SCD2_MOUSE
ID SCD2_MOUSE Reviewed; 358 AA.
AC P13011; Q8BH96;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Stearoyl-CoA desaturase 2 {ECO:0000303|PubMed:16118274};
DE EC=1.14.19.1 {ECO:0000269|PubMed:16443825, ECO:0000305|PubMed:16118274};
DE AltName: Full=Acyl-CoA desaturase 2;
DE AltName: Full=Delta(9)-desaturase 2;
DE Short=Delta-9 desaturase 2 {ECO:0000303|PubMed:16443825};
DE AltName: Full=Fatty acid desaturase 2;
GN Name=Scd2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adipocyte;
RX PubMed=2570068; DOI=10.1016/s0021-9258(18)63763-9;
RA Kaestner K.H., Ntambi J.M., Kelly T.J. Jr., Lane M.D.;
RT "Differentiation-induced gene expression in 3T3-L1 preadipocytes. A second
RT differentially expressed gene encoding stearoyl-CoA desaturase.";
RL J. Biol. Chem. 264:14755-14761(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Spinal ganglion;
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]
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].
RC STRAIN=129; TISSUE=Mammary tumor;
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=10545940; DOI=10.1038/15446;
RA Zheng Y., Eilertsen K.J., Ge L., Zhang L., Sundberg J.P., Prouty S.M.,
RA Stenn K.S., Parimoo S.;
RT "Scd1 is expressed in sebaceous glands and is disrupted in the asebia
RT mouse.";
RL Nat. Genet. 23:268-270(1999).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
RP INDUCTION BY UNSATURATED FATTY ACIDS AND NR1H3, AND TISSUE SPECIFICITY.
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND 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 [9]
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 (PubMed:16443825). Catalyzes the insertion of
CC a cis double bond at the delta-9 position into fatty acyl-CoA
CC substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:16443825).
CC Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids
CC (PubMed:16443825). Contributes to the biosynthesis of membrane
CC phospholipids, cholesterol esters and triglycerides, especially during
CC embryonic development and in neonates (PubMed:16118274). Important for
CC normal permeability barrier function of the skin in neonates
CC (PubMed:16118274). {ECO:0000269|PubMed:16118274,
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:16443825, ECO:0000305|PubMed:16118274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722;
CC Evidence={ECO:0000305|PubMed:16118274, ECO:0000305|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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC Evidence={ECO:0000305|PubMed:16443825};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P13516};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P13516};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:16443825}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:16443825}. Microsome membrane
CC {ECO:0000269|PubMed:16443825}.
CC -!- TISSUE SPECIFICITY: Detected in brain and skin (PubMed:10545940,
CC PubMed:11161812, PubMed:16118274). Highly expressed in brain, and
CC detected at low levels in heart, stomach, lung and testis
CC (PubMed:11161812, PubMed:12815040). Detected both in dermis and
CC epidermis (PubMed:16118274). {ECO:0000269|PubMed:10545940,
CC ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16118274}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during embryonic development and
CC during the first three weeks after birth. Expression is low in adults.
CC {ECO:0000269|PubMed:16118274}.
CC -!- INDUCTION: Up-regulated by agonists that activate NR1H3
CC (PubMed:12815040). Slightly down-regulated by a high-carbohydrate diet
CC enriched in unsaturated fatty acids (PubMed:12815040).
CC {ECO:0000269|PubMed:12815040}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate. Neonates are smaller than wild-type and present high mortality,
CC ranging from 70 to 100%, depending on the genetic background. Neonates
CC display a shiny skin, but after a few hours their skin appears dry and
CC cracked. The permeability barrier function of their skin is impaired,
CC leading to rapid weight loss due to dehydration. Their epidermis has
CC decreased levels of cholesterol esters, triglycerides, acylceramide,
CC and glucosylacylceramide containing unsaturated fatty acids. In mutant
CC neonates, triglyceride levels in liver and blood plasma are reduced by
CC half, due to strongly reduced levels of stearoyl-CoA desaturase
CC activity in the liver and strongly reduced levels of triglyceride
CC biosynthesis. In contrast, the levels of stearoyl-CoA desaturase
CC activity are normal in adult mice deficient for Scd2. Adult mice
CC display kinked tails. {ECO:0000269|PubMed:16118274}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; M26270; AAA40094.1; -; mRNA.
DR EMBL; AK083922; BAC39066.1; -; mRNA.
DR EMBL; AK147406; BAE27893.1; -; mRNA.
DR EMBL; CH466534; EDL41928.1; -; Genomic_DNA.
DR EMBL; BC040384; AAH40384.1; -; mRNA.
DR CCDS; CCDS29848.1; -.
DR PIR; A36507; A36507.
DR RefSeq; NP_033154.2; NM_009128.2.
DR AlphaFoldDB; P13011; -.
DR SMR; P13011; -.
DR BioGRID; 203089; 2.
DR IntAct; P13011; 1.
DR MINT; P13011; -.
DR STRING; 10090.ENSMUSP00000026221; -.
DR iPTMnet; P13011; -.
DR PhosphoSitePlus; P13011; -.
DR SwissPalm; P13011; -.
DR EPD; P13011; -.
DR MaxQB; P13011; -.
DR PaxDb; P13011; -.
DR PeptideAtlas; P13011; -.
DR PRIDE; P13011; -.
DR ProteomicsDB; 285646; -.
DR DNASU; 20250; -.
DR Ensembl; ENSMUST00000026221; ENSMUSP00000026221; ENSMUSG00000025203.
DR GeneID; 20250; -.
DR KEGG; mmu:20250; -.
DR UCSC; uc008hpp.2; mouse.
DR CTD; 20250; -.
DR MGI; MGI:98240; Scd2.
DR VEuPathDB; HostDB:ENSMUSG00000025203; -.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000154908; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; P13011; -.
DR OMA; FWVTTHR; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; P13011; -.
DR TreeFam; TF313251; -.
DR BRENDA; 1.14.19.1; 3474.
DR Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
DR BioGRID-ORCS; 20250; 12 hits in 76 CRISPR screens.
DR ChiTaRS; Scd2; mouse.
DR PRO; PR:P13011; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P13011; protein.
DR Bgee; ENSMUSG00000025203; Expressed in migratory enteric neural crest cell and 268 other tissues.
DR ExpressionAtlas; P13011; baseline and differential.
DR Genevisible; P13011; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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:0004768; F:stearoyl-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; ISO:MGI.
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..358
FT /note="Stearoyl-CoA desaturase 2"
FT /id="PRO_0000185398"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 93..96
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 118..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 237..240
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 263..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT REGION 16..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 119..124
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 156..160
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 297..301
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="substrate"
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:P13516"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 154
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="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT CONFLICT 220
FT /note="G -> D (in Ref. 1; AAA40094)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="G -> R (in Ref. 1; AAA40094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40916 MW; 3E04893F12E92A9A CRC64;
MPAHILQEIS GAYSATTTIT APPSGGQQNG GEKFEKSSHH WGADVRPELK DDLYDPTYQD
DEGPPPKLEY VWRNIILMAL LHLGALYGIT LVPSCKLYTC LFAYLYYVIS ALGITAGAHR
LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH
VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFVLPT LVPWYCWGET
FVNSLCVSTF LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH
HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSR AAVLARIKRT GDGSCKSG
