FAD3E_BRANA
ID FAD3E_BRANA Reviewed; 383 AA.
AC P48624; A0A078EMX0; P46311;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Acyl-lipid omega-3 desaturase (cytochrome b5), endoplasmic reticulum {ECO:0000303|PubMed:1455229};
DE EC=1.14.19.25 {ECO:0000269|PubMed:1455229};
DE AltName: Full=Omega-3 fatty acid desaturase 3, endoplasmic reticulum {ECO:0000303|PubMed:1455229};
GN Name=FAD3 {ECO:0000303|PubMed:1455229};
GN ORFNames=BnaC04g14820D {ECO:0000312|EMBL:CDY02019.1},
GN GSBRNA2T00113350001 {ECO:0000312|EMBL:CDY02019.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=1455229; DOI=10.1126/science.1455229;
RA Arondel V., Lemieux B., Hwang I., Gibson S., Goodman H.M., Somerville C.R.;
RT "Map-based cloning of a gene controlling omega-3 fatty acid desaturation in
RT Arabidopsis.";
RL Science 258:1353-1355(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed;
RX PubMed=8029334; DOI=10.1104/pp.103.2.467;
RA Yadav N.S., Wierzbicki A., Aegerter M., Caster C.S., Perez-Grau L.,
RA Kinney A.J., Hitz W.D., Booth J.R. Jr., Schweiger B., Stecca K.L.,
RA Allen S.M., Blackwell M., Reiter R.S., Carlson T.J., Russell S.H.,
RA Feldmann K.A., Pierce J., Browse J.;
RT "Cloning of higher plant omega-3 fatty acid desaturases.";
RL Plant Physiol. 103:467-476(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh;
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- FUNCTION: ER (microsomal) omega-3 fatty acid desaturase introduces the
CC third double bond in the biosynthesis of 18:3 fatty acids, important
CC constituents of plant membranes. It is thought to use cytochrome b5 as
CC an electron donor and to act on fatty acids esterified to
CC phosphatidylcholine and, possibly, other phospholipids.
CC {ECO:0000269|PubMed:1455229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (9Z,12Z,15Z)-octadecatrienoyl-
CC containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46404, 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:88351,
CC ChEBI:CHEBI:90078; EC=1.14.19.25;
CC Evidence={ECO:0000269|PubMed:1455229};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:1455229}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:1455229}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L01418; AAA32994.1; -; mRNA.
DR EMBL; L22962; AAA61775.1; -; mRNA.
DR EMBL; LK031931; CDY02019.1; -; Genomic_DNA.
DR PIR; A44227; A44227.
DR PIR; JQ2337; JQ2337.
DR RefSeq; NP_001302640.1; NM_001315711.1.
DR AlphaFoldDB; P48624; -.
DR STRING; 3708.P48624; -.
DR TCDB; 9.A.76.1.1; the omega3 fatty acid desaturase 3/putative transporter (fad3) family.
DR GeneID; 106377255; -.
DR KEGG; bna:106377255; -.
DR BRENDA; 1.14.19.25; 944.
DR UniPathway; UPA00658; -.
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:0102872; F:1-16:0-2-18:2-phosphatidylcholine desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102859; F:1-18:1-2-18:2-phosphatidylcholine desaturase activity (SN2-18:3 forming); IEA:UniProtKB-EC.
DR GO; GO:0102856; F:1-18:2-2-18:2-sn-glycerol-3-phosphocholine desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102862; F:1-18:2-2-18:2-sn-glycerol-3-phosphocholine desaturase activity (SN2-18:3 forming); IEA:UniProtKB-EC.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..383
FT /note="Acyl-lipid omega-3 desaturase (cytochrome b5),
FT endoplasmic reticulum"
FT /id="PRO_0000185412"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..102
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 134..138
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 301..305
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="V -> A (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 15..22
FT /note="SGARKEEG -> ER (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="T -> A (in Ref. 2; AAA61775 and 3; CDY02019)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> V (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="M -> V (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="L -> F (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="V -> A (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="SV -> TA (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="P -> S (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="I -> L (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="F -> Y (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="D -> G (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="E -> D (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..321
FT /note="RA -> KS (in Ref. 2; AAA61775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 43936 MW; DAD7C3A6FA12826A CRC64;
MVVAMDQRSN VNGDSGARKE EGFDPSAQPP FKIGDIRAAI PKHCWVKSPL RSMSYVTRDI
FAVAALAMAA VYFDSWFLWP LYWVAQGTLF WAIFVLGHDC GHGSFSDIPL LNSVVGHILH
SFILVPYHGW RISHRTHHQN HGHVENDESW VPLPEKLYKN LPHSTRMLRY TVPLPMLAYP
IYLWYRSPGK EGSHFNPYSS LFAPSERKLI ATSTTCWSIM LATLVYLSFL VDPVTVLKVY
GVPYIIFVMW LDAVTYLHHH GHDEKLPWYR GKEWSYLRGG LTTIDRDYGI FNNIHHDIGT
HVIHHLFPQI PHYHLVDATR AAKHVLGRYY REPKTSGAIP IHLVESLVAS IKKDHYVSDT
GDIVFYETDP DLYVYASDKS KIN
