ID A0A2K6D4T4_MACNE Unreviewed; 444 AA.
AC A0A2K6D4T4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Acyl-CoA 6-desaturase {ECO:0000256|ARBA:ARBA00039476};
DE EC=1.14.19.3 {ECO:0000256|ARBA:ARBA00038914};
DE AltName: Full=Fatty acid desaturase 2 {ECO:0000256|ARBA:ARBA00042828};
GN Name=FADS2 {ECO:0000313|Ensembl:ENSMNEP00000030911.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000030911.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000030911.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (6Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:46064, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296,
CC ChEBI:CHEBI:85652; Evidence={ECO:0000256|ARBA:ARBA00036342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46065;
CC Evidence={ECO:0000256|ARBA:ARBA00036342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:39567, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74264,
CC ChEBI:CHEBI:76410; Evidence={ECO:0000256|ARBA:ARBA00036205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39568;
CC Evidence={ECO:0000256|ARBA:ARBA00036205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z,17Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:39571, 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:74265, ChEBI:CHEBI:74328;
CC Evidence={ECO:0000256|ARBA:ARBA00036846};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39572;
CC Evidence={ECO:0000256|ARBA:ARBA00036846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:47140, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57363,
CC ChEBI:CHEBI:57383; EC=1.14.19.3;
CC Evidence={ECO:0000256|ARBA:ARBA00036039};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47141;
CC Evidence={ECO:0000256|ARBA:ARBA00036039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:47144, 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:71489, ChEBI:CHEBI:74034; EC=1.14.19.3;
CC Evidence={ECO:0000256|ARBA:ARBA00035980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47145;
CC Evidence={ECO:0000256|ARBA:ARBA00035980};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z,18Z,21Z)-tetracosapentaenoyl-CoA + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z,18Z,21Z)-
CC tetracosahexaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36999, 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:74083,
CC ChEBI:CHEBI:74086; Evidence={ECO:0000256|ARBA:ARBA00036321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37000;
CC Evidence={ECO:0000256|ARBA:ARBA00036321};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005105}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
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DR RefSeq; XP_011718716.1; XM_011720414.1.
DR AlphaFoldDB; A0A2K6D4T4; -.
DR SMR; A0A2K6D4T4; -.
DR STRING; 9545.ENSMNEP00000030911; -.
DR Ensembl; ENSMNET00000055334.1; ENSMNEP00000030911.1; ENSMNEG00000038871.1.
DR GeneID; 105469424; -.
DR KEGG; mni:105469424; -.
DR CTD; 9415; -.
DR GeneTree; ENSGT00950000182990; -.
DR OMA; QWWKNKH; -.
DR OrthoDB; 294339at2759; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000038871; Expressed in temporal lobe and 12 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:Ensembl.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353:SF12; ACYL-COA 6-DESATURASE; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..95
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 444 AA; 52301 MW; 6A57B278995FE52E CRC64;
MGKGGNQGEG AAEREVPMPT FSWEEIQKHN LRTDRWLVID RKVYNITKWS TQHPGGQRVI
GHYAGEDATD AFRAFHPDLK FVGKFLKPLL IGELAPEEPS QDHGKNSKII EDFRALKKTA
EDMNLFKTNH VFFLLLLAHI IALESIAWFT VFYFGNGWIP TLITAFVLAT SQAQAGWLQH
DYGHLSVYRK PKWNHLVHKF VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDVNMLHVFV
LGEWQPIEYG KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIVH KNWVDLAWAI
SYYIRFFVTY IPFYGILGAL LFLNFIRFLE SHWFVWVTQM NHIVMEIDQE AYRDWFSSQL
TATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA PLVKSLCAKH GIEYQEKPLL
RALLDIIRSL RKSGKLWLDA YLHK
//
