ID   FAD2_VERFO              Reviewed;         383 AA.
AC   Q8GZC3;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Delta(12)-fatty-acid desaturase FAD2 {ECO:0000303|PubMed:12481086};
DE            EC=1.14.19.6 {ECO:0000269|PubMed:12481086};
GN   Name=FAD2 {ECO:0000303|PubMed:12481086};
OS   Vernicia fordii (Tung) (Aleurites fordii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Aleuritideae;
OC   Vernicia.
OX   NCBI_TaxID=73154 {ECO:0000312|EMBL:AAN87573.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=12481086; DOI=10.1104/pp.102.010835;
RA   Dyer J.M., Chapital D.C., Kuan J.C., Mullen R.T., Turner C., McKeon T.A.,
RA   Pepperman A.B.;
RT   "Molecular analysis of a bifunctional fatty acid conjugase/desaturase from
RT   tung. Implications for the evolution of plant fatty acid diversity.";
RL   Plant Physiol. 130:2027-2038(2002).
CC   -!- FUNCTION: Catalyzes the desaturation of oleic acid (18:1(9Z)) to
CC       linoleic acid (18:2(9Z,12Z)). {ECO:0000269|PubMed:12481086}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:25856, 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:57383,
CC         ChEBI:CHEBI:57387; EC=1.14.19.6;
CC         Evidence={ECO:0000269|PubMed:12481086};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:45096, 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:61540,
CC         ChEBI:CHEBI:76552; EC=1.14.19.6;
CC         Evidence={ECO:0000269|PubMed:12481086};
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12481086}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and seeds.
CC       {ECO:0000269|PubMed:12481086}.
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}.
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DR   EMBL; AF525534; AAN87573.1; -; mRNA.
DR   AlphaFoldDB; Q8GZC3; -.
DR   BRENDA; 1.14.19.34; 9082.
DR   BRENDA; 1.14.19.6; 9082.
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:0102985; F:delta12-fatty-acid desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102987; F:palmitoleic acid delta 12 desaturase activity; IEA:RHEA.
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="Delta(12)-fatty-acid desaturase FAD2"
FT                   /id="PRO_0000434404"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           105..109
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           141..145
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           315..319
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   383 AA;  44152 MW;  F5D06112C313B3CB CRC64;
     MGAGGRMSVP PPPKKLESEV LKRVPHSKPP FTLGQLKKAI PPHCFQRSVL RSFSYVVYDL
     TVAFIFYYIA TNYFHLLPQP LSYVAWPIYW ALQGCVLTGV WVIAHECGHH AFSDYQLLDD
     IVGLVLHSCL LVPYFSWKHS HRRHHSNTAS LERDEVFVPK KKSSIRWFSK YLNNPPGRLF
     TLTITLTLGW PLYLAFNVSG RPYDRFACHY DPYGPIYTDR ERTEIYISDA GVLAVTFGLY
     RLAAAKGLAW VICVYGVPLL IVNAFLVMIT YLQHTHPSIP HYDSSEWDWL RGALATVDRD
     YGILNKVFHN ITDTHVAHHL FSTMPHYHAM EATKAIKPIL GEYYQFDGTP FYKAMWREAK
     ECIYVEADDG DESKGVYWYN KKF