SCD4_MOUSE
ID SCD4_MOUSE Reviewed; 353 AA.
AC Q6T707; B9EIY5;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Stearoyl-CoA desaturase 4 {ECO:0000303|PubMed:12815040};
DE EC=1.14.19.1 {ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16443825};
DE AltName: Full=Acyl-CoA desaturase 4 {ECO:0000305};
DE AltName: Full=Delta(9)-desaturase 4 {ECO:0000303|PubMed:16443825};
DE Short=Delta-9 desaturase 4 {ECO:0000303|PubMed:16443825};
DE AltName: Full=Fatty acid desaturase 4 {ECO:0000305};
GN Name=Scd4 {ECO:0000312|MGI:MGI:2670997};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAR06950.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY NR1H3 AGONISTS; FAT-FREE
RP HIGH-CARBOHYDRATE DIET AND LEPTIN.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAR06950.1};
RX PubMed=12815040; DOI=10.1074/jbc.m304724200;
RA Miyazaki M., Jacobson M.J., Man W.C., Cohen P., Asilmaz E., Friedman J.M.,
RA Ntambi J.M.;
RT "Identification and characterization of murine SCD4, a novel heart-specific
RT stearoyl-CoA desaturase isoform regulated by leptin and dietary factors.";
RL J. Biol. Chem. 278:33904-33911(2003).
RN [2] {ECO:0000312|Ensembl:ENSMUSP00000059860, ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000059860,
RC ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16118274; DOI=10.1073/pnas.0503132102;
RA Miyazaki M., Dobrzyn A., Elias P.M., Ntambi J.M.;
RT "Stearoyl-CoA desaturase-2 gene expression is required for lipid synthesis
RT during early skin and liver development.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12501-12506(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=16443825; DOI=10.1194/jlr.c500025-jlr200;
RA Miyazaki M., Bruggink S.M., Ntambi J.M.;
RT "Identification of mouse palmitoyl-coenzyme A Delta9-desaturase.";
RL J. Lipid Res. 47:700-704(2006).
CC -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond
CC at the delta-9 position into fatty acyl-CoA substrates including
CC palmitoyl-CoA and stearoyl-CoA (PubMed:12815040, PubMed:16443825).
CC Required for the biosynthesis of membrane phospholipids, cholesterol
CC esters and triglycerides (By similarity).
CC {ECO:0000250|UniProtKB:O00767, ECO:0000269|PubMed:12815040,
CC ECO:0000269|PubMed:16443825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, 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:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16443825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36931, 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:57379,
CC ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:16443825};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:O00767};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O00767}. Microsome membrane
CC {ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16443825}.
CC -!- TISSUE SPECIFICITY: Detected in heart, but not in brain, liver, skin or
CC adipose tissue. {ECO:0000269|PubMed:12815040}.
CC -!- INDUCTION: Up-regulated by agonists that activate NR1H3. Up-regulated
CC by a fat-free high-carbohydrate diet. Not down-regulated by a high-
CC carbohydrate diet supplemented with unsaturated fatty acids. Down-
CC regulated by leptin. {ECO:0000269|PubMed:12815040}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000255|RuleBase:RU000581}.
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DR EMBL; AY430080; AAR06950.1; -; mRNA.
DR EMBL; AC123853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466534; EDL41929.1; -; Genomic_DNA.
DR EMBL; BC141234; AAI41235.1; -; mRNA.
DR CCDS; CCDS29849.1; -.
DR RefSeq; NP_899039.2; NM_183216.3.
DR AlphaFoldDB; Q6T707; -.
DR SMR; Q6T707; -.
DR STRING; 10090.ENSMUSP00000059860; -.
DR SwissLipids; SLP:000001657; -.
DR iPTMnet; Q6T707; -.
DR PhosphoSitePlus; Q6T707; -.
DR SwissPalm; Q6T707; -.
DR MaxQB; Q6T707; -.
DR PaxDb; Q6T707; -.
DR PRIDE; Q6T707; -.
DR DNASU; 329065; -.
DR Ensembl; ENSMUST00000058856; ENSMUSP00000059860; ENSMUSG00000050195.
DR GeneID; 329065; -.
DR KEGG; mmu:329065; -.
DR UCSC; uc008hpq.1; mouse.
DR CTD; 329065; -.
DR MGI; MGI:2670997; Scd4.
DR VEuPathDB; HostDB:ENSMUSG00000050195; -.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000154908; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; Q6T707; -.
DR OMA; WVLHMTW; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; Q6T707; -.
DR TreeFam; TF313251; -.
DR BRENDA; 1.14.19.1; 3474.
DR BioGRID-ORCS; 329065; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q6T707; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6T707; protein.
DR Bgee; ENSMUSG00000050195; Expressed in lip and 28 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0032896; F:palmitoyl-CoA 9-desaturase activity; IDA:MGI.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:MGI.
DR GO; GO:0031670; P:cellular response to nutrient; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:MGI.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0070542; P:response to fatty acid; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IBA:GO_Central.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Microsome; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..353
FT /note="Stearoyl-CoA desaturase 4"
FT /id="PRO_0000433872"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 88..91
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 113..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 232..235
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 258..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767, ECO:0000305"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..119
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 151..155
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 292..296
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 292
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 295
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT CONFLICT 193
FT /note="N -> S (in Ref. 3; EDL41929 and 4; AAI41235)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="M -> T (in Ref. 3; EDL41929 and 4; AAI41235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 41042 MW; EEF07F95776A4E0D CRC64;
MTAHLPQEIS SRCSTTNIME PHSRRQQDGE EKMPLQAEDI RPEIKDDLYD PSYQDEEGPP
PKLEYVWRNI IFMALLHVGA LYGITLVPSC KVYTWLLGVF YNVVAGLGIT AGAHRLWSHR
TYKARLPLRI FLIMANTMAF QNDVYEWARD HRAHHKFSET HADPHNSRRG FFFSHVGWLL
VRKHPAVKEK GKNLDMSDLK AEKLVMFQRR YYKLAVTLMF IILPTLVPWY LWGETFQHSL
CVSNFLRYAV LLNFTWLVNS AAHLYGYRPY DRGIGARENP FVSMASLGEG FHNYHHTFPY
DYSVSEYRWH INFTTFFIDC MAALGLAYDR KKVSKAVVLA RIKRTGDGSH KSS
