FADS2_TACFU
ID FADS2_TACFU Reviewed; 445 AA.
AC A0A0C5PRW9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Fatty acid desaturase 2 {ECO:0000305};
DE EC=1.14.19.3 {ECO:0000250|UniProtKB:O95864};
DE AltName: Full=Acyl-CoA 6-desaturase {ECO:0000305};
DE AltName: Full=Delta(6) fatty acid desaturase {ECO:0000303|PubMed:25497832};
DE Short=Fads2 (delta6) {ECO:0000303|PubMed:25497832};
DE AltName: Full=Delta-6 fatty acid desaturase {ECO:0000305};
GN Name=FADS2 {ECO:0000305}; Synonyms=Delta6FAD {ECO:0000312|EMBL:AJQ20793.1};
OS Tachysurus fulvidraco (Yellow catfish) (Pimelodus fulvidraco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Bagridae; Tachysurus.
OX NCBI_TaxID=1234273 {ECO:0000312|EMBL:AJQ20793.1};
RN [1] {ECO:0000312|EMBL:AJQ20793.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Liver {ECO:0000303|PubMed:25497832};
RX PubMed=25497832; DOI=10.1016/j.gene.2014.12.014;
RA Song Y.F., Luo Z., Pan Y.X., Zhang L.H., Chen Q.L., Zheng J.L.;
RT "Three unsaturated fatty acid biosynthesis-related genes in yellow catfish
RT Pelteobagrus fulvidraco: Molecular characterization, tissue expression and
RT transcriptional regulation by leptin.";
RL Gene 563:1-9(2015).
CC -!- FUNCTION: Component of a lipid metabolic pathway that catalyzes
CC biosynthesis of highly unsaturated fatty acids (HUFA) from precursor
CC essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-
CC 6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first and
CC rate limiting step in this pathway which is the desaturation of LA
CC (18:2n-6) and ALA (18:3n-3) into gamma-linoleic acid (GLA) (18:3n-6)
CC and stearidonic acid (18:4n-3) respectively and other desaturation
CC steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many
CC biological functions. {ECO:0000250|UniProtKB:O95864}.
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:0000250|UniProtKB:O95864};
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:0000250|UniProtKB:O95864};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:O95864}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95864}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O95864}.
CC -!- TISSUE SPECIFICITY: Expression is highest in intestine, followed by
CC brain and heart, and lowest in gill. Also expressed in liver, spleen
CC and muscle. {ECO:0000269|PubMed:25497832}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; KJ831068; AJQ20793.1; -; mRNA.
DR AlphaFoldDB; A0A0C5PRW9; -.
DR SMR; A0A0C5PRW9; -.
DR UniPathway; UPA00658; -.
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:0016213; F:linoleoyl-CoA desaturase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="Fatty acid desaturase 2"
FT /id="PRO_0000441397"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..158
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..306
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..96
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 181..185
FT /note="Histidine box-1"
FT /evidence="ECO:0000305|PubMed:25497832"
FT MOTIF 218..222
FT /note="Histidine box-2"
FT /evidence="ECO:0000305|PubMed:25497832"
FT MOTIF 383..387
FT /note="Histidine box-3"
FT /evidence="ECO:0000305|PubMed:25497832"
SQ SEQUENCE 445 AA; 52133 MW; CB34B49B9B356BA0 CRC64;
MGGGGQLTEP GEQGSGRAGG VYTWEEVQSH SSRNDQWLVI DRKVYNITQW AKRHPGGIRV
ISHCCGEDAT DAFAAFHPDQ RYVRKFMKPL LLGELTPSEP SQDHDKNAAL MEDFRDLRKR
LESQGLFRTS PLFFILYLGH ILLLEALSVA LLWNFGNGWI ISLLLSVLLA TSQAQAGWLQ
HDFGHLSVFK NSTWDHLMHK FIIGHLKGAS ANWWNHRHFQ HHAKPNIVSK DPDVNMLNIL
VLGNILPVEY GIKKVKHMPY NHQHRYFFLV GPPLLLPLYF NLHVIQTMYL QRDWVDFAWF
LSYYARFFMF YSPYYGILGS LVLITFVRFL ESHWFVWVTQ MNHIPMDIDH DKHDDWLSMQ
LKATCNIEHS QFNDWFSGHL NFQIEHHLFP MMPRHNYSRA SPQVRELCEK YGIQYQVKGL
WESWCDIVRS LKKSGELWLD AYLHK
