ID   FAD12_PUNGR             Reviewed;         387 AA.
AC   Q84VT2; Q84UB7;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 2.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Delta(12)-acyl-lipid-desaturase {ECO:0000303|PubMed:12354116};
DE            EC=1.14.19.- {ECO:0000305};
DE   AltName: Full=Delta(12)-oleate desaturase {ECO:0000303|PubMed:12464604};
DE            Short=PgFAD2 {ECO:0000303|PubMed:12464604};
GN   Name=FAD12 {ECO:0000303|PubMed:12354116};
GN   Synonyms=FAD2 {ECO:0000303|PubMed:12464604};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000312|EMBL:CAD24671.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=12354116; DOI=10.1046/j.1432-1033.2002.03184.x;
RA   Hornung E., Pernstich C., Feussner I.;
RT   "Formation of conjugated Delta11Delta13-double bonds by Delta12-linoleic
RT   acid (1,4)-acyl-lipid-desaturase in pomegranate seeds.";
RL   Eur. J. Biochem. 269:4852-4859(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=12464604; DOI=10.1074/jbc.m210748200;
RA   Iwabuchi M., Kohno-Murase J., Imamura J.;
RT   "Delta 12-oleate desaturase-related enzymes associated with formation of
RT   conjugated trans-delta 11, cis-delta 13 double bonds.";
RL   J. Biol. Chem. 278:4603-4610(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=25000918; DOI=10.1007/s00425-014-2109-z;
RA   Mietkiewska E., Miles R., Wickramarathna A., Sahibollah A.F., Greer M.S.,
RA   Chen G., Weselake R.J.;
RT   "Combined transgenic expression of Punica granatum conjugase (FADX) and
RT   FAD2 desaturase in high linoleic acid Arabidopsis thaliana mutant leads to
RT   increased accumulation of punicic acid.";
RL   Planta 240:575-583(2014).
CC   -!- FUNCTION: Delta(12)-fatty acid desaturase producing in a heterologous
CC       system linoleic acid (18:2(9Z,12Z)) and to a lower extent
CC       hexadecadienoic acid (16:2(9Z,12Z)). {ECO:0000269|PubMed:12354116,
CC       ECO:0000269|PubMed:12464604, ECO:0000269|PubMed:25000918}.
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {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; AJ437139; CAD24671.1; -; mRNA.
DR   EMBL; AY178447; AAO37754.1; -; mRNA.
DR   AlphaFoldDB; Q84VT2; -.
DR   BRENDA; 1.14.19.34; 14164.
DR   UniPathway; UPA00658; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..387
FT                   /note="Delta(12)-acyl-lipid-desaturase"
FT                   /id="PRO_0000434637"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           109..113
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000250|UniProtKB:P48631"
FT   MOTIF           145..149
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000250|UniProtKB:P48631"
FT   MOTIF           319..323
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000250|UniProtKB:P48631"
FT   CONFLICT        205
FT                   /note="W -> R (in Ref. 2; AAO37754)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   387 AA;  44280 MW;  9C7569242930E5E1 CRC64;
     MGAGGRMTVP NKWEGEGDEK SQKPVQRVPS AKPPFTLSEI KKAIPPHCFK RSLLKSFSYV
     LYDLTLVAIF YYVATTYIDA LPGPLRYAAW PVYWALQGCV LTGVWVIAHE CGHHAFSDYQ
     WVDDCVGLVL HSALLVPYFS WKYSHRRHHS NTGSLERDEV FVPKPKSKMP WFSKYLNNPP
     GRVMTLIVTL TLGWPLYLAL NVSGWPYDRF ACHFDPYGPI YTDRERLQIY ISDVGIMAAT
     YTLYKIAAAR GLAWLVCVYG VPLLIVNAFL VTITYLQHTH PALPHYDSSE WDWLRGALAT
     ADRDYGILNK VFHNITDTHV AHHLFSTMPH YHAMEATKAI KPILGDYYQF DGTPVYKAMW
     REARECLYVE PDDGANSKGV FWYKKNL