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Fatty acid desaturase 2 (EC 1.14.19.-) (Delta(6) fatty acid desaturase) (D6D) (Delta(6) desaturase) (Delta-6 desaturase)

 FADS2_RAT               Reviewed;         444 AA.
Q9Z122; H2BF31;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 123.
RecName: Full=Fatty acid desaturase 2;
EC=1.14.19.-;
AltName: Full=Delta(6) fatty acid desaturase;
Short=D6D;
Short=Delta(6) desaturase;
Short=Delta-6 desaturase;
Name=Fads2; Synonyms=Fadsd6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=10049752; DOI=10.1006/bbrc.1999.0235;
Aki T., Shimada Y., Inagaki K., Higashimoto H., Kawamoto S.,
Shigeta S., Ono K., Suzuki O.;
"Molecular cloning and functional characterization of rat Delta-6
fatty acid desaturase.";
Biochem. Biophys. Res. Commun. 255:575-579(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=Dark agouti;
PubMed=22216341; DOI=10.1371/journal.pone.0029662;
Gregory M.K., Gibson R.A., Cook-Johnson R.J., Cleland L.G.,
James M.J.;
"Elongase reactions as control points in long-chain polyunsaturated
fatty acid synthesis.";
PLoS ONE 6:E29662-E29662(2011).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INDUCTION.
PubMed=12538079; DOI=10.1016/S0952-3278(02)00265-X;
Brenner R.R.;
"Hormonal modulation of delta-6 and delta-5 desaturases: case of
diabetes.";
Prostaglandins Leukot. Essent. Fatty Acids 68:151-162(2003).
[5]
TISSUE SPECIFICITY.
PubMed=5094766; DOI=10.1007/BF02531137;
Brenner R.R.;
"The desaturation step in the animal biosynthesis of polyunsaturated
fatty acids.";
Lipids 6:567-575(1971).
[6]
FUNCTION.
PubMed=14563830; DOI=10.1194/jlr.M300339-JLR200;
Guillou H., D'Andrea S., Rioux V., Barnouin R., Dalaine S.,
Pedrono F., Jan S., Legrand P.;
"Distinct roles of endoplasmic reticulum cytochrome b5 and fused
cytochrome b5-like domain for rat delta-6-desaturase activity.";
J. Lipid Res. 45:32-40(2004).
-!- FUNCTION: Component of a lipid metabolic pathway that catalyzes
biosynthesis of highly unsaturated fatty acids (HUFA) from
precursor essential polyunsaturated fatty acids (PUFA) linoleic
acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3).
Catalyzes the first and rate limiting step in this pathway which
is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-
linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3)
respectively and other desaturation steps. Highly unsaturated
fatty acids (HUFA) play pivotal roles in many biological
functions. {ECO:0000269|PubMed:10049752,
ECO:0000269|PubMed:14563830, ECO:0000269|PubMed:22216341}.
-!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid
biosynthesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- TISSUE SPECIFICITY: Highest activity is found in the liver and
adrenals followed by the testes and other organs, absent in
adipose tissue. {ECO:0000269|PubMed:5094766}.
-!- INDUCTION: Inhibited by a shortage of insulin and an increase of
glucagon. {ECO:0000269|PubMed:12538079}.
-!- DOMAIN: The histidine box domains may contain the active site
and/or be involved in metal ion binding.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
{ECO:0000305}.
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EMBL; AB021980; BAA75496.1; -; mRNA.
EMBL; HQ909027; AEX15918.1; -; mRNA.
EMBL; BC081776; AAH81776.1; -; mRNA.
PIR; JG0180; JG0180.
RefSeq; NP_112634.1; NM_031344.2.
UniGene; Rn.162483; -.
ProteinModelPortal; Q9Z122; -.
SMR; Q9Z122; -.
STRING; 10116.ENSRNOP00000027756; -.
BindingDB; Q9Z122; -.
ChEMBL; CHEMBL5088; -.
SwissLipids; SLP:000000272; -.
SwissLipids; SLP:000001190; -.
PaxDb; Q9Z122; -.
PRIDE; Q9Z122; -.
GeneID; 83512; -.
KEGG; rno:83512; -.
CTD; 9415; -.
RGD; 68339; Fads2.
eggNOG; KOG4232; Eukaryota.
eggNOG; ENOG410XVSZ; LUCA.
HOGENOM; HOG000012997; -.
HOVERGEN; HBG002839; -.
InParanoid; Q9Z122; -.
KO; K10226; -.
OrthoDB; EOG091G0E0W; -.
PhylomeDB; Q9Z122; -.
UniPathway; UPA00658; -.
PRO; PR:Q9Z122; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045485; F:omega-6 fatty acid desaturase activity; TAS:Reactome.
GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; TAS:RGD.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; TAS:RGD.
Gene3D; 3.10.120.10; -; 1.
InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
InterPro; IPR005804; FA_desaturase_dom.
InterPro; IPR012171; Fatty_acid_desaturase.
Pfam; PF00173; Cyt-b5; 1.
Pfam; PF00487; FA_desaturase; 1.
PIRSF; PIRSF015921; FA_sphinglp_des; 1.
SMART; SM01117; Cyt-b5; 1.
SUPFAM; SSF55856; SSF55856; 1.
PROSITE; PS50255; CYTOCHROME_B5_2; 1.
2: Evidence at transcript level;
Complete proteome; Electron transport; Endoplasmic reticulum;
Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 444 Fatty acid desaturase 2.
/FTId=PRO_0000307105.
TOPO_DOM 1 130 Cytoplasmic. {ECO:0000255}.
TRANSMEM 131 151 Helical. {ECO:0000255}.
TOPO_DOM 152 157 Lumenal. {ECO:0000255}.
TRANSMEM 158 178 Helical. {ECO:0000255}.
TOPO_DOM 179 264 Cytoplasmic. {ECO:0000255}.
TRANSMEM 265 285 Helical. {ECO:0000255}.
TOPO_DOM 286 305 Lumenal. {ECO:0000255}.
TRANSMEM 306 326 Helical. {ECO:0000255}.
TOPO_DOM 327 444 Cytoplasmic. {ECO:0000255}.
DOMAIN 18 95 Cytochrome b5 heme-binding.
{ECO:0000255|PROSITE-ProRule:PRU00279}.
MOTIF 180 184 Histidine box-1.
MOTIF 217 221 Histidine box-2.
MOTIF 382 386 Histidine box-3.
CONFLICT 101 101 L -> M (in Ref. 2; AEX15918).
{ECO:0000305}.
SEQUENCE 444 AA; 52380 MW; D9AE0C7AE499A1AE CRC64;
MGKGGNQGEG STELQAPMPT FRWEEIQKHN LRTDRWLVID RKVYNVTKWS QRHPGGHRVI
GHYSGEDATD AFRAFHLDLD FVGKFLKPLL IGELAPEEPS LDRGKSSQIT EDFRALKKTA
EDMNLFKTNH LFFFLLLSHI IVMESIAWFI LSYFGNGWIP TVITAFVLAT SQAQAGWLQH
DYGHLSVYKK SIWNHIVHKF VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDIKSLHVFV
LGEWQPLEYG KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIRR RDWVDLAWAI
SYYARFFYTY IPFYGILGAL VFLNFIRFLE SHWFVWVTQM NHIVMEIDLD HYRDWFSSQL
AATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA PLVKSLCAKH GIEYQEKPLL
RALLDIVSSL KKSGELWLDA YLHK


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