FAD2B_CALOF
ID FAD2B_CALOF Reviewed; 377 AA.
AC Q9SCG2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Delta(12) fatty acid desaturase DES8.11;
DE EC=1.14.19.- {ECO:0000305};
DE AltName: Full=(8,11)-linoleoyl desaturase {ECO:0000303|PubMed:10622705};
DE Short=CoDes8,11 {ECO:0000303|PubMed:10622705};
GN Name=DES8.11 {ECO:0000303|PubMed:10622705};
OS Calendula officinalis (Pot marigold).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Calenduleae;
OC Calendula.
OX NCBI_TaxID=41496 {ECO:0000312|EMBL:CAB64256.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Seed;
RX PubMed=10622705; DOI=10.1016/s0014-5793(99)01541-0;
RA Fritsche K., Hornung E., Peitzsch N., Renz A., Feussner I.;
RT "Isolation and characterization of a calendic acid producing (8,11)-
RT linoleoyl desaturase.";
RL FEBS Lett. 462:249-253(1999).
CC -!- FUNCTION: Converts linoleic acid into a conjugated octadecatrienoic
CC acid, probably calendic acid. {ECO:0000269|PubMed:10622705}.
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}.
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DR EMBL; AJ245938; CAB64256.1; -; mRNA.
DR AlphaFoldDB; Q9SCG2; -.
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..377
FT /note="Delta(12) fatty acid desaturase DES8.11"
FT /id="PRO_0000435421"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 100..104
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 136..140
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 310..314
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 43615 MW; 1CBF7650955F26BF CRC64;
MGAGGRMSDP SEGKNILERV PVDPPFTLSD LKKAIPTHCF ERSVIRSSYY VVHDLIVAYV
FYYLANTYIP LIPTPLAYLA WPVYWFCQAS ILTGLWVIGH ECGHHAFSDY QLIDDIVGFV
LHSALLTPYF SWKYSHRNHH ANTNSLDNDE VYIPKRKSKV KIYSKLLNNP PGRVFTLVFR
LTLGFPLYLL TNISGKKYGR FANHFDPMSP IFNDRERVQV LLSDFGLLAV FYAIKLLVAA
KGAAWVINMY AIPVLGVSVF FVLITYLHHT HLSLPHYDST EWNWIKGALS TIDRDFGFLN
RVFHDVTHTH VLHHLISYIP HYHAKEARDA IKPVLGEYYK IDRTPIFKAM YREAKECIYI
EPDEDSEHKG VFWYHKM
