570.1; -.
DR RefSeq; NP_068690.3; NM_021890.3.
DR AlphaFoldDB; Q9JJE7; -.
DR SMR; Q9JJE7; -.
DR BioGRID; 208598; 3.
DR IntAct; Q9JJE7; 1.
DR STRING; 10090.ENSMUSP00000111659; -.
DR iPTMnet; Q9JJE7; -.
DR PhosphoSitePlus; Q9JJE7; -.
DR SwissPalm; Q9JJE7; -.
DR jPOST; Q9JJE7; -.
DR MaxQB; Q9JJE7; -.
DR PaxDb; Q9JJE7; -.
DR PRIDE; Q9JJE7; -.
DR ProteomicsDB; 275849; -.
DR Antibodypedia; 28347; 157 antibodies from 22 providers.
DR DNASU; 60527; -.
DR Ensembl; ENSMUST00000115995; ENSMUSP00000111659; ENSMUSG00000024664.
DR GeneID; 60527; -.
DR KEGG; mmu:60527; -.
DR UCSC; uc008goz.1; mouse.
DR CTD; 3995; -.
DR MGI; MGI:1928740; Fads3.
DR VEuPathDB; HostDB:ENSMUSG00000024664; -.
DR eggNOG; KOG4232; Eukaryota.
DR GeneTree; ENSGT00950000182990; -.
DR HOGENOM; CLU_016265_0_1_1; -.
DR InParanoid; Q9JJE7; -.
DR OMA; WMHEAGH; -.
DR OrthoDB; 1060606at2759; -.
DR PhylomeDB; Q9JJE7; -.
DR TreeFam; TF313604; -.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 60527; 3 hits in 77 CRISPR screens.
DR PRO; PR:Q9JJE7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9JJE7; protein.
DR Bgee; ENSMUSG00000024664; Expressed in vestibular membrane of cochlear duct and 197 other tissues.
DR ExpressionAtlas; Q9JJE7; baseline and differential.
DR Genevisible; Q9JJE7; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..449
FT /note="Fatty acid desaturase 3"
FT /id="PRO_0000307109"
FT TOPO_DOM 1..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..163
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..310
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..101
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..190
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Q0"
FT MOTIF 223..227
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Q0"
FT MOTIF 387..391
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Q0"
FT CONFLICT 136
FT /note="T -> S (in Ref. 2; BAC37908)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="Q -> R (in Ref. 1; BAA95044)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> P (in Ref. 2; BAC26393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 51469 MW; 0E0B74EC8C9E5199 CRC64;
MGGVGEPGGG PGPREGPAPL GAPLPIFRWE QIRQHDLPGD KWLVIERRVY DISRWAQRHP
GGSRLIGHHG AEDATDAFHA FHQDLHFVRK FLKPLLIGEL APEEPSQDGA QNAQLIEDFR
ALRQAAEDMK LFEADTTFFA LLLGHILAME LLAWLIIYLL GPGWVSSILA ALILAISQAQ
CWCLQHDLGH ASIFTKSRWN HVAQQFVMGQ LKGFSAHWWN FRHFQHHAKP NIFHKDPDVT
VAPVFLLGES SVEYGKKKRR YLPYNHQHLY FFLIGPPLLT LVNFEVENLA YMLVCMQWTD
LLWAASFYSR FFLSYSPFYG ATGTLLLFVA VRVLESHWFV WITQMNHIPK EIGHEKHRDW
ASSQLAATCN VEPSLFIDWF SGHLNFQIEH HLFPTMPRHN YRRVAPLVKA FCAKHGLHYE
VKPFLTALVD IIGSLKKSGD IWLDAYLHQ
