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0NOS1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNOS1
DescriptionNitric-oxide synthase, brain (ec 1.14.13.39) (nos type i) (neuronal nos) (n-nos) (nnos) (constitutive nos) (nc-nos) (bnos).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005624 membrane fraction (TAS)
0004517 nitric-oxide synthase activity (TAS)
0006936 muscle contraction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Nitric oxide synthase () (NOS) enzymes produce nitric oxide (NO) by catalyzing a five-electron oxidation of a guanidino nitrogen of L-arginine (L-Arg). Oxidation of L-Arg to L-citrulline occurs via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine as an intermediate. 2 mol of O(2) and 1.5 mol of NADPH are consumed per mole of NO formed .Arginine-derived NO synthesis has been identified in mammals.ish.irds.nvertebrates.lants.nd bacteria . Best studied are mammals.here three distinct genes encode NOS isozymes: neuronal (nNOS or NOS-1).ytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . iNOS and nNOS are soluble and found predominantly in the cytosol.hile eNOS is membrane associated. The enzymes exist as homodimers.ach monomer consisting of two major domains: an N-terminal oxygenase domain.hich belongs to the class of heme-thiolate proteins.nd a C-terminal reductase domain.hich is homologous to NADPH:P450 reductase (). The interdomain linker between the oxygenase and reductase domains contains a calmodulin (CaM)-binding sequence. NOSs are the only enzymes known to simultaneously require five bound cofactors animal NOS isozymes are catalytically self-sufficient. The electron flow in the NO synthase reaction is: NADPH --> FAD --> FMN --> heme --> O(2).eNOS localisation to endothelial membranes is mediated by cotranslational N-terminal myristoylation and post-translational palmitoylation . The subcellular localisation of nNOS in skeletal muscle ismediated by anchoring of nNOS to dystrophin. nNOS contains an additional N-terminal domain.he PDZ domain . Some bacteria.ike Bacillus halodurans.acillus subtilis or Deinococcus radiodurans.ontain homologs of NOS oxygenase domain. The pattern is directed against the N-terminal heme binding site.
  IPR004030:Nitric oxide synthase, NOS
Flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin:NADP+reductases (FNR) .lant and fungal NAD(P)H:nitrate reductases NADH:cytochrome b5 reductases .ADPH:P450 reductases .ADPH:sulphite reductases .itric oxide synthases .hthalate dioxygenase reductase .nd various other flavoproteins.
  IPR003097:FAD-binding
This domain is found in a number of proteins including flavodoxin and nitric-oxide synthase. Flavodoxins are electron-transfer proteins that function in various electron transport systems. They bind one FMN molecule.hich serves as aredox-active prosthetic group and are functionally interchangeable with ferredoxins. They have been isolated from prokaryotes.yanobacteria.nd some eukaryotic algae. Nitric oxide synthase () produces nitric oxide from L-arginie and NADPH. Nitric oxide acts as a messenger molecule in the body.
  IPR008254:Flavodoxin/nitric oxide synthase
Bacterial ferredoxin-NADP+ reductase may be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes.Chloroplast ferredoxin-NADP+ reductase () may play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. It is involved in the final step in the linear photosynthetic electron transport chain and has also been implicated in cyclic electron flow around photosystem I where its role would be to return electrons from ferredoxin to the cytochrome B-F complex.This domain is present in a variety of proteins that include.acterial flavohemoprotein.ammalian NADH-cytochrome b5 reductase.ukaryotic NADPH-cytochrome P450 reductase.itrate reductase from plants.itric-oxide synthase.acterial vanillate demethylase and others.
  IPR001433:Oxidoreductase FAD/NAD(P)-binding
PDZ domains are found in diverse signaling proteins in bacteria.easts.lants.nsects and vertebrates . PDZ domains can occur in one or multiple copies and are nearly always found in cytoplasmic proteins. They bind either the carboxyl-terminal sequences of proteins or internal peptide sequences . In most cases.nteraction between a PDZ domain and its target is constitutive.ith a binding affinity of 1 to 10 ┬ÁM. However.gonist-dependent activation of cell surface receptors is sometimes required to promote interaction with a PDZ protein. PDZ domain proteins are frequently associated with the plasma membrane. compartment where high concentrations of phosphatidylinositol 4.-bisphosphate (PIP2) are found. Direct interaction between PIP2 and a subset of class II PDZ domains (syntenin.ASK.iam-1) has been demonstrated. PDZ domains consist of 80 to 90 amino acids comprising six beta-strands (betaA to betaF) and two alpha-helices. and B.ompactly arranged in a globular structure. Peptide binding of the ligand takes place in an elongated surface groove as an antiparallel beta-strand interacts with the betaB strand and the B helix. The structure of PDZ domains allows binding to a free carboxylate group at the end of a peptide through a carboxylate-binding loop between the betaA and betaB strands.
  IPR001478:PDZ/DHR/GLGF
Flavodoxins act in various electron-transport systems as functionalanalogues of ferredoxins . Although flavodoxins are found onlyin certain bacteria and algae the proteins share similaritywith a number of protein domains of both prokaryotic and eukaryotic origin .
  IPR001094:Flavodoxin-like
Flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin:NADP+reductases (FNR) .lant and fungal NAD(P)H:nitrate reductases NADH:cytochrome b5 reductases .ADPH:P450 reductases .ADPH:sulphite reductases .itric oxide synthases .hthalate dioxygenase reductase .nd various other flavoproteins.Despite functional similarities.PNCRs show no sequence similarity to NADPH:adrenodoxin reductases .or to bacterial ferredoxin:NAD+reductases and their homologues . To date.D-structures of 4 members of the family have been solved: Spinacia oleracea (spinach) ferredoxin:NADP+ reductase ; Pseudomonas cepacia phthalate dioxygenase reductase ; the flavoprotein domain of Zea mays (corn) nitrate reductase ; and Sus scrofa (pig) NADH:cytochrome b5 reductase . In all of them.he FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel.hile the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet with 2 helices on each side) . In spite of such structural similarities.he level of amino acid identity between family members is at or below the limit of significance (e.g..itrate reductase is only 15% identical to FNR) .
  IPR001709:Flavoprotein pyridine nucleotide cytochrome reductase
Nitric oxide synthase () (NOS) enzymes produce nitric oxide (NO) by catalyzing a five-electron oxidation of a guanidino nitrogen of L-arginine (L-Arg). Oxidation of L-Arg to L-citrulline occurs via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine as an intermediate. 2 mol of O(2) and 1.5 mol of NADPH are consumed per mole of NO formed .Arginine-derived NO synthesis has been identified in mammals.ish.irds.nvertebrates.lants.nd bacteria . Best studied are mammals.here three distinct genes encode NOS isozymes: neuronal (nNOS or NOS-1).ytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . iNOS and nNOS are soluble and found predominantly in the cytosol.hile eNOS is membrane associated. The enzymes exist as homodimers.ach monomer consisting of two major domains: an N-terminal oxygenase domain.hich belongs to the class of heme-thiolate proteins.nd a C-terminal reductase domain.hich is homologous to NADPH:P450 reductase (). The interdomain linker between the oxygenase and reductase domains contains a calmodulin (CaM)-binding sequence. NOSs are the only enzymes known to simultaneously require five bound cofactors animal NOS isozymes are catalytically self-sufficient. The electron flow in the NO synthase reaction is: NADPH --> FAD --> FMN --> heme --> O(2).eNOS localisation to endothelial membranes is mediated by cotranslational N-terminal myristoylation and post-translational palmitoylation . The subcellular localisation of nNOS in skeletal muscle is mediated by anchoring of nNOS to dystrophin. nNOS contains an additional N-terminal domain.he PDZ domain .This entry represents all forms of NOS found in metazoa. For further information see .
  IPR012144:Nitric-oxide synthase
IPR004030:NO_synthase 
Evalue:-1e+125 
Location:351-722IPR003097:FAD_binding_1 
Evalue:-130.301025390625 
Location:990-1219IPR008254:Flavodoxin_1 
Evalue:-52.040958404541 
Location:762-935IPR001433:NAD_binding_1 
Evalue:-34.2006607055664 
Location:1250-1365IPR001478:PDZ 
Evalue:-23.2218494415283 
Location:17-96
SequencesProtein: NOS1_HUMAN (1434 aa)
mRNA: NM_000620
Local Annotation
Synapse Ontology
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentK00491
  Level 3 annotation:
    nitric-oxide synthase
  Level 2 annotation:
    Arginine and proline metabolism
    Calcium signaling pathway
    Long-term depression
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 718 residues, 116135361-116137512Exon2: 41 residues, 116140233-116140352Exon3: 67 residues, 116142262-116142457Exon4: 51 residues, 116144902-116145051Exon5: 42 residues, 116147203-116147325Exon6: 31 residues, 116148870-116148958Exon7: 72 residues, 116149618-116149829Exon8: 58 residues, 116154149-116154319Exon9: 66 residues, 116156752-116156946Exon10: 28 residues, 116164814-116164893Exon11: 48 residues, 116165484-116165623Exon12: 60 residues, 116169535-116169710Exon13: 41 residues, 116175825-116175942Exon14: 21 residues, 116180584-116180643Exon15: 37 residues, 116181213-116181318Exon16: 50 residues, 116182652-116182797Exon17: 30 residues, 116186076-116186162Exon18: 67 residues, 116187503-116187698Exon19: 36 residues, 116190230-116190332Exon20: 60 residues, 116194572-116194747Exon21: 48 residues, 116200146-116200286Exon22: 49 residues, 116202912-116203054Exon23: 32 residues, 116207428-116207520Exon24: 56 residues, 116208291-116208454Exon25: 50 residues, 116210261-116210407Exon26: 45 residues, 116212485-116212614Exon27: 44 residues, 116233653-116233780Exon28: 383 residues, 116252532-116253677Exon29: 90 residues, 116283699-116283965Exon30: 2 residues, -Jump to NOS1_HUMAN  
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