ID A0A1D2MJ01_ORCCI Unreviewed; 516 AA.
AC A0A1D2MJ01;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA Delta(11) desaturase {ECO:0000313|EMBL:ODM92901.1};
GN ORFNames=Ocin01_13782 {ECO:0000313|EMBL:ODM92901.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM92901.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM92901.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM92901.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU000581};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000256|RuleBase:RU000581}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|RuleBase:RU000581}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM92901.1}.
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DR EMBL; LJIJ01001121; ODM92901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2MJ01; -.
DR STRING; 48709.A0A1D2MJ01; -.
DR OrthoDB; 5487114at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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: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 PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU000581};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Lipid metabolism {ECO:0000256|RuleBase:RU000581};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000581};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000581};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..258
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 60066 MW; 2E9BF4C255DB01E4 CRC64;
MGTLEKKKTE PYLAFERPLG LEQHVFNTIN LGAAHSLAFY YFWLDFRGET PPTFWFEFFY
GYIGGLGITV GCHRLWTHRT FKAALPLQIF LMICQTISMQ LPIRKWCLDH RIHHKFTDTS
RDPHNSKRGF WFSHVMWLVL PKHPDLQKEL KTFEVPDLDN DPVVRFQSKY YWPLILIFHI
LVPILTMQYF WPEITLLQCL GADMRRYVIS LHVTYCVNSV AHMWGDKPYD GNITAVESPI
VSFLAIGEGW HNFHHTFPWD YKTSEFGWKL NVSTVFIDFM AKIGWAYDLK TVSHQIIQQR
IARTGPPVED SNCNIPNNSE GDKTNDQVYQ AVKEWMMESE ENPVWGWNDE RIPQELRKAT
KILNVKTLSW LRSFRLFIGT SFPSPHGKDD SNEESSKIFS TKRTPAQFVG MSDVTRSIHE
DGQIPTELPR GEMFECPSRF PVLENQAELE GFKNTLGSNL ICLENRKEDL SAFINCHSFL
FHTLLCEKVV GDKPSCWYEA ELEGCYADLF LDFPAD
//
