FADS2_HUMAN
ID FADS2_HUMAN Reviewed; 444 AA.
AC O95864; A8K2M6; B7Z634; Q6MZQ7; Q96H07; Q96SV8; Q9H3G3; Q9Y3X4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Acyl-CoA 6-desaturase {ECO:0000305|PubMed:12713571};
DE EC=1.14.19.3 {ECO:0000269|PubMed:12713571};
DE AltName: Full=Delta(6) fatty acid desaturase;
DE Short=D6D {ECO:0000250|UniProtKB:Q9Z0R9};
DE Short=Delta(6) desaturase;
DE Short=Delta-6 desaturase {ECO:0000303|PubMed:12713571, ECO:0000303|PubMed:9867867};
DE AltName: Full=Fatty acid desaturase 2 {ECO:0000303|PubMed:10860662};
GN Name=FADS2 {ECO:0000312|HGNC:HGNC:3575};
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), AND TISSUE SPECIFICITY.
RX PubMed=9867867; DOI=10.1074/jbc.274.1.471;
RA Cho H.P., Nakamura M.T., Clarke S.D.;
RT "Cloning, expression, and nutritional regulation of the mammalian Delta-6
RT desaturase.";
RL J. Biol. Chem. 274:471-477(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Mesothelium;
RA Zhang J.S.S., Reddel R.R.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 277-444 (ISOFORMS 1/2).
RC TISSUE=Tongue;
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).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-444 (ISOFORMS 1/2).
RC TISSUE=Uterus;
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 [10]
RP INDUCTION.
RX PubMed=12147235; DOI=10.1016/s0006-291x(02)00851-3;
RA Nara T.Y., He W.S., Tang C., Clarke S.D., Nakamura M.T.;
RT "The E-box like sterol regulatory element mediates the suppression of human
RT Delta-6 desaturase gene by highly unsaturated fatty acids.";
RL Biochem. Biophys. Res. Commun. 296:111-117(2002).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12713571; DOI=10.1046/j.1523-1747.2003.12123.x;
RA Ge L., Gordon J.S., Hsuan C., Stenn K., Prouty S.M.;
RT "Identification of the delta-6 desaturase of human sebaceous glands:
RT expression and enzyme activity.";
RL J. Invest. Dermatol. 120:707-714(2003).
RN [12]
RP ERRATUM OF PUBMED:12713571.
RA Ge L., Gordon J.S., Hsuan C., Stenn K., Prouty S.M.;
RL J. Invest. Dermatol. 121:434-434(2003).
RN [13]
RP INDUCTION.
RX PubMed=12562861; DOI=10.1194/jlr.m200195-jlr200;
RA Tang C., Cho H.P., Nakamura M.T., Clarke S.D.;
RT "Regulation of human delta-6 desaturase gene transcription: identification
RT of a functional direct repeat-1 element.";
RL J. Lipid Res. 44:686-695(2003).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=12851727;
RA Lane J., Mansel R.E., Jiang W.G.;
RT "Expression of human delta-6-desaturase is associated with aggressiveness
RT of human breast cancer.";
RL Int. J. Mol. Med. 12:253-257(2003).
RN [15]
RP IDENTIFICATION BY MASS 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in the biosynthesis of highly unsaturated fatty
CC acids (HUFA) from the essential polyunsaturated fatty acids (PUFA)
CC linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3)
CC precursors, acting as a fatty acyl-coenzyme A (CoA) desaturase that
CC introduces a cis double bond at carbon 6 of the fatty acyl chain.
CC Catalyzes the first and rate limiting step in this pathway which is the
CC desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate
CC (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively
CC (PubMed:12713571). Subsequently, in the biosynthetic pathway of HUFA n-
CC 3 series, it desaturates tetracosapentaenoate (24:5n-3) to
CC tetracosahexaenoate (24:6n-3), which is then converted to
CC docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system
CC function (By similarity). Desaturates hexadecanate (palmitate) to
CC produce 6Z-hexadecenoate (sapienate), a fatty acid unique to humans and
CC major component of human sebum, that has been implicated in the
CC development of acne and may have potent antibacterial activity
CC (PubMed:12713571). It can also desaturate (11E)-octadecenoate (trans-
CC vaccenoate, the predominant trans fatty acid in human milk) at carbon 6
CC generating (6Z,11E)-octadecadienoate (By similarity). In addition to
CC Delta-6 activity, this enzyme exhibits Delta-8 activity with slight
CC biases toward n-3 fatty acyl-CoA substrates (By similarity).
CC {ECO:0000250|UniProtKB:B8R1K0, ECO:0000250|UniProtKB:Q9Z122,
CC ECO:0000269|PubMed:12713571}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:47140, 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:57363,
CC ChEBI:CHEBI:57383; EC=1.14.19.3;
CC Evidence={ECO:0000269|PubMed:12713571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47141;
CC Evidence={ECO:0000269|PubMed:12713571};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:47144, 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:71489, ChEBI:CHEBI:74034; EC=1.14.19.3;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0R9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47145;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0R9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (6Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:37023, 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:74339; Evidence={ECO:0000269|PubMed:12713571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37024;
CC Evidence={ECO:0000269|PubMed:12713571};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z,18Z,21Z)-tetracosapentaenoyl-CoA + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z,18Z,21Z)-
CC tetracosahexaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36999, 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:74083,
CC ChEBI:CHEBI:74086; Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37000;
CC Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (6Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:46064, 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:85652; Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46065;
CC Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:39567, 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:74264,
CC ChEBI:CHEBI:76410; Evidence={ECO:0000250|UniProtKB:B8R1K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39568;
CC Evidence={ECO:0000250|UniProtKB:B8R1K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z,17Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:39571, 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:74265, ChEBI:CHEBI:74328;
CC Evidence={ECO:0000250|UniProtKB:B8R1K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39572;
CC Evidence={ECO:0000250|UniProtKB:B8R1K0};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305|PubMed:9867867}.
CC -!- INTERACTION:
CC O95864-3; Q15323: KRT31; NbExp=3; IntAct=EBI-12057609, EBI-948001;
CC O95864-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-12057609, EBI-10171697;
CC O95864-3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12057609, EBI-22310682;
CC O95864-3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-12057609, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95864-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95864-2; Sequence=VSP_028568;
CC Name=3;
CC IsoId=O95864-3; Sequence=VSP_028569;
CC Name=4;
CC IsoId=O95864-4; Sequence=VSP_054809;
CC -!- TISSUE SPECIFICITY: Expressed in a wide array of tissues, highest
CC expression is found in liver followed by brain, lung, heart, and
CC retina. A lower level is found in breast tumor when compared with
CC normal tissues; lowest levels were found in patients with poor
CC prognostic index. {ECO:0000269|PubMed:10860662,
CC ECO:0000269|PubMed:12851727, ECO:0000269|PubMed:9867867}.
CC -!- DEVELOPMENTAL STAGE: Found in fetal heart.
CC -!- INDUCTION: Repressed by dietary highly unsaturated fatty acids.
CC {ECO:0000269|PubMed:12147235, ECO:0000269|PubMed:12562861}.
CC -!- DOMAIN: The protein sequence includes a number of characteristic
CC features of microsomal fatty acid desaturases including the three
CC histidine boxes HXXXH, HXXHH, and QXXHH (these domains may contain the
CC active site and/or be involved in metal ion binding), and the N-
CC terminal cytochrome b5 domain containing the heme-binding motif, HPGG,
CC similar to that of other fatty acid desaturases.
CC {ECO:0000303|PubMed:9867867}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF126799; AAD20018.1; -; mRNA.
DR EMBL; AF084559; AAG23121.1; -; mRNA.
DR EMBL; AF108658; AAG43192.1; -; mRNA.
DR EMBL; AK027513; BAB55167.1; -; mRNA.
DR EMBL; AK290291; BAF82980.1; -; mRNA.
DR EMBL; AK299762; BAH13120.1; -; mRNA.
DR EMBL; AK074939; BAC11305.1; -; mRNA.
DR EMBL; AP002380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73975.1; -; Genomic_DNA.
DR EMBL; BC009011; AAH09011.1; -; mRNA.
DR EMBL; AL050118; CAB43280.1; -; mRNA.
DR EMBL; BX640945; CAE45971.1; -; mRNA.
DR CCDS; CCDS60807.1; -. [O95864-2]
DR CCDS; CCDS60808.1; -. [O95864-4]
DR CCDS; CCDS8012.1; -. [O95864-1]
DR PIR; T13155; T13155.
DR RefSeq; NP_001268430.1; NM_001281501.1. [O95864-2]
DR RefSeq; NP_001268431.1; NM_001281502.1. [O95864-4]
DR RefSeq; NP_004256.1; NM_004265.3. [O95864-1]
DR AlphaFoldDB; O95864; -.
DR SMR; O95864; -.
DR BioGRID; 114810; 66.
DR IntAct; O95864; 25.
DR MINT; O95864; -.
DR STRING; 9606.ENSP00000278840; -.
DR BindingDB; O95864; -.
DR ChEMBL; CHEMBL6097; -.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR DrugBank; DB11358; Evening primrose oil.
DR DrugBank; DB13168; Omega-6 fatty acids.
DR SwissLipids; SLP:000000275; -.
DR iPTMnet; O95864; -.
DR PhosphoSitePlus; O95864; -.
DR SwissPalm; O95864; -.
DR BioMuta; FADS2; -.
DR EPD; O95864; -.
DR jPOST; O95864; -.
DR MassIVE; O95864; -.
DR MaxQB; O95864; -.
DR PaxDb; O95864; -.
DR PeptideAtlas; O95864; -.
DR PRIDE; O95864; -.
DR ProteomicsDB; 51097; -. [O95864-1]
DR ProteomicsDB; 51098; -. [O95864-2]
DR ProteomicsDB; 51099; -. [O95864-3]
DR ProteomicsDB; 6739; -.
DR Antibodypedia; 1645; 186 antibodies from 25 providers.
DR DNASU; 9415; -.
DR Ensembl; ENST00000257261.10; ENSP00000257261.6; ENSG00000134824.14. [O95864-2]
DR Ensembl; ENST00000278840.9; ENSP00000278840.4; ENSG00000134824.14. [O95864-1]
DR Ensembl; ENST00000521849.5; ENSP00000431091.1; ENSG00000134824.14. [O95864-3]
DR Ensembl; ENST00000522056.5; ENSP00000429500.1; ENSG00000134824.14. [O95864-4]
DR GeneID; 9415; -.
DR KEGG; hsa:9415; -.
DR MANE-Select; ENST00000278840.9; ENSP00000278840.4; NM_004265.4; NP_004256.1.
DR UCSC; uc001nsj.4; human. [O95864-1]
DR CTD; 9415; -.
DR DisGeNET; 9415; -.
DR GeneCards; FADS2; -.
DR HGNC; HGNC:3575; FADS2.
DR HPA; ENSG00000134824; Tissue enhanced (adrenal).
DR MIM; 606149; gene.
DR neXtProt; NX_O95864; -.
DR OpenTargets; ENSG00000134824; -.
DR PharmGKB; PA27974; -.
DR VEuPathDB; HostDB:ENSG00000134824; -.
DR eggNOG; KOG4232; Eukaryota.
DR GeneTree; ENSGT00950000182990; -.
DR HOGENOM; CLU_016265_0_0_1; -.
DR InParanoid; O95864; -.
DR OMA; QWWKNKH; -.
DR OrthoDB; 1060606at2759; -.
DR PhylomeDB; O95864; -.
DR TreeFam; TF313604; -.
DR BioCyc; MetaCyc:HS05918-MON; -.
DR BRENDA; 1.14.19.3; 2681.
DR PathwayCommons; O95864; -.
DR Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR SignaLink; O95864; -.
DR SIGNOR; O95864; -.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 9415; 30 hits in 1080 CRISPR screens.
DR ChiTaRS; FADS2; human.
DR GeneWiki; FADS2; -.
DR GenomeRNAi; 9415; -.
DR Pharos; O95864; Tbio.
DR PRO; PR:O95864; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O95864; protein.
DR Bgee; ENSG00000134824; Expressed in right adrenal gland cortex and 147 other tissues.
DR ExpressionAtlas; O95864; baseline and differential.
DR Genevisible; O95864; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016213; F:linoleoyl-CoA desaturase activity; TAS:Reactome.
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:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:Ensembl.
DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
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:0006636; P:unsaturated fatty acid biosynthetic process; TAS:ProtInc.
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 Alternative splicing; Electron transport; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..444
FT /note="Acyl-CoA 6-desaturase"
FT /id="PRO_0000307101"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..157
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..305
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 18..95
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 180..184
FT /note="Histidine box-1"
FT MOTIF 217..221
FT /note="Histidine box-2"
FT MOTIF 382..386
FT /note="Histidine box-3"
FT VAR_SEQ 1..69
FT /note="MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQ
FT HPGGQRVIGHYAGEDAT -> MHGREAGPFVCVCVLLASIPTPQTPLLQASLPPFHPAS
FT AGHPITGQQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_028568"
FT VAR_SEQ 1..69
FT /note="MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQ
FT HPGGQRVIGHYAGEDAT -> MTREPPGCRRVNSLMLYTLRSITSHRSSHPERWATSSQ
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054809"
FT VAR_SEQ 386..444
FT /note="HLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLW
FT LDAYLHK -> Q (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028569"
FT CONFLICT 134..137
FT /note="LLLL -> RTRG (in Ref. 9; CAB43280)"
FT /evidence="ECO:0000305"
FT CONFLICT 380..381
FT /note="NF -> SL (in Ref. 4; BAB55167)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..431
FT /note="SLK -> DLM (in Ref. 9; CAB43280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 52259 MW; F65CE58076961A7A CRC64;
MGKGGNQGEG AAEREVSVPT FSWEEIQKHN LRTDRWLVID RKVYNITKWS IQHPGGQRVI
GHYAGEDATD AFRAFHPDLE FVGKFLKPLL IGELAPEEPS QDHGKNSKIT EDFRALRKTA
EDMNLFKTNH VFFLLLLAHI IALESIAWFT VFYFGNGWIP TLITAFVLAT SQAQAGWLQH
DYGHLSVYRK PKWNHLVHKF VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDVNMLHVFV
LGEWQPIEYG KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIVH KNWVDLAWAV
SYYIRFFITY IPFYGILGAL LFLNFIRFLE SHWFVWVTQM NHIVMEIDQE AYRDWFSSQL
TATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA PLVKSLCAKH GIEYQEKPLL
RALLDIIRSL KKSGKLWLDA YLHK
