ID NOS3_MOUSE Reviewed; 1202 AA. AC P70313; O55056; Q7TSV7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 24-JAN-2024, entry version 219. DE RecName: Full=Nitric oxide synthase 3 {ECO:0000312|MGI:MGI:97362}; DE EC=1.14.13.39 {ECO:0000250|UniProtKB:P29474}; DE AltName: Full=Constitutive NOS; DE Short=cNOS; DE AltName: Full=EC-NOS; DE AltName: Full=NOS type III; DE Short=NOSIII; DE AltName: Full=Nitric oxide synthase, endothelial {ECO:0000305}; DE Short=Endothelial NOS {ECO:0000305}; DE Short=eNOS {ECO:0000305}; GN Name=Nos3 {ECO:0000312|MGI:MGI:97362}; Synonyms=Ecnos; 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=Fetal heart; RX PubMed=8764825; DOI=10.1016/0167-4781(96)00098-x; RA Gnanapandithen K., Chen Z., Kau C.-L., Gorczynski R.M., Marsden P.A.; RT "Cloning and characterization of murine endothelial constitutive nitric RT oxide synthase."; RL Biochim. Biophys. Acta 1308:103-106(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54, AND FUNCTION. RX PubMed=9843834; DOI=10.1152/ajpheart.1998.275.6.h2319; RA Gregg A.R., Schauer A., Shi O., Liu Z., Lee C.G.L., O'Brien W.E.; RT "Limb reduction defects in endothelial nitric oxide synthase-deficient RT mice."; RL Am. J. Physiol. 275:H2319-H2324(1998). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1174, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614; THR-1174; SER-1176 AND RP SER-1178, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP INTERACTION WITH ASL; ASS1 AND SLC7A1. RX PubMed=22081021; DOI=10.1038/nm.2544; RA Erez A., Nagamani S.C., Shchelochkov O.A., Premkumar M.H., Campeau P.M., RA Chen Y., Garg H.K., Li L., Mian A., Bertin T.K., Black J.O., Zeng H., RA Tang Y., Reddy A.K., Summar M., O'Brien W.E., Harrison D.G., Mitch W.E., RA Marini J.C., Aschner J.L., Bryan N.S., Lee B.; RT "Requirement of argininosuccinate lyase for systemic nitric oxide RT production."; RL Nat. Med. 17:1619-1626(2011). CC -!- FUNCTION: Produces nitric oxide (NO) which is implicated in vascular CC smooth muscle relaxation through a cGMP-mediated signal transduction CC pathway. NO mediates vascular endothelial growth factor (VEGF)-induced CC angiogenesis in coronary vessels and promotes blood clotting through CC the activation of platelets. May play a significant role in normal and CC abnormal limb development. {ECO:0000269|PubMed:9843834}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline CC + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; CC Evidence={ECO:0000250|UniProtKB:P29474}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898; CC Evidence={ECO:0000250|UniProtKB:P29474}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000250|UniProtKB:P29474}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P29476}; CC Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000250|UniProtKB:P35228}; CC Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P35228}; CC -!- COFACTOR: CC Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P35228}; CC Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the CC enzyme. {ECO:0000250|UniProtKB:P35228}; CC -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin. Inhibited by CC NOSIP and NOSTRIN (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By similarity). CC Interacts with HSP90AB1 (By similarity). Forms a complex with ASL, ASS1 CC and SLC7A1; the complex regulates cell-autonomous L-arginine synthesis CC and citrulline recycling while channeling extracellular L-arginine to CC nitric oxide synthesis pathway. {ECO:0000250|UniProtKB:P29474, CC ECO:0000269|PubMed:22081021}. CC -!- SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000250}. Cytoplasm, CC cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell CC membrane {ECO:0000250}. Note=Specifically associates with actin CC cytoskeleton in the G2 phase of the cell cycle, which is favored by CC interaction with NOSIP and results in a reduced enzymatic activity. CC {ECO:0000250}. CC -!- PTM: Phosphorylation by AMPK at Ser-1176 in the presence of Ca(2+)- CC calmodulin (CaM) activates activity. In absence of Ca(2+)-calmodulin, CC AMPK also phosphorylates Thr-494, resulting in inhibition of activity CC (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NOS family. {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; U53142; AAC52766.1; -; mRNA. DR EMBL; BC052636; AAH52636.1; -; mRNA. DR EMBL; AF045940; AAC02553.1; -; Genomic_DNA. DR CCDS; CCDS19117.1; -. DR PIR; S71424; S71424. DR RefSeq; NP_032739.3; NM_008713.4. DR AlphaFoldDB; P70313; -. DR BMRB; P70313; -. DR SMR; P70313; -. DR BioGRID; 201807; 11. DR DIP; DIP-31086N; -. DR IntAct; P70313; 3. DR STRING; 10090.ENSMUSP00000030834; -. DR BindingDB; P70313; -. DR ChEMBL; CHEMBL2643; -. DR GlyGen; P70313; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P70313; -. DR PhosphoSitePlus; P70313; -. DR SwissPalm; P70313; -. DR jPOST; P70313; -. DR MaxQB; P70313; -. DR PaxDb; 10090-ENSMUSP00000030834; -. DR ProteomicsDB; 293676; -. DR Antibodypedia; 3692; 1917 antibodies from 44 providers. DR DNASU; 18127; -. DR Ensembl; ENSMUST00000030834.7; ENSMUSP00000030834.5; ENSMUSG00000028978.13. DR GeneID; 18127; -. DR KEGG; mmu:18127; -. DR UCSC; uc008wrd.2; mouse. DR AGR; MGI:97362; -. DR CTD; 4846; -. DR MGI; MGI:97362; Nos3. DR VEuPathDB; HostDB:ENSMUSG00000028978; -. DR eggNOG; KOG1158; Eukaryota. DR GeneTree; ENSGT00940000161389; -. DR InParanoid; P70313; -. DR OMA; KGDFRIW; -. DR OrthoDB; 276396at2759; -. DR PhylomeDB; P70313; -. DR TreeFam; TF324410; -. DR BRENDA; 1.14.13.39; 3474. DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes. DR Reactome; R-MMU-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation. DR Reactome; R-MMU-203615; eNOS activation. DR Reactome; R-MMU-203641; NOSTRIN mediated eNOS trafficking. DR Reactome; R-MMU-203754; NOSIP mediated eNOS trafficking. DR Reactome; R-MMU-392154; Nitric oxide stimulates guanylate cyclase. DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR BioGRID-ORCS; 18127; 3 hits in 79 CRISPR screens. DR PRO; PR:P70313; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P70313; Protein. DR Bgee; ENSMUSG00000028978; Expressed in brain blood vessel and 191 other cell types or tissues. DR ExpressionAtlas; P70313; baseline and differential. DR GO; GO:0045177; C:apical part of cell; ISO:MGI. DR GO; GO:0005901; C:caveola; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0042383; C:sarcolemma; ISO:MGI. DR GO; GO:0003779; F:actin binding; ISO:MGI. DR GO; GO:0003785; F:actin monomer binding; ISO:MGI. DR GO; GO:0034618; F:arginine binding; ISO:MGI. DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI. DR GO; GO:0045296; F:cadherin binding; ISO:MGI. DR GO; GO:0005516; F:calmodulin binding; ISO:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; ISO:MGI. DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004517; F:nitric-oxide synthase activity; IMP:MGI. DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI. DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL. DR GO; GO:0034617; F:tetrahydrobiopterin binding; ISO:MGI. DR GO; GO:0001525; P:angiogenesis; IMP:MGI. DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL. DR GO; GO:0006527; P:arginine catabolic process; ISO:MGI. DR GO; GO:0097746; P:blood vessel diameter maintenance; IMP:BHF-UCL. DR GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL. DR GO; GO:0006816; P:calcium ion transport; IMP:MGI. DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI. DR GO; GO:0003203; P:endocardial cushion morphogenesis; IGI:BHF-UCL. DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI. DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI. DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:BHF-UCL. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0070168; P:negative regulation of biomineral tissue development; IMP:BHF-UCL. DR GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central. DR GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL. DR GO; GO:0014740; P:negative regulation of muscle hyperplasia; IMP:BHF-UCL. DR GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:MGI. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:MGI. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI. DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central. DR GO; GO:0001542; P:ovulation from ovarian follicle; IMP:MGI. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL. DR GO; GO:0006813; P:potassium ion transport; IMP:MGI. DR GO; GO:0003184; P:pulmonary valve morphogenesis; IGI:BHF-UCL. DR GO; GO:0031644; P:regulation of nervous system process; IGI:ARUK-UCL. DR GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI. DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; ISO:MGI. DR GO; GO:0003057; P:regulation of the force of heart contraction by chemical signal; IGI:MGI. DR GO; GO:0019430; P:removal of superoxide radicals; ISO:MGI. DR GO; GO:0032355; P:response to estradiol; ISO:MGI. DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl. DR GO; GO:0009725; P:response to hormone; IBA:GO_Central. DR GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central. DR GO; GO:0014806; P:smooth muscle hyperplasia; IMP:BHF-UCL. DR GO; GO:0060412; P:ventricular septum morphogenesis; IGI:BHF-UCL. DR CDD; cd00795; NOS_oxygenase_euk; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR003097; CysJ-like_FAD-binding. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha. DR InterPro; IPR044943; NOS_dom_1. DR InterPro; IPR044940; NOS_dom_2. DR InterPro; IPR044944; NOS_dom_3. DR InterPro; IPR012144; NOS_euk. DR InterPro; IPR004030; NOS_N. DR InterPro; IPR036119; NOS_N_sf. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1. DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF02898; NO_synthase; 1. DR PIRSF; PIRSF000333; NOS; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. DR Genevisible; P70313; MM. PE 1: Evidence at protein level; KW Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; FAD; KW Flavoprotein; FMN; Golgi apparatus; Heme; Iron; Lipoprotein; Membrane; KW Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P29473" FT CHAIN 2..1202 FT /note="Nitric oxide synthase 3" FT /id="PRO_0000170944" FT DOMAIN 519..702 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088" FT DOMAIN 755..1001 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 1..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 97..485 FT /note="Interaction with NOSIP" FT /evidence="ECO:0000250" FT REGION 490..509 FT /note="Calmodulin-binding" FT /evidence="ECO:0000255" FT REGION 817..843 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 35..64 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between homodimeric partners" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between homodimeric partners" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 101 FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin" FT /ligand_id="ChEBI:CHEBI:59560" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 183 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 246 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 355 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 356 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 360 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 445 FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin" FT /ligand_id="ChEBI:CHEBI:59560" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 446 FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin" FT /ligand_id="ChEBI:CHEBI:59560" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 459 FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin" FT /ligand_id="ChEBI:CHEBI:59560" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 474 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 525 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 526 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 527 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 529 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 571 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 572 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 653 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 660 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 686 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 690 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:P35228" FT BINDING 775 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 797 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 937 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 939 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 940 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 955 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 957 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 961 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 974 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 975 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 976 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 1015 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 1048 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 1077 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 1078 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 1084 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 1086 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT BINDING 1088 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29476" FT MOD_RES 494 FT /note="Phosphothreonine; by AMPK" FT /evidence="ECO:0000250|UniProtKB:P29473" FT MOD_RES 614 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 632 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P29473" FT MOD_RES 637 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P29474" FT MOD_RES 835 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P29474" FT MOD_RES 1174 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1176 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000305, ECO:0007744|PubMed:21183079" FT MOD_RES 1178 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250" FT LIPID 15 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 26 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CONFLICT 50 FT /note="P -> A (in Ref. 1; AAC52766)" FT /evidence="ECO:0000305" FT CONFLICT 298 FT /note="P -> S (in Ref. 1; AAC52766)" FT /evidence="ECO:0000305" SQ SEQUENCE 1202 AA; 132916 MW; E1F65C43601F0937 CRC64; MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSQ APAPPSPTRP APDHSPPLTR PPDGPRFPRV KNWEVGSITY DTLSAQAQQD GPCTSRRCLG SLVFPRKLQS RPTQGPSPTE QLLGQARDFI NQYYNSIKRS GSQAHEQRLQ EVEAEVAATG TYQLRESELV FGAKQAWRNA PRCVGRIQWG KLQVFDARDC RTAQEMFTYI CNHIKYATNR GNLRSAITVF PQRCPGRGDF RIWNSQLIRY AGYRQQDGSV RGDPANVEIT ELCIQHGWTP GNGRFDVLPL LLQAPDEPPE LFTLPPEMVL EVPLEHPTLE WFAALGLRWY ALPAVSNMLL EIGGLEFPAA PFSGWYMSSE IGMRDLCDPH RYNILEDVAV CMDLDTRTTS SLWKDKAAVE INVAVLHSYQ LAKVTIVDHH AATASFMKHL ENEQKARGGC PADWAWIVPP ISGSLTPVFH QEMVNYFLSP AFRYQPDPWK GSAAKGAGIT RKKTFKEVAN AVKISASLMG TVMAKRVKAT ILYGSETGRA QSYAQQLGRL FRKAFDPRVL CMDEYDVVSL EHEALVLVVT STFGNGDPPE NGESFAAALM EMSGPYNSSP RPEQHKSYKI RFNSVSCSDP LVSSWRRKRK ESSNTDSAGA LGTLRFCVFG LGSRAYPHFC AFARAVDTRL EELGGERLLQ LGQGDELCGQ EEAFRGWAQA AFQAACETFC VGEDAKAAAR DIFSPKRSWK RQRYRLSTQA ESLQLLPGLT HVHRRKMFQA TILSVENLQS SKSTRATILV RLDTGGQEGL QYQPGDHIGV CPPNRPGLVE ALLSRVEDPP PSTEPVAVEQ LEKGSPGGPP PGWVRDPRLP PCTLRQALTY FLDITSPPSP RLLRLLSTLA EESSEQQELE ALSQDPRRYE EWKWFSCPTL LEVLEQFPSV ALPAPLILTQ LPLLQPRYYS VSSAPSAHPG EIHLTIAVLA YRTQDGLGPL HYGVCSTWMS QLKAGDPVPC FIRGAPSFRL PPDPNLPCIL VGPGTGIAPF RGFWQDRLHD IEIKGLQPAP MTLVFGCRCS QLDHLYRDEV LDAQQRGVFG QVLTAFSRDP GSPKTYVQDL LRTELAAEVH RVLCLEQGHM FVCGDVTMAT SVLQTVQRIL ATEGGMELDE AGDVIGVLRD QQRYHEDIFG LTLRTQEVTS RIRTQSFSLQ ERQLRGAVPW SFDPPGPEIP GS //