SCD_HUMAN
ID SCD_HUMAN Reviewed; 359 AA.
AC O00767; B2R5U0; D3DR68; Q16150; Q53GR9; Q5W037; Q5W038; Q6GSS4; Q96KF6;
AC Q9BS07; Q9Y695;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Stearoyl-CoA desaturase {ECO:0000303|PubMed:18765284};
DE Short=hSCD1 {ECO:0000303|PubMed:15907797};
DE EC=1.14.19.1 {ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284};
DE AltName: Full=Acyl-CoA desaturase;
DE AltName: Full=Delta(9)-desaturase;
DE Short=Delta-9 desaturase;
DE AltName: Full=Fatty acid desaturase;
GN Name=SCD;
GN Synonyms=FADS5 {ECO:0000312|HGNC:HGNC:10571},
GN SCD1 {ECO:0000303|PubMed:15610069}, SCDOS {ECO:0000312|HGNC:HGNC:10571};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Al-Jeryan L., McCord A., Pierotti A.R., Craft J.A.;
RT "Characterization and expression of a stearoyl CoA desaturase from human
RT liver.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-224.
RC TISSUE=Brain, Liver, and Skin;
RX PubMed=10229681; DOI=10.1042/bj3400255;
RA Zhang L., Ge L., Parimoo S., Stenn K., Prouty S.M.;
RT "Human stearoyl-CoA desaturase: alternative transcripts generated from a
RT single gene by usage of tandem polyadenylation sites.";
RL Biochem. J. 340:255-264(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-224.
RA Hoshino T., Ohtsu K.;
RT "Cloning, sequencing and expression of human stearoyl-CoA desaturase.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-224.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-224.
RC TISSUE=Mammary gland, and Placenta;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=11415448; DOI=10.1042/0264-6021:3570183;
RA Zhang L., Ge L., Tran T., Stenn K., Prouty S.M.;
RT "Isolation and characterization of the human stearoyl-CoA desaturase gene
RT promoter: requirement of a conserved CCAAT cis-element.";
RL Biochem. J. 357:183-193(2001).
RN [10]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-27.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-239.
RC TISSUE=Adipose tissue;
RX PubMed=7909540; DOI=10.1002/ijc.2910570310;
RA Li J., Ding S.-F., Habib N.A., Fermor B.F., Wood C.B., Gilmour R.S.;
RT "Partial characterization of a cDNA for human stearoyl-CoA desaturase and
RT changes in its mRNA expression in some normal and malignant tissues.";
RL Int. J. Cancer 57:348-352(1994).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15907797; DOI=10.1016/j.bbrc.2005.05.013;
RA Wang J., Yu L., Schmidt R.E., Su C., Huang X., Gould K., Cao G.;
RT "Characterization of HSCD5, a novel human stearoyl-CoA desaturase unique to
RT primates.";
RL Biochem. Biophys. Res. Commun. 332:735-742(2005).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=15610069; DOI=10.1042/bj20041554;
RA Zhang S., Yang Y., Shi Y.;
RT "Characterization of human SCD2, an oligomeric desaturase with improved
RT stability and enzyme activity by cross-linking in intact cells.";
RL Biochem. J. 388:135-142(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=18765284; DOI=10.1016/j.pep.2008.08.002;
RA Goren M.A., Fox B.G.;
RT "Wheat germ cell-free translation, purification, and assembly of a
RT functional human stearoyl-CoA desaturase complex.";
RL Protein Expr. Purif. 62:171-178(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198 AND SER-203, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 45-359 IN COMPLEX WITH
RP STEAROYL-COENZYME A AND ZINC IONS, AND TOPOLOGY.
RX PubMed=26098317; DOI=10.1038/nsmb.3049;
RA Wang H., Klein M.G., Zou H., Lane W., Snell G., Levin I., Li K., Sang B.C.;
RT "Crystal structure of human stearoyl-coenzyme A desaturase in complex with
RT substrate.";
RL Nat. Struct. Mol. Biol. 22:581-585(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 (PubMed:15907797, PubMed:18765284). Catalyzes
CC the insertion of a cis double bond at the delta-9 position into fatty
CC acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA
CC (PubMed:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and
CC 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role
CC in lipid biosynthesis. Plays an important role in regulating the
CC expression of genes that are involved in lipogenesis and in regulating
CC mitochondrial fatty acid oxidation (By similarity). Plays an important
CC role in body energy homeostasis (By similarity). Contributes to the
CC biosynthesis of membrane phospholipids, cholesterol esters and
CC triglycerides (By similarity). {ECO:0000250|UniProtKB:P13516,
CC ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797,
CC ECO:0000269|PubMed:18765284}.
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:15610069, ECO:0000269|PubMed:15907797,
CC ECO:0000269|PubMed:18765284};
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:15610069};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:18765284, ECO:0000305|PubMed:26098317};
CC Note=Expected to bind 2 Fe(2+) ions per subunit, instead of the Zn(2+)
CC ions seen in the 3D-structure. {ECO:0000305|PubMed:26098317};
CC -!- SUBUNIT: May self-associate and form homodimers.
CC {ECO:0000269|PubMed:15610069}.
CC -!- INTERACTION:
CC O00767; Q13520: AQP6; NbExp=3; IntAct=EBI-2684237, EBI-13059134;
CC O00767; Q9UJ71: CD207; NbExp=3; IntAct=EBI-2684237, EBI-2873235;
CC O00767; P20138: CD33; NbExp=3; IntAct=EBI-2684237, EBI-3906571;
CC O00767; Q9HA82: CERS4; NbExp=3; IntAct=EBI-2684237, EBI-2622997;
CC O00767; Q2HXU8-2: CLEC12B; NbExp=3; IntAct=EBI-2684237, EBI-12811991;
CC O00767; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2684237, EBI-6942903;
CC O00767; P49447: CYB561; NbExp=3; IntAct=EBI-2684237, EBI-8646596;
CC O00767; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-2684237, EBI-2680384;
CC O00767; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2684237, EBI-781551;
CC O00767; P08034: GJB1; NbExp=3; IntAct=EBI-2684237, EBI-17565645;
CC O00767; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2684237, EBI-13345167;
CC O00767; O15529: GPR42; NbExp=3; IntAct=EBI-2684237, EBI-18076404;
CC O00767; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2684237, EBI-11721746;
CC O00767; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-2684237, EBI-18053395;
CC O00767; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2684237, EBI-10266796;
CC O00767; P48051: KCNJ6; NbExp=3; IntAct=EBI-2684237, EBI-12017638;
CC O00767; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-2684237, EBI-2341610;
CC O00767; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-2684237, EBI-2689785;
CC O00767; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2684237, EBI-373355;
CC O00767; O14880: MGST3; NbExp=3; IntAct=EBI-2684237, EBI-724754;
CC O00767; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-2684237, EBI-3923617;
CC O00767; P15151: PVR; NbExp=3; IntAct=EBI-2684237, EBI-3919694;
CC O00767; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-2684237, EBI-11337973;
CC O00767; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-2684237, EBI-10192441;
CC O00767; Q99942: RNF5; NbExp=3; IntAct=EBI-2684237, EBI-348482;
CC O00767; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-2684237, EBI-17247926;
CC O00767; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-2684237, EBI-2855401;
CC O00767; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2684237, EBI-18159983;
CC O00767; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-2684237, EBI-5235586;
CC O00767; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-2684237, EBI-10819434;
CC O00767; P27105: STOM; NbExp=3; IntAct=EBI-2684237, EBI-1211440;
CC O00767; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2684237, EBI-6268651;
CC O00767; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-2684237, EBI-12947623;
CC O00767; Q3MIR4: TMEM30B; NbExp=3; IntAct=EBI-2684237, EBI-9527107;
CC O00767; O15393-2: TMPRSS2; NbExp=4; IntAct=EBI-2684237, EBI-12345267;
CC O00767; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2684237, EBI-6447886;
CC O00767; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-2684237, EBI-1055364;
CC O00767; A0A142I5B9; Xeno; NbExp=3; IntAct=EBI-2684237, EBI-20625235;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15907797}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18765284, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in fetal liver, lung and brain. Highly
CC expressed in adult adipose tissue, and at lower levels in adult brain
CC and lung. {ECO:0000269|PubMed:15907797}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000269|PubMed:26098317}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; Y13647; CAA73998.1; -; mRNA.
DR EMBL; AF097514; AAD29870.1; -; mRNA.
DR EMBL; AB032261; BAA93510.1; -; mRNA.
DR EMBL; AK312312; BAG35237.1; -; mRNA.
DR EMBL; AK222862; BAD96582.1; -; mRNA.
DR EMBL; AL139819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49829.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49830.1; -; Genomic_DNA.
DR EMBL; BC005807; AAH05807.1; -; mRNA.
DR EMBL; BC062303; AAH62303.1; -; mRNA.
DR EMBL; AF320307; AAK54510.1; -; Genomic_DNA.
DR EMBL; S70284; AAB30631.1; -; mRNA.
DR CCDS; CCDS7493.1; -.
DR PIR; I54779; I54779.
DR RefSeq; NP_005054.3; NM_005063.4.
DR PDB; 4ZYO; X-ray; 3.25 A; A=45-359.
DR PDBsum; 4ZYO; -.
DR AlphaFoldDB; O00767; -.
DR SMR; O00767; -.
DR BioGRID; 112225; 114.
DR IntAct; O00767; 58.
DR MINT; O00767; -.
DR STRING; 9606.ENSP00000359380; -.
DR BindingDB; O00767; -.
DR ChEMBL; CHEMBL5555; -.
DR SwissLipids; SLP:000000465; -.
DR GlyGen; O00767; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00767; -.
DR MetOSite; O00767; -.
DR PhosphoSitePlus; O00767; -.
DR SwissPalm; O00767; -.
DR BioMuta; SCD; -.
DR EPD; O00767; -.
DR jPOST; O00767; -.
DR MassIVE; O00767; -.
DR MaxQB; O00767; -.
DR PaxDb; O00767; -.
DR PeptideAtlas; O00767; -.
DR PRIDE; O00767; -.
DR ProteomicsDB; 48027; -.
DR TopDownProteomics; O00767; -.
DR Antibodypedia; 1335; 311 antibodies from 39 providers.
DR DNASU; 6319; -.
DR Ensembl; ENST00000370355.3; ENSP00000359380.2; ENSG00000099194.6.
DR GeneID; 6319; -.
DR KEGG; hsa:6319; -.
DR MANE-Select; ENST00000370355.3; ENSP00000359380.2; NM_005063.5; NP_005054.3.
DR UCSC; uc001kqy.4; human.
DR CTD; 6319; -.
DR DisGeNET; 6319; -.
DR GeneCards; SCD; -.
DR HGNC; HGNC:10571; SCD.
DR HPA; ENSG00000099194; Tissue enhanced (adipose tissue, brain, liver).
DR MIM; 604031; gene.
DR neXtProt; NX_O00767; -.
DR OpenTargets; ENSG00000099194; -.
DR PharmGKB; PA34984; -.
DR VEuPathDB; HostDB:ENSG00000099194; -.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000154908; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; O00767; -.
DR OMA; SCGESWH; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; O00767; -.
DR TreeFam; TF313251; -.
DR BRENDA; 1.14.19.1; 2681.
DR PathwayCommons; O00767; -.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis.
DR SignaLink; O00767; -.
DR SIGNOR; O00767; -.
DR BioGRID-ORCS; 6319; 514 hits in 1087 CRISPR screens.
DR ChiTaRS; SCD; human.
DR GeneWiki; Stearoyl-CoA_desaturase-1; -.
DR GenomeRNAi; 6319; -.
DR Pharos; O00767; Tchem.
DR PRO; PR:O00767; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O00767; protein.
DR Bgee; ENSG00000099194; Expressed in inferior vagus X ganglion and 203 other tissues.
DR Genevisible; O00767; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0032896; F:palmitoyl-CoA 9-desaturase activity; IBA:GO_Central.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:UniProtKB.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0070542; P:response to fatty acid; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Stearoyl-CoA desaturase"
FT /id="PRO_0000185395"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26098317"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098317"
FT TOPO_DOM 94..97
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26098317"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098317"
FT TOPO_DOM 119..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26098317"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098317"
FT TOPO_DOM 238..241
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26098317"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098317"
FT TOPO_DOM 264..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26098317"
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 BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098317"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098317"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098317"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098317"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098317"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098317"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098317"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098317"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098317"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 224
FT /note="M -> L (in dbSNP:rs2234970)"
FT /evidence="ECO:0000269|PubMed:10229681,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.7"
FT /id="VAR_025994"
FT CONFLICT 5
FT /note="L -> M (in Ref. 11; AAB30631)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="D -> E (in Ref. 11; AAB30631)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..26
FT /note="SR -> PG (in Ref. 1; CAA73998 and 11; AAB30631)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="F -> C (in Ref. 11; AAB30631)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="H -> L (in Ref. 5; BAD96582)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="T -> N (in Ref. 1; CAA73998)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="C -> W (in Ref. 1; CAA73998)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="A -> T (in Ref. 1; CAA73998)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..359
FT /note="Missing (in Ref. 8; AAH05807)"
FT /evidence="ECO:0000305"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4ZYO"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:4ZYO"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:4ZYO"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:4ZYO"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:4ZYO"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4ZYO"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4ZYO"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:4ZYO"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:4ZYO"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:4ZYO"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:4ZYO"
SQ SEQUENCE 359 AA; 41523 MW; ED56A63DBD850F05 CRC64;
MPAHLLQDDI SSSYTTTTTI TAPPSRVLQN GGDKLETMPL YLEDDIRPDI KDDIYDPTYK
DKEGPSPKVE YVWRNIILMS LLHLGALYGI TLIPTCKFYT WLWGVFYYFV SALGITAGAH
RLWSHRSYKA RLPLRLFLII ANTMAFQNDV YEWARDHRAH HKFSETHADP HNSRRGFFFS
HVGWLLVRKH PAVKEKGSTL DLSDLEAEKL VMFQRRYYKP GLLMMCFILP TLVPWYFWGE
TFQNSVFVAT FLRYAVVLNA TWLVNSAAHL FGYRPYDKNI SPRENILVSL GAVGEGFHNY
HHSFPYDYSA SEYRWHINFT TFFIDCMAAL GLAYDRKKVS KAAILARIKR TGDGNYKSG
