FAD1_SIGCA
ID FAD1_SIGCA Reviewed; 443 AA.
AC B2KKL4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Acyl-CoA Delta-6 desaturase {ECO:0000305|PubMed:20826444};
DE Short=Delta-6 desaturase {ECO:0000303|PubMed:18639644};
DE EC=1.14.19.3 {ECO:0000269|PubMed:20826444};
DE EC=1.14.19.44 {ECO:0000269|PubMed:20826444};
DE AltName: Full=Delta(5)/Delta(6) fatty acid desaturase {ECO:0000305|PubMed:20826444};
DE Short=D5D/D6D fatty acid desaturase {ECO:0000305|PubMed:20826444};
DE Short=Delta-5/Delta-6 fatty acid desaturase {ECO:0000305|PubMed:20826444};
DE AltName: Full=FAD1 {ECO:0000303|PubMed:20826444};
DE AltName: Full=Linoleoyl-CoA desaturase {ECO:0000303|PubMed:18639644};
GN Name=fad1 {ECO:0000303|PubMed:20826444};
OS Siganus canaliculatus (White-spotted spinefoot) (Chaetodon canaliculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Siganidae; Siganus.
OX NCBI_TaxID=75042;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=18639644; DOI=10.1016/j.cbpb.2008.06.013;
RA Li Y.Y., Hu C.B., Zheng Y.J., Xia X.A., Xu W.J., Wang S.Q., Chen W.Z.,
RA Sun Z.W., Huang J.H.;
RT "The effects of dietary fatty acids on liver fatty acid composition and
RT Delta(6)-desaturase expression differ with ambient salinities in Siganus
RT canaliculatus.";
RL Comp. Biochem. Physiol. 151:183-190(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20826444; DOI=10.1073/pnas.1008429107;
RA Li Y., Monroig O., Zhang L., Wang S., Zheng X., Dick J.R., You C.,
RA Tocher D.R.;
RT "Vertebrate fatty acyl desaturase with Delta4 activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16840-16845(2010).
CC -!- FUNCTION: Fatty acid desaturase with bifunctional delta-5 and delta-6
CC activities. Component of a lipid metabolic pathway that catalyzes the
CC biosynthesis of polyunsaturated fatty acids (PUFA) with preference
CC toward n-3 substrates and Delta(6)function.
CC {ECO:0000269|PubMed:20826444}.
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:20826444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47141;
CC Evidence={ECO:0000269|PubMed:20826444};
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:0000269|PubMed:20826444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47145;
CC Evidence={ECO:0000269|PubMed:20826444};
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:20826444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421;
CC Evidence={ECO:0000269|PubMed:20826444};
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:20826444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46425;
CC Evidence={ECO:0000269|PubMed:20826444};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305|PubMed:20826444}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: High expression in the brain and liver and weak
CC expression in the gill. {ECO:0000269|PubMed:18639644}.
CC -!- DOMAIN: The protein sequence includes a number of characteristic
CC features of microsomal fatty acid desaturases including three histidine
CC boxes and an N-terminal cytochrome b5 domain containing the heme-
CC binding motif. {ECO:0000305|PubMed:20826444}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; EF424276; ABR12315.2; -; mRNA.
DR AlphaFoldDB; B2KKL4; -.
DR SMR; B2KKL4; -.
DR SwissLipids; SLP:000000443; -.
DR BRENDA; 1.14.19.3; 10882.
DR UniPathway; UPA00658; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0062076; F:acyl-CoA delta5-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0016213; F:linoleoyl-CoA desaturase activity; IEA:UniProtKB-EC.
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 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 Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..443
FT /note="Acyl-CoA Delta-6 desaturase"
FT /id="PRO_0000451734"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 17..94
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 443 AA; 51872 MW; E6705508FC451C04 CRC64;
MGGGGQPRES GEPGSSPAVY TWEEVQHHSS RNDQWLVIDR KVYNISQWAK RHPGGYRVIG
HYAGEDATEA FTAFHPDLKF VQKFLKPLLI GELAATEPSQ DRNKNAALIQ DFHTLRQQAE
SEGLFQARPL FFLLHLGHIL LLEALALLMV WHWGTGWLQT LLCAVMLATA QSQAGWLQHD
FGHLSVFKKS RWNHLVHHFV IGHLKGASAN WWNHRHFQHH AKPNIFKKDP DINMVDLFVL
GETQPVEYGV KKIKLMPYNH QHQYFHLIGP PLLIPVFFHY QLLKIMISHR YWLDLVWCLS
FYLRYMCCYV PVYGLFGSVV LIVFTRFLES HWFVWVTQMN HLPMDINYEN HNDWLSMQLQ
ATCNVEQSLF NDWFSGHLNF QIEHHLFPTM PRHNYHLVVP RVRALCEKHE IPYQVKTLPQ
AFADIIRSLK NSGELWLDAY LHK
