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FAD2_CALOF
ID   FAD2_CALOF              Reviewed;         383 AA.
AC   Q9AT72;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Delta(12) fatty acid desaturase FAD2 {ECO:0000303|PubMed:11161042};
DE            Short=CoFad2 {ECO:0000303|PubMed:11161042};
DE            EC=1.14.19.- {ECO:0000305};
GN   Name=FAD2 {ECO:0000303|PubMed:11161042};
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:AAK26633.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11161042; DOI=10.1104/pp.125.2.847;
RA   Qiu X., Reed D.W., Hong H., MacKenzie S.L., Covello P.S.;
RT   "Identification and analysis of a gene from Calendula officinalis encoding
RT   a fatty acid conjugase.";
RL   Plant Physiol. 125:847-855(2001).
CC   -!- FUNCTION: Catalyzes the desaturation of oleic acid to linoleic acid.
CC       Introduces a double bond at position 12 of 16:1(9Z) and 18:1(9Z).
CC       {ECO:0000269|PubMed:11161042}.
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, flower buds and developing
CC       seeds.
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; AF343065; AAK26633.1; -; mRNA.
DR   AlphaFoldDB; Q9AT72; -.
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; IDA:UniProtKB.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
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..383
FT                   /note="Delta(12) fatty acid desaturase FAD2"
FT                   /id="PRO_0000435420"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           106..110
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           142..146
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           316..320
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   383 AA;  43996 MW;  2FCAD57AA56EF667 CRC64;
     MGAGGRMQDP TNGGNKTEPE PIQRVPHEKP PFTVGDIKKA IPPHCFNRSV IRSFSYVFYD
     LTIASILYYI ANNYISTLPS PLAYVAWPVY WAVQGCVLTG VWVIAHECGH HAFSDHQWLD
     DTVGLVLHSF LLVPYFSWKY SHRRHHSNTG SIEHDEVFVP KLKSGVRSTA RYLNNPPGRI
     LTLLVTLTLG WPLYLTFNVS GRYYDRFACH FDPNSPIYSK RERAQIFISD AGILAVVFVL
     FRLAMTKGLT WVLTMYGGPL LVVNGFLVLI TFLQHTHPSL PHYDSTEWDW LRGALTTIDR
     DYGILNKVFH NITDTHVAHH LFSTMPHYHA MEATKVIKPI LGDYYQFDGT SIFKAMYRET
     KECIYVDKDE EVKDGVYWYR NKI
 
 
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