FADS2_DANRE
ID FADS2_DANRE Reviewed; 444 AA.
AC Q9DEX7; Q7ZWF3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Acyl-CoA 6-desaturase {ECO:0000250|UniProtKB:O95864};
DE EC=1.14.19.3 {ECO:0000269|PubMed:11724940};
DE EC=1.14.19.44 {ECO:0000269|PubMed:11724940};
DE AltName: Full=Delta(5)/Delta(6) fatty acid desaturase;
DE Short=D5D/D6D fatty acid desaturase;
DE Short=Delta-5/Delta-6 fatty acid desaturase;
DE AltName: Full=Fatty acid desaturase 2;
GN Name=fads2; Synonyms=fadsd6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP DOMAIN.
RC TISSUE=Liver;
RX PubMed=11724940; DOI=10.1073/pnas.251516598;
RA Hastings N., Agaba M., Tocher D.R., Leaver M.J., Dick J.R., Sargent J.R.,
RA Teale A.J.;
RT "A vertebrate fatty acid desaturase with delta5 and delta6 activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14304-14309(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Fatty acid desaturase with bifunctional delta-5 and delta-6
CC activities. Component of a lipid metabolic pathway that catalyzes the
CC biosynthesis of polyunsaturated fatty acids (PUFA) with preference
CC toward n-3 substrates and Delta-6 function.
CC {ECO:0000269|PubMed:11724940}.
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:0000269|PubMed:11724940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47141;
CC Evidence={ECO:0000269|PubMed:11724940};
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:0000269|PubMed:11724940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47145;
CC Evidence={ECO:0000269|PubMed:11724940};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome
CC b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2
CC Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46420, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:73862, ChEBI:CHEBI:74265;
CC EC=1.14.19.44; Evidence={ECO:0000269|PubMed:11724940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421;
CC Evidence={ECO:0000269|PubMed:11724940};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46424, 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:57368, ChEBI:CHEBI:74264; EC=1.14.19.44;
CC Evidence={ECO:0000269|PubMed:11724940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46425;
CC Evidence={ECO:0000269|PubMed:11724940};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305|PubMed:11724940}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The protein sequence includes a number of characteristic
CC features of microsomal fatty acid desaturases including the three
CC histidine boxes HXXXH, HXXHH, and QXXHH (these domains may contain the
CC active site and/or be involved in metal ion binding), and the N-
CC terminal cytochrome b5 domain containing the heme-binding motif, HPGG,
CC similar to that of other fatty acid desaturases.
CC {ECO:0000303|PubMed:11724940}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF309556; AAG25710.1; -; mRNA.
DR EMBL; BC049438; AAH49438.1; -; mRNA.
DR RefSeq; NP_571720.2; NM_131645.2.
DR AlphaFoldDB; Q9DEX7; -.
DR SMR; Q9DEX7; -.
DR STRING; 7955.ENSDARP00000022396; -.
DR SwissLipids; SLP:000000464; -.
DR PaxDb; Q9DEX7; -.
DR GeneID; 140615; -.
DR KEGG; dre:140615; -.
DR CTD; 9415; -.
DR ZFIN; ZDB-GENE-011212-1; fads2.
DR eggNOG; KOG4232; Eukaryota.
DR InParanoid; Q9DEX7; -.
DR OrthoDB; 1060606at2759; -.
DR PhylomeDB; Q9DEX7; -.
DR BRENDA; 1.14.19.3; 928.
DR Reactome; R-DRE-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-DRE-2046106; alpha-linolenic acid (ALA) metabolism.
DR UniPathway; UPA00658; -.
DR ChiTaRS; fads2; zebrafish.
DR PRO; PR:Q9DEX7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0062076; F:acyl-CoA delta5-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0016213; F:linoleoyl-CoA desaturase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IMP:ZFIN.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.120.10; -; 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; PTHR19353; 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; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..444
FT /note="Acyl-CoA 6-desaturase"
FT /id="PRO_0000185408"
FT TOPO_DOM 1..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..157
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..305
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 18..95
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 180..184
FT /note="Histidine box-1"
FT MOTIF 217..221
FT /note="Histidine box-2"
FT MOTIF 382..386
FT /note="Histidine box-3"
FT CONFLICT 26
FT /note="V -> M (in Ref. 2; AAH49438)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="V -> M (in Ref. 2; AAH49438)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="M -> V (in Ref. 2; AAH49438)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="H -> R (in Ref. 2; AAH49438)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="K -> Q (in Ref. 2; AAH49438)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="V -> M (in Ref. 2; AAH49438)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="A -> S (in Ref. 2; AAH49438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 52032 MW; 6AA25A1DC1DC0F65 CRC64;
MGGGGQQTDR ITDTNGRFSS YTWEEVQKHT KHGDQWVVVE RKVYNVSQWV KRHPGGLRIL
GHYAGEDATE AFTAFHPNLQ LVRKYLKPLL IGELEASEPS QDRQKNAALV EDFRALRERL
EAEGCFKTQP LFFALHLGHI LLLEAIAFMM VWYFGTGWIN TLIVAVILAT AQSQAGWLQH
DFGHLSVFKT SGMNHLVHKF VIGHLKGASA GWWNHRHFQH HAKPNIFKKD PDVNMLNAFV
VGNVQPVEYG VKKIKHLPYN HQHKYFFFIG PPLLIPVYFQ FQIFHNMISH GMWVDLLWCI
SYYVRYFLCY TQFYGVFWAI ILFNFVRFME SHWFVWVTQM SHIPMNIDYE KNQDWLSMQL
VATCNIEQSA FNDWFSGHLN FQIEHHLFPT VPRHNYWRAA PRVRALCEKY GVKYQEKTLY
GAFADIIRSL EKSGELWLDA YLNK
