ACO11_TRINI
ID ACO11_TRINI Reviewed; 349 AA.
AC O44390; Q9BKA3; Q9BKA4;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Acyl-CoA Delta(11) desaturase;
DE EC=1.14.19.5 {ECO:0000269|PubMed:9860961};
DE AltName: Full=Acyl-CoA Delta-11 desaturase;
DE Short=Delta(11)-desaturase;
GN Name=D11DS; Synonyms=PGD11DS;
OS Trichoplusia ni (Cabbage looper).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Plusiinae; Trichoplusia.
OX NCBI_TaxID=7111;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pheromone gland;
RX PubMed=9860961; DOI=10.1073/pnas.95.26.15287;
RA Knipple D.C., Rosenfield C.-L., Miller S.J., Liu W., Tang J., Ma P.W.K.,
RA Roelofs W.L.;
RT "Cloning and functional expression of a cDNA encoding a pheromone gland-
RT specific acyl-CoA delta11-desaturase of the cabbage looper moth,
RT Trichoplusia ni.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15287-15292(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-259.
RX PubMed=11483431; DOI=10.1016/s0965-1748(01)00043-1;
RA Rosenfield C.-L., You K.M., Marsella-Herrick P., Roelofs W.L.,
RA Knipple D.C.;
RT "Structural and functional conservation and divergence among acyl-CoA
RT desaturases of two noctuid species, the corn earworm, Helicoverpa zea, and
RT the cabbage looper, Trichoplusia ni.";
RL Insect Biochem. Mol. Biol. 31:949-964(2001).
CC -!- FUNCTION: Catalyzes the formation of Delta(11) fatty acyl precursors in
CC the pheromone gland. {ECO:0000269|PubMed:9860961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an 11,12-saturated fatty acyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = an (11Z)-Delta(11)-fatty acyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:25852, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:84947, ChEBI:CHEBI:84948; EC=1.14.19.5;
CC Evidence={ECO:0000269|PubMed:9860961};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Adult female pheromone gland. Increases by two or
CC three orders of magnitude during the first 2 days after adult eclosion.
CC {ECO:0000269|PubMed:9860961}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF035375; AAD03775.1; -; mRNA.
DR EMBL; AF297114; AAK21864.1; -; Genomic_DNA.
DR EMBL; AF297113; AAK21863.1; -; Genomic_DNA.
DR AlphaFoldDB; O44390; -.
DR SMR; O44390; -.
DR BioCyc; MetaCyc:MON-18385; -.
DR BRENDA; 1.14.19.5; 6461.
DR Proteomes; UP000322000; Genome assembly.
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:0017105; F:acyl-CoA delta11-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050601; F:myristoyl-CoA 11-(Z) desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..349
FT /note="Acyl-CoA Delta(11) desaturase"
FT /id="PRO_0000185410"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 86..91
FT /note="Histidine box-1"
FT MOTIF 123..127
FT /note="Histidine box-2"
FT MOTIF 263..267
FT /note="Histidine box-3"
FT CONFLICT 22
FT /note="V -> M (in Ref. 2; AAK21863)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> V (in Ref. 2; AAK21863)"
FT /evidence="ECO:0000305"
FT CONFLICT 125..135
FT /note="LHHKYSDTDAD -> YITNTAILMLI (in Ref. 2; AAK21863)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="A -> T (in Ref. 2; AAK21864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 40243 MW; F91AF7A2F59F0450 CRC64;
MAVMAQTVQE TATVLEEEAR TVTLVAPKTT PRKYKYIYTN FLTFSYAHLA ALYGLYLCFT
SAKWETLLFS FVLFHMSNIG ITAGAHRLWT HKTFKAKLPL EIVLMIFNSL AFQNTAITWA
REHRLHHKYS DTDADPHNAS RGFFYSHVGW LLVKKHPDVL KYGKTIDMSD VYNNPVLKFQ
KKYAVPLIGT VCFALPTLIP VYCWGESWNN AWHIALFRYI FNLNVTFLVN SAAHIWGNKP
YDKSILPAQN LLVSFLASGE GFHNYHHVFP WDYRTAELGN NFLNLTTLFI DFCAWFGWAY
DLKSVSEDII KQRAKRTGDG SSGVIWGWDD KDMDRDIKSK ANIFYAKKE
