ID ACOD_HUMAN Reviewed; 359 AA. AC O00767; B2R5U0; D3DR68; Q16150; Q53GR9; Q5W037; Q5W038; Q6GSS4; AC Q96KF6; Q9BS07; Q9Y695; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 11-NOV-2015, entry version 153. DE RecName: Full=Acyl-CoA desaturase; DE EC=1.14.19.1 {ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284}; DE AltName: Full=Delta(9)-desaturase; DE Short=Delta-9 desaturase; DE AltName: Full=Fatty acid desaturase; DE AltName: Full=Stearoyl-CoA desaturase {ECO:0000303|PubMed:18765284}; DE Short=hSCD1 {ECO:0000303|PubMed:15907797}; GN Name=SCD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT human 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=10.1042/0264-6021:3400255; RA Zhang L., Ge L., Parimoo S., Stenn K., Prouty S.M.; RT "Human stearoyl-CoA desaturase: alternative transcripts generated from RT a 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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT gene 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 RT labeling of 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 RT and changes in its mRNA expression in some normal and malignant RT tissues."; RL Int. J. Cancer 57:348-352(1994). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE RP 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 RT unique to 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 RT improved stability and enzyme activity by cross-linking in intact RT cells."; RL Biochem. J. 388:135-142(2005). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION RP BY 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 RT the 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., RA Buerckstuemmer T., 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] 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., RA Sang B.C.; RT "Crystal structure of human stearoyl-coenzyme A desaturase in complex RT with substrate."; RL Nat. Struct. Mol. Biol. 22:581-585(2015). CC -!- FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons CC from reduced cytochrome b5 to introduce the first double bond into CC saturated fatty acyl-CoA substrates (PubMed:15907797, CC PubMed:18765284). Catalyzes the insertion of a cis double bond at CC the delta-9 position into fatty acyl-CoA substrates including CC palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:18765284). CC Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids CC (PubMed:15610069). Plays an important role in lipid biosynthesis. CC Plays an important role in regulating the expression of genes that CC are involved in lipogenesis and in regulating mitochondrial fatty CC acid oxidation (By similarity). Plays an important role in body CC 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: Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 CC H(+) = oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O. CC {ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, CC ECO:0000269|PubMed:18765284}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000269|PubMed:18765284, CC ECO:0000305|PubMed:26098317}; CC Note=Expected to bind 2 Fe(2+) ions per subunit, instead of the CC Zn(2+) ions seen in the 3D-structure. CC {ECO:0000305|PubMed:26098317}; CC -!- SUBUNIT: May self-associate and form homodimers. CC {ECO:0000269|PubMed:15610069}. 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. CC Highly expressed in adult adipose tissue, and at lower levels in CC adult brain and lung. {ECO:0000269|PubMed:15907797}. CC -!- DOMAIN: The histidine box domains are involved in binding the CC catalytic metal ions. {ECO:0000269|PubMed:26098317}. CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CAH72823.1; -; Genomic_DNA. DR EMBL; AL139819; CAH72824.1; -; 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 UniGene; Hs.558396; -. DR PDB; 4ZYO; X-ray; 3.25 A; A=45-359. DR PDBsum; 4ZYO; -. DR ProteinModelPortal; O00767; -. DR SMR; O00767; 53-350. DR BioGrid; 112225; 5. DR IntAct; O00767; 2. DR MINT; MINT-2997962; -. DR STRING; 9606.ENSP00000359380; -. DR ChEMBL; CHEMBL5555; -. DR PhosphoSite; O00767; -. DR BioMuta; SCD; -. DR MaxQB; O00767; -. DR PaxDb; O00767; -. DR PRIDE; O00767; -. DR Ensembl; ENST00000370355; ENSP00000359380; ENSG00000099194. DR GeneID; 6319; -. DR KEGG; hsa:6319; -. DR UCSC; uc001kqy.3; human. DR CTD; 6319; -. DR GeneCards; SCD; -. DR H-InvDB; HIX0009123; -. DR HGNC; HGNC:10571; SCD. DR HPA; HPA012107; -. DR MIM; 604031; gene. DR neXtProt; NX_O00767; -. DR PharmGKB; PA34984; -. DR eggNOG; KOG1600; Eukaryota. DR eggNOG; COG1398; LUCA. DR GeneTree; ENSGT00530000063158; -. DR HOVERGEN; HBG003367; -. DR InParanoid; O00767; -. DR KO; K00507; -. DR OMA; LIPTCKF; -. DR OrthoDB; EOG7ZPNKS; -. DR PhylomeDB; O00767; -. DR TreeFam; TF313251; -. DR BRENDA; 1.14.19.1; 2681. DR ChiTaRS; SCD; human. DR GeneWiki; Stearoyl-CoA_desaturase-1; -. DR GenomeRNAi; 6319; -. DR NextBio; 24520; -. DR PRO; PR:O00767; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; O00767; -. 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:0016021; C:integral component of membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:UniProtKB. DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB. DR InterPro; IPR001522; Fatty_acid_desaturase-1_C. DR InterPro; IPR015876; Fatty_acid_desaturase-1_core. DR PRINTS; PR00075; FACDDSATRASE. DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; KW Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 359 Acyl-CoA desaturase. FT /FTId=PRO_0000185395. FT TOPO_DOM 1 72 Cytoplasmic. FT {ECO:0000305|PubMed:26098317}. FT TRANSMEM 73 93 Helical. {ECO:0000269|PubMed:26098317}. FT TOPO_DOM 94 97 Lumenal. {ECO:0000305|PubMed:26098317}. FT TRANSMEM 98 118 Helical. {ECO:0000269|PubMed:26098317}. FT TOPO_DOM 119 217 Cytoplasmic. FT {ECO:0000305|PubMed:26098317}. FT TRANSMEM 218 237 Helical. {ECO:0000269|PubMed:26098317}. FT TOPO_DOM 238 241 Lumenal. {ECO:0000305|PubMed:26098317}. FT TRANSMEM 242 263 Helical. {ECO:0000269|PubMed:26098317}. FT TOPO_DOM 264 359 Cytoplasmic. FT {ECO:0000305|PubMed:26098317}. FT MOTIF 120 125 Histidine box-1. {ECO:0000305}. FT MOTIF 157 161 Histidine box-2. {ECO:0000305}. FT MOTIF 298 302 Histidine box-3. {ECO:0000305}. FT METAL 120 120 Iron 1. {ECO:0000305|PubMed:26098317}. FT METAL 125 125 Iron 1. {ECO:0000305|PubMed:26098317}. FT METAL 157 157 Iron 1. {ECO:0000305|PubMed:26098317}. FT METAL 160 160 Iron 2. {ECO:0000305|PubMed:26098317}. FT METAL 161 161 Iron 1. {ECO:0000305|PubMed:26098317}. FT METAL 269 269 Iron 2. {ECO:0000305|PubMed:26098317}. FT METAL 298 298 Iron 2. {ECO:0000305|PubMed:26098317}. FT METAL 301 301 Iron 1. {ECO:0000305|PubMed:26098317}. FT METAL 302 302 Iron 2. {ECO:0000305|PubMed:26098317}. FT BINDING 75 75 Substrate. {ECO:0000269|PubMed:26098317}. FT BINDING 148 148 Substrate. {ECO:0000269|PubMed:26098317}. FT BINDING 155 155 Substrate. {ECO:0000269|PubMed:26098317}. FT BINDING 156 156 Substrate. {ECO:0000269|PubMed:26098317}. FT BINDING 188 188 Substrate. {ECO:0000269|PubMed:26098317}. FT BINDING 189 189 Substrate. {ECO:0000269|PubMed:26098317}. FT BINDING 262 262 Substrate. {ECO:0000269|PubMed:26098317}. FT MOD_RES 203 203 Phosphoserine. FT {ECO:0000244|PubMed:18691976}. FT VARIANT 224 224 M -> L (in dbSNP:rs2234970). FT {ECO:0000269|PubMed:10229681, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.3, ECO:0000269|Ref.7}. FT /FTId=VAR_025994. FT CONFLICT 5 5 L -> M (in Ref. 11; AAB30631). FT {ECO:0000305}. FT CONFLICT 8 8 D -> E (in Ref. 11; AAB30631). FT {ECO:0000305}. FT CONFLICT 25 26 SR -> PG (in Ref. 1; CAA73998 and 11; FT AAB30631). {ECO:0000305}. FT CONFLICT 237 237 F -> C (in Ref. 11; AAB30631). FT {ECO:0000305}. FT CONFLICT 269 269 H -> L (in Ref. 5; BAD96582). FT {ECO:0000305}. FT CONFLICT 320 320 T -> N (in Ref. 1; CAA73998). FT {ECO:0000305}. FT CONFLICT 326 326 C -> W (in Ref. 1; CAA73998). FT {ECO:0000305}. FT CONFLICT 333 333 A -> T (in Ref. 1; CAA73998). FT {ECO:0000305}. FT CONFLICT 356 359 Missing (in Ref. 8; AAH05807). FT {ECO:0000305}. FT HELIX 57 59 {ECO:0000244|PDB:4ZYO}. FT STRAND 63 65 {ECO:0000244|PDB:4ZYO}. FT HELIX 73 91 {ECO:0000244|PDB:4ZYO}. FT TURN 92 95 {ECO:0000244|PDB:4ZYO}. FT HELIX 98 115 {ECO:0000244|PDB:4ZYO}. FT HELIX 116 124 {ECO:0000244|PDB:4ZYO}. FT HELIX 132 144 {ECO:0000244|PDB:4ZYO}. FT HELIX 150 162 {ECO:0000244|PDB:4ZYO}. FT TURN 163 165 {ECO:0000244|PDB:4ZYO}. FT HELIX 173 175 {ECO:0000244|PDB:4ZYO}. FT HELIX 177 181 {ECO:0000244|PDB:4ZYO}. FT HELIX 183 185 {ECO:0000244|PDB:4ZYO}. FT HELIX 192 196 {ECO:0000244|PDB:4ZYO}. FT HELIX 203 206 {ECO:0000244|PDB:4ZYO}. FT HELIX 209 216 {ECO:0000244|PDB:4ZYO}. FT HELIX 218 226 {ECO:0000244|PDB:4ZYO}. FT HELIX 228 237 {ECO:0000244|PDB:4ZYO}. FT HELIX 242 247 {ECO:0000244|PDB:4ZYO}. FT TURN 248 250 {ECO:0000244|PDB:4ZYO}. FT HELIX 251 262 {ECO:0000244|PDB:4ZYO}. FT TURN 263 266 {ECO:0000244|PDB:4ZYO}. FT HELIX 267 269 {ECO:0000244|PDB:4ZYO}. FT STRAND 271 273 {ECO:0000244|PDB:4ZYO}. FT STRAND 278 280 {ECO:0000244|PDB:4ZYO}. FT HELIX 286 291 {ECO:0000244|PDB:4ZYO}. FT STRAND 292 294 {ECO:0000244|PDB:4ZYO}. FT HELIX 298 303 {ECO:0000244|PDB:4ZYO}. FT STRAND 308 313 {ECO:0000244|PDB:4ZYO}. FT HELIX 319 329 {ECO:0000244|PDB:4ZYO}. FT HELIX 341 346 {ECO:0000244|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 //