FAD12_TRICA
ID FAD12_TRICA Reviewed; 358 AA.
AC B7SB92;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Acyl-CoA Delta-12 desaturase {ECO:0000303|PubMed:19133076};
DE EC=1.14.19.6 {ECO:0000269|PubMed:21300802, ECO:0000305|PubMed:19133076};
DE AltName: Full=Acyl-CoA Delta(11) desaturase-like Protein {ECO:0000312|EMBL:EFA00770.1};
GN Name=D12Des {ECO:0000312|EMBL:ABY26958.1};
GN ORFNames=TcasGA2_TC003656 {ECO:0000312|EMBL:EFA00770.1};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19133076; DOI=10.1111/j.1365-2583.2008.00841.x;
RA Zhou X.-R., Horne I., Damcevski K., Haritos V., Green A., Singh S.;
RT "Isolation and functional characterization of two independently-evolved
RT fatty acid Delta12-desaturase genes from insects.";
RL Insect Mol. Biol. 17:667-676(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000312|EMBL:EFA00770.1};
RA Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT "Tools and pipelines for BioNano data: molecule assembly pipeline and FASTA
RT super scaffolding tool.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000312|EMBL:EFA00770.1,
RC ECO:0000312|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000312|EMBL:EFA00770.1,
RC ECO:0000312|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
RN [5]
RP CATALYTIC ACTIVITY.
RX PubMed=21300802; DOI=10.1074/jbc.m110.191098;
RA Vanhercke T., Shrestha P., Green A.G., Singh S.P.;
RT "Mechanistic and structural insights into the regioselectivity of an acyl-
RT CoA fatty acid desaturase via directed molecular evolution.";
RL J. Biol. Chem. 286:12860-12869(2011).
CC -!- FUNCTION: Catalyzes the formation of a Delta12 double bond, acting on
CC monounsaturated fatty acyl subtrates like palmitoleoyl-CoA ((9Z)-
CC hexadecenoyl-CoA) and oleoyl-CoA ((9Z)-octadecenoyl-CoA) with higher
CC desaturation activity on (9Z)-octadecenoyl-CoA than (9Z)-hexadecenoyl-
CC CoA. Requires preexisting cis double bond at the Delta9 position of
CC fatty acyls to be able to insert the Delta12 double bond. Delta12-
CC desaturation of (9Z)-octadecenoyl-CoA in insects produces (9Z,12Z)-
CC octadecadienoyl-CoA (linoleoyl-CoA) which may be used to supply
CC precursors of crucial mediators of immunity and reproduction and other
CC essential functions. {ECO:0000269|PubMed:19133076}.
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:21300802, ECO:0000305|PubMed:19133076};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25857;
CC Evidence={ECO:0000305|PubMed:19133076, ECO:0000305|PubMed:21300802};
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:0000305|PubMed:19133076};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45097;
CC Evidence={ECO:0000305|PubMed:19133076};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:O00767};
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:0000255|RuleBase:RU000581}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; EU159449; ABY26958.1; -; mRNA.
DR EMBL; KQ971322; EFA00770.1; -; Genomic_DNA.
DR RefSeq; NP_001137206.1; NM_001143734.1.
DR RefSeq; XP_008191083.1; XM_008192861.2.
DR RefSeq; XP_008191084.1; XM_008192862.2.
DR RefSeq; XP_008191086.1; XM_008192864.2.
DR RefSeq; XP_015833598.1; XM_015978112.1.
DR AlphaFoldDB; B7SB92; -.
DR SMR; B7SB92; -.
DR STRING; 7070.TC003656-PA; -.
DR EnsemblMetazoa; TC003656_001; TC003656_001; TC003656.
DR GeneID; 100233160; -.
DR KEGG; tca:100233160; -.
DR CTD; 100233160; -.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_0_2_1; -.
DR InParanoid; B7SB92; -.
DR OMA; CQHGPID; -.
DR PhylomeDB; B7SB92; -.
DR Proteomes; UP000007266; Linkage group 3.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IBA:GO_Central.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..358
FT /note="Acyl-CoA Delta-12 desaturase"
FT /id="PRO_0000452362"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 75..80
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:Q6US81"
FT MOTIF 112..116
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:Q6US81"
FT MOTIF 254..258
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:Q6US81"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
SQ SEQUENCE 358 AA; 42475 MW; E032CB723579A51C CRC64;
MSAQTITTTE TTQNAQKPQQ YHWRMVWRNI ILYIIMHLTG FYGLYLAMFY AQWKTVFYSW
FLLVIALQGV TAGSHRLWAH KAYKARLPLR MLLCIFQTLS LQNHIYDWAT YHRVHHKFVD
TNADPHNSRR GFFFSHMGWL FIEPHKDVED KYKSIDFSDL HADSVVMIQK KYYHTFFAPV
IGFYLPAAIP WYFWGENFWT AFFVATMLRY CACTNITFLV NSWAHIYGSR PYDKNIYPTE
SATIAVLTGG EGWHNYHHTF PWDYKTGEFG KYRSNLTTGF LDFMAAIGWA YDLKTVSEEM
IMKRVLRTGD GTRKFDKIDK ILNVDDDHHH EDMLWGWGDS DMAKEEMNYV KIHNRKED
