SCD3_MOUSE
ID SCD3_MOUSE Reviewed; 359 AA.
AC Q99PL7; Q3UWK5; Q9D550;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Acyl-CoA desaturase 3 {ECO:0000305};
DE EC=1.14.19.- {ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:26098370};
DE AltName: Full=Delta(9)-desaturase 3 {ECO:0000303|PubMed:16443825};
DE Short=Delta-9 desaturase 3 {ECO:0000303|PubMed:16443825};
DE AltName: Full=Fatty acid desaturase 3 {ECO:0000305};
DE AltName: Full=Palmitoyl-CoA desaturase {ECO:0000303|PubMed:16443825};
DE AltName: Full=Stearoyl-CoA desaturase 3 {ECO:0000303|PubMed:11161812};
GN Name=Scd3 {ECO:0000312|MGI:MGI:1353437};
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:AAK13256.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11161812; DOI=10.1006/geno.2000.6429;
RA Zheng Y., Prouty S.M., Harmon A., Sundberg J.P., Stenn K.S., Parimoo S.;
RT "Scd3--a novel gene of the stearoyl-CoA desaturase family with restricted
RT expression in skin.";
RL Genomics 71:182-191(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE22909.1};
RC TISSUE=Eye {ECO:0000312|EMBL:BAE22909.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {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 [4] {ECO:0000312|EMBL:EDL01300.1}
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
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 [7]
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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 112-ILE-GLU-113.
RX PubMed=26098370; DOI=10.1038/nature14549;
RA Bai Y., McCoy J.G., Levin E.J., Sobrado P., Rajashankar K.R., Fox B.G.,
RA Zhou M.;
RT "X-ray structure of a mammalian stearoyl-CoA desaturase.";
RL Nature 524:252-256(2015).
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 (PubMed:16443825, PubMed:26098370). Has a strong
CC preference for saturated fatty acids with chain lengths of 14 or 16
CC carbon atoms (C14:0 and C16:0), and has only very low activity with
CC stearatate (C18:0) (PubMed:16443825, PubMed:26098370). Required for the
CC biosynthesis of membrane phospholipids, cholesterol esters and
CC triglycerides (By similarity). {ECO:0000250|UniProtKB:O00767,
CC ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:26098370}.
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 ECO:0000269|PubMed:26098370};
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:16443825}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99PL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99PL7-2; Sequence=VSP_057848;
CC -!- TISSUE SPECIFICITY: Detected in skin, but at lower levels compared to
CC Scd1. Detected in the middlle part of the sebaceous gland, but not in
CC hair follicle. Not detected in liver and brain.
CC {ECO:0000269|PubMed:11161812}.
CC -!- DEVELOPMENTAL STAGE: Expression is increased during the first eight
CC days (anagen) of the hair cycle in male mice, and is low during the
CC quiescent phase (telogen) of the hair cycle. Expression is very low
CC throughout the hair cycle in female mice.
CC {ECO:0000269|PubMed:11161812}.
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; AF272037; AAK13256.1; -; mRNA.
DR EMBL; AK015784; BAB29975.1; -; mRNA.
DR EMBL; AK136277; BAE22909.1; -; mRNA.
DR EMBL; AC123853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH468367; EDL01300.1; -; Genomic_DNA.
DR EMBL; BC118033; AAI18034.1; -; mRNA.
DR EMBL; BC118045; AAI18046.1; -; mRNA.
DR CCDS; CCDS29847.1; -. [Q99PL7-1]
DR RefSeq; NP_077770.1; NM_024450.2. [Q99PL7-1]
DR AlphaFoldDB; Q99PL7; -.
DR SMR; Q99PL7; -.
DR STRING; 10090.ENSMUSP00000026220; -.
DR iPTMnet; Q99PL7; -.
DR PhosphoSitePlus; Q99PL7; -.
DR SwissPalm; Q99PL7; -.
DR MaxQB; Q99PL7; -.
DR PaxDb; Q99PL7; -.
DR PRIDE; Q99PL7; -.
DR ProteomicsDB; 255486; -. [Q99PL7-1]
DR ProteomicsDB; 255487; -. [Q99PL7-2]
DR DNASU; 30049; -.
DR Ensembl; ENSMUST00000026220; ENSMUSP00000026220; ENSMUSG00000025202. [Q99PL7-1]
DR Ensembl; ENSMUST00000237324; ENSMUSP00000157819; ENSMUSG00000025202. [Q99PL7-2]
DR GeneID; 30049; -.
DR KEGG; mmu:30049; -.
DR UCSC; uc008hpn.1; mouse. [Q99PL7-1]
DR UCSC; uc008hpo.1; mouse.
DR CTD; 30049; -.
DR MGI; MGI:1353437; Scd3.
DR VEuPathDB; HostDB:ENSMUSG00000025202; -.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000162971; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; Q99PL7; -.
DR OMA; FIDCMAS; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; Q99PL7; -.
DR TreeFam; TF313251; -.
DR BioGRID-ORCS; 30049; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q99PL7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99PL7; protein.
DR Bgee; ENSMUSG00000025202; Expressed in animal zygote and 139 other tissues.
DR Genevisible; Q99PL7; MM.
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; ISO:MGI.
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:1903966; P:monounsaturated fatty acid biosynthetic process; IDA:MGI.
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 Alternative splicing; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Microsome; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Acyl-CoA desaturase 3"
FT /id="PRO_0000433871"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 94..97
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 119..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 238..241
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 264..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..125
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 157..161
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 298..302
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 9..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT VAR_SEQ 1..224
FT /note="Missing (in isoform 2)"
FT /id="VSP_057848"
FT MUTAGEN 112..113
FT /note="IE->AL: Changes substrate specificity so that
FT stearate becomes a good substrate."
FT CONFLICT 124
FT /note="S -> G (in Ref. 2; BAE22909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 41432 MW; 60E30AD688587E0F CRC64;
MPGHLLQEEM TPSYTTTTTI TAPPSGSLQN GREKVKTVPL YLEEDIRPEM KEDIYDPTYQ
DEEGPPPKLE YVWRNIILMA LLHVGALYGI TLVPSCKLYT CLFAFVYYVI SIEGIGAGVH
RLWSHRTYKA RLPLRIFLII ANTMAFQNDV YEWARDHRAH HKFSETHADP HNSRRGFFFS
HVGWLLVRKH PAVKEKGGKL DMSDLKAEKL VMFQRRYYKP GILLMCFILP TLVPWYCWGE
TFLNSFYVAT LLRYAVVLNA TWLVNSAAHL YGYRPYDKNI DPRQNALVSL GSMGEGFHNY
HHAFPYDYSA SEYRWHINFT TFFIDCMAAL GLAYDRKRVS KATVLARIKR TGDGSHKSG
