FADS3_BOVIN
ID FADS3_BOVIN Reviewed; 443 AA.
AC A4IFP3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Fatty acid desaturase 3 {ECO:0000250|UniProtKB:Q8K1P9};
DE EC=1.14.19.- {ECO:0000250|UniProtKB:Q8K1P9};
DE AltName: Full=Delta(13) fatty acid desaturase {ECO:0000250|UniProtKB:Q8K1P9};
DE Short=Delta(13) desaturase {ECO:0000250|UniProtKB:Q8K1P9};
GN Name=FADS3 {ECO:0000250|UniProtKB:Q8K1P9};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mammals have different sphingoid bases that differ in their
CC length and/or pattern of desaturation and hydroxyl groups. The
CC predominant sphingoid base in mammalian ceramides is sphing-4-enine
CC (sphingosine or SPH) which has a trans desaturation at carbon 4. FADS3
CC is a ceramide desaturase that introduces a cis double bond between
CC carbon 14 and carbon 15 of the SPH-containing ceramides, producing
CC sphinga-4,14-dienine-containing ceramides (SPD ceramides). SPD
CC ceramides occur widely in mammalian tissues and cells. Due to their
CC unusual structure containing a cis double bond, SPD ceramides may have
CC an opposite, negative role in lipid microdomain formation relative to
CC conventional ceramides (By similarity). FADS3 also acts as a methyl-end
CC fatty acyl coenzyme A (CoA) desaturase that introduces a cis double
CC bond between the preexisting double bond and the terminal methyl group
CC of the fatty acyl chain. Desaturates (11E)-octadecenoate (trans-
CC vaccenoate, the predominant trans fatty acid in cow milk) at carbon 13
CC to generate (11E,13Z)-octadecadienoate (also known as conjugated
CC linoleic acid 11E,13Z-CLA), likely participating in the
CC biohydrogenation pathway of linoleic acid (LA) (By similarity).
CC {ECO:0000250|UniProtKB:Q8K1P9, ECO:0000250|UniProtKB:Q9Y5Q0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = an N-acyl-sphinga-4E,14Z-dienine + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:63928, 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:52639,
CC ChEBI:CHEBI:139573; Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63929;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N-(hexanoyl)sphing-4-enine
CC + O2 = 2 Fe(III)-[cytochrome b5] + 2 H2O + N-hexanoyl-sphinga-4E,14Z-
CC dienine; Xref=Rhea:RHEA:63940, 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:63867,
CC ChEBI:CHEBI:149631; Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63941;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Q0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (11E,13Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:46056, 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:85650; Evidence={ECO:0000250|UniProtKB:Q8K1P9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46057;
CC Evidence={ECO:0000250|UniProtKB:Q8K1P9};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q8K1P9}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q9Y5Q0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y5Q0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The protein sequence includes a number of characteristic
CC features of microsomal fatty acid desaturases including the three
CC histidine boxes (these domains may contain the active site and/or be
CC involved in metal ion binding), and the N-terminal cytochrome b5 domain
CC containing the heme-binding motif, HPGG, similar to that of other fatty
CC acid desaturases. {ECO:0000250|UniProtKB:Q9Y5Q0}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; BC134687; AAI34688.1; -; mRNA.
DR RefSeq; NP_001077160.1; NM_001083691.2.
DR AlphaFoldDB; A4IFP3; -.
DR SMR; A4IFP3; -.
DR STRING; 9913.ENSBTAP00000020612; -.
DR PaxDb; A4IFP3; -.
DR PRIDE; A4IFP3; -.
DR Ensembl; ENSBTAT00000020612; ENSBTAP00000020612; ENSBTAG00000015511.
DR GeneID; 515925; -.
DR KEGG; bta:515925; -.
DR CTD; 3995; -.
DR VEuPathDB; HostDB:ENSBTAG00000015511; -.
DR VGNC; VGNC:28703; FADS3.
DR eggNOG; KOG4232; Eukaryota.
DR GeneTree; ENSGT00950000182990; -.
DR HOGENOM; CLU_016265_0_1_1; -.
DR InParanoid; A4IFP3; -.
DR OMA; WMHEAGH; -.
DR OrthoDB; 1060606at2759; -.
DR TreeFam; TF313604; -.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000009136; Chromosome 29.
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: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:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
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 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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..443
FT /note="Fatty acid desaturase 3"
FT /id="PRO_0000307107"
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
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..282
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..443
FT /note="Lumenal"
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 /evidence="ECO:0000250|UniProtKB:Q9Y5Q0"
FT MOTIF 217..221
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Q0"
FT MOTIF 381..385
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Q0"
SQ SEQUENCE 443 AA; 51306 MW; 862F13D78FA45C50 CRC64;
MGGVGEPDWE PGQRGAPLPT LRWEQVRRHN LPGDKWLVIE RRVYDISRWA QRHPGGSRLI
GHHGAEDATD AFHAFHQDLS FVRKFLQPLL IGELAPEEPS QDGPQNTQLI EDFRALRQAV
EDMKLFEAKP AFFGLLLGHI LAMEVLAWLM IYMLGPGWVP STLAALILAI SQAQSWCLQH
DLGHTSIFRN SRWNHLAQQF VMGQLKGFSA HWWNFRHFQH HAKPNIFHKD PDVTVAPVFL
LGESSVEYGK KKRRYLPYNH QHLYFFLIGP PLLTLVNFEV ENLAYMLVCM QWMDLLWAAS
FYARFLLSYI PFYGIPGALL LFVAVRVLES HWFVWITQMN HIPREIGHEK HRDWASSQLA
ATCNVEPSLF IDWFSGHLNF QIEHHLFPTM PRHNYRRVAP LVKALCAKHG LSYEVKPFLT
ALVDIIRSLK KSGNVWLEAY LHQ
