LOCUS       NP_062673                444 aa            linear   ROD 26-MAR-2025
DEFINITION  acyl-CoA 6-desaturase [Mus musculus].
ACCESSION   NP_062673
VERSION     NP_062673.1
DBSOURCE    REFSEQ: accession NM_019699.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Yi,Zhang., Feng,R., Li,H., Wu,W., Ma,W., Chen,X., Chen,J. and
            Liang,C.
  TITLE     CXCR4 influences PUFA desaturation and oxidative stress injury in
            experimental prostatitis mice by activating Fads2 via PPARgamma
  JOURNAL   Free Radic Biol Med 223, 237-249 (2024)
   PUBMED   39094710
  REMARK    GeneRIF: CXCR4 influences PUFA desaturation and oxidative stress
            injury in experimental prostatitis mice by activating Fads2 via
            PPARgamma.
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Lorito,N., Subbiani,A., Smiriglia,A., Bacci,M., Bonechi,F.,
            Tronci,L., Romano,E., Corrado,A., Longo,D.L., Iozzo,M.,
            Ippolito,L., Comito,G., Giannoni,E., Meattini,I., Avgustinova,A.,
            Chiarugi,P., Bachi,A. and Morandi,A.
  TITLE     FADS1/2 control lipid metabolism and ferroptosis susceptibility in
            triple-negative breast cancer
  JOURNAL   EMBO Mol Med 16 (7), 1533-1559 (2024)
   PUBMED   38926633
  REMARK    GeneRIF: FADS1/2 control lipid metabolism and ferroptosis
            susceptibility in triple-negative breast cancer.
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Liu,Y., Ni,F., Huang,J., Hu,Y., Wang,J., Wang,X., Du,X. and
            Jiang,H.
  TITLE     PPAR-alpha inhibits DHEA-induced ferroptosis in granulosa cells
            through upregulation of FADS2
  JOURNAL   Biochem Biophys Res Commun 715, 150005 (2024)
   PUBMED   38678785
  REMARK    GeneRIF: PPAR-alpha inhibits DHEA-induced ferroptosis in granulosa
            cells through upregulation of FADS2.
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Zhang,J., Ruiz,M., Bergh,P.O., Henricsson,M., Stojanovic,N.,
            Devkota,R., Henn,M., Bohlooly-Y,M., Hernandez-Hernandez,A.,
            Alsheimer,M., Boren,J., Pilon,M. and Shibuya,H.
  TITLE     Regulation of meiotic telomere dynamics through membrane fluidity
            promoted by AdipoR2-ELOVL2
  JOURNAL   Nat Commun 15 (1), 2315 (2024)
   PUBMED   38485951
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Yamamoto,H., Lee-Okada,H.C., Ikeda,M., Nakamura,T., Saito,T.,
            Takata,A., Yokomizo,T., Iwata,N., Kato,T. and Kasahara,T.
  TITLE     GWAS-identified bipolar disorder risk allele in the FADS1/2 gene
            region links mood episodes and unsaturated fatty acid metabolism in
            mutant mice
  JOURNAL   Mol Psychiatry 28 (7), 2848-2856 (2023)
   PUBMED   36806390
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Hargrave-Barnes,K.M., Azain,M.J. and Miner,J.L.
  TITLE     Conjugated linoleic acid-induced fat loss dependence on
            Delta6-desaturase or cyclooxygenase
  JOURNAL   Obesity (Silver Spring) 16 (10), 2245-2252 (2008)
   PUBMED   18719641
  REMARK    GeneRIF: Conjugated linoleic acid-induced fat loss was found to be
            dependent on delta6-desaturase activity.
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Devlin,A.M., Singh,R., Wade,R.E., Innis,S.M., Bottiglieri,T. and
            Lentz,S.R.
  TITLE     Hypermethylation of Fads2 and altered hepatic fatty acid and
            phospholipid metabolism in mice with hyperhomocysteinemia
  JOURNAL   J Biol Chem 282 (51), 37082-37090 (2007)
   PUBMED   17971455
  REMARK    GeneRIF: methylation silencing of liver Fads2 expression and
            changes in liver fatty acids may contribute to the pathology of
            hyperhomocysteinemia.
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Ferdinandusse,S., Denis,S., Mooijer,P.A., Zhang,Z., Reddy,J.K.,
            Spector,A.A. and Wanders,R.J.
  TITLE     Identification of the peroxisomal beta-oxidation enzymes involved
            in the biosynthesis of docosahexaenoic acid
  JOURNAL   J Lipid Res 42 (12), 1987-1995 (2001)
   PUBMED   11734571
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Marquardt,A., Stohr,H., White,K. and Weber,B.H.
  TITLE     cDNA cloning, genomic structure, and chromosomal localization of
            three members of the human fatty acid desaturase family
  JOURNAL   Genomics 66 (2), 175-183 (2000)
   PUBMED   10860662
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Cho,H.P., Nakamura,M.T. and Clarke,S.D.
  TITLE     Cloning, expression, and nutritional regulation of the mammalian
            Delta-6 desaturase
  JOURNAL   J Biol Chem 274 (1), 471-477 (1999)
   PUBMED   9867867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135670.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF126798.1, AK143524.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 6.36 cM"
     Protein         1..444
                     /product="acyl-CoA 6-desaturase"
                     /EC_number="1.14.19.3"
                     /note="D6D; delta(6) desaturase; delta(6) fatty acid
                     desaturase"
                     /calculated_mol_wt=52257
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     Region          20..435
                     /region_name="PLN03198"
                     /note="delta6-acyl-lipid desaturase; Provisional"
                     /db_xref="CDD:178739"
     Site            131..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     Site            153..173
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     Region          162..412
                     /region_name="Delta6-FADS-like"
                     /note="The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like
                     CD includes the integral-membrane enzymes: delta-4,
                     delta-5, delta-6, delta-8, delta-8-sphingolipid, and
                     delta-11 desaturases found in vertebrates, higher plants,
                     fungi, and bacteria. These desaturases...; cd03506"
                     /db_xref="CDD:239583"
     Site            order(180,184,217,220..221,382,385..386)
                     /site_type="other"
                     /note="putative di-iron ligands [ion binding]"
                     /db_xref="CDD:239583"
     Region          180..184
                     /region_name="Histidine box-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     Region          217..221
                     /region_name="Histidine box-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     Region          382..386
                     /region_name="Histidine box-3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z0R9.1)"
     CDS             1..444
                     /gene="Fads2"
                     /gene_synonym="2900042M13Rik; Fads2a; Fadsd2"
                     /coded_by="NM_019699.2:75..1409"
                     /db_xref="CCDS:CCDS29571.1"
                     /db_xref="GeneID:56473"
                     /db_xref="MGI:MGI:1930079"
ORIGIN      
        1 mgkggnqgeg sterqapmpt frweeiqkhn lrtdrwlvid rkvynvtkws qrhpgghrvi
       61 ghysgedatd afrafhldld fvgkflkpll igelapeeps ldrgkssqit edfralkkta
      121 edmnlfktnh lffflllshi ivmeslawfi lsyfgtgwip tlvtafvlat sqaqagwlqh
      181 dyghlsvykk siwnhvvhkf vighlkgasa nwwnhrhfqh hakpnifhkd pdikslhvfv
      241 lgewqpleyg kkklkylpyn hqheyfflig ppllipmyfq yqiimtmisr rdwvdlawai
      301 syymrffyty ipfygilgal vflnfirfle shwfvwvtqm nhlvmeidld hyrdwfssql
      361 aatcnveqsf fndwfsghln fqiehhlfpt mprhnlhkia plvkslcakh gieyqekpll
      421 ralidivssl kksgelwlda ylhk
//
