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Entry version 201 (16 Jan 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Stimulated by calcium/calmodulin. Inhibited by NOSIP and NOSTRIN (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi96Zinc1
Metal bindingi101Zinc1
Metal bindingi186Iron (heme axial ligand)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi651 – 682FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi795 – 806FADBy similarityAdd BLAST12
Nucleotide bindingi937 – 947FADBy similarityAdd BLAST11
Nucleotide bindingi1012 – 1030NADPBy similarityAdd BLAST19
Nucleotide bindingi1110 – 1125NADPBy similarityAdd BLAST16

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalmodulin-binding, Oxidoreductase
Biological processBlood coagulation, Hemostasis
LigandCalcium, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.13.39 908

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Nitric oxide synthase, endothelial (EC:1.14.13.39)
Alternative name(s):
Constitutive NOS
Short name:
cNOS
EC-NOS
Endothelial NOS
Short name:
eNOS
NOS type III
Short name:
NOSIII
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NOS3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4802

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001709412 – 1205Nitric oxide synthase, endothelialAdd BLAST1204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi15S-palmitoyl cysteine1 Publication1
Lipidationi26S-palmitoyl cysteine1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei116Phosphoserine; by CDK5By similarity1
Modified residuei497Phosphothreonine; by AMPK and PKA1 Publication1
Modified residuei617PhosphoserineBy similarity1
Modified residuei635Phosphoserine1 Publication1
Modified residuei640PhosphoserineBy similarity1
Modified residuei838PhosphoserineBy similarity1
Modified residuei1177PhosphothreonineBy similarity1
Modified residuei1179Phosphoserine; by AMPK, PDPK1 and PKA1 Publication1
Modified residuei1181PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation by AMPK at Ser-1179 in the presence of Ca2+-calmodulin (CaM) activates activity. In absence of Ca2+-calmodulin, AMPK also phosphorylates Thr-497, resulting in inhibition of activity. Phosphorylation of Ser-116 by CDK5 reduces activity (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P29473

PRoteomics IDEntifications database

More...
PRIDEi
P29473

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P29473

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P29473

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Interacts with NOSIP and NOSTRIN (By similarity). Interacts with HSP90AB1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-42217N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P29473

Protein interaction database and analysis system

More...
IntActi
P29473, 2 interactors

Molecular INTeraction database

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MINTi
P29473

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000023515

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P29473

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D0CX-ray1.65A/B39-482[»]
1D0OX-ray1.95A/B39-482[»]
1D1VX-ray1.93A/B39-482[»]
1D1WX-ray2.00A/B39-482[»]
1D1XX-ray2.00A/B39-482[»]
1D1YX-ray2.20A/B39-482[»]
1DM6X-ray1.95A/B39-482[»]
1DM7X-ray2.10A/B39-482[»]
1DM8X-ray2.25A/B39-482[»]
1DMIX-ray2.00A/B39-482[»]
1DMJX-ray2.35A/B39-482[»]
1DMKX-ray1.90A/B39-482[»]
1ED4X-ray1.86A/B39-482[»]
1ED5X-ray1.80A/B39-482[»]
1ED6X-ray2.05A/B39-482[»]
1FOIX-ray1.93A/B39-482[»]
1FOJX-ray2.10A/B39-482[»]
1FOLX-ray2.20A/B39-482[»]
1FOOX-ray2.00A/B39-482[»]
1FOPX-ray2.30A/B39-482[»]
1I83X-ray2.00A/B39-482[»]
1NSEX-ray1.90A/B39-482[»]
1P6LX-ray2.35A/B67-483[»]
1P6MX-ray2.27A/B67-483[»]
1P6NX-ray2.50A/B67-483[»]
1Q2OX-ray1.74A/B67-482[»]
1RS8X-ray2.30A/B67-482[»]
1RS9X-ray2.22A/B67-482[»]
1ZZSX-ray1.85A/B67-482[»]
1ZZTX-ray2.14A/B67-482[»]
2G6OX-ray1.90A/B67-482[»]
2HX2X-ray1.95A/B67-482[»]
2NSEX-ray2.34A/B39-482[»]
3DQSX-ray2.03A/B67-482[»]
3DQTX-ray2.54A/B67-482[»]
3E7SX-ray2.50A/B57-487[»]
3JWWX-ray2.20A/B39-482[»]
3JWXX-ray2.00A/B39-482[»]
3JWYX-ray2.24A/B39-482[»]
3JWZX-ray2.40A/B39-482[»]
3N5PX-ray2.39A/B39-482[»]
3N5QX-ray2.90A/B39-482[»]
3N5RX-ray2.57A/B39-482[»]
3N5SX-ray2.18A/B39-482[»]
3N5TX-ray2.52A/B39-482[»]
3NLDX-ray2.28A/B39-482[»]
3NLEX-ray1.95A/B39-482[»]
3NLFX-ray2.32A/B39-482[»]
3NLGX-ray2.38A/B39-482[»]
3NLHX-ray2.10A/B39-482[»]
3NLIX-ray1.98A/B39-482[»]
3NLTX-ray2.74A/B39-482[»]
3NLUX-ray2.65A/B39-482[»]
3NSEX-ray2.10A/B39-482[»]
3PNHX-ray1.93A/B67-482[»]
3RQOX-ray2.08A/B40-482[»]
3RQPX-ray2.35A/B40-482[»]
4C3AX-ray2.20A/B40-482[»]
4CARX-ray2.05A/B40-482[»]
4CFTX-ray1.79A/B40-482[»]
4CTYX-ray2.30A/B40-482[»]
4CTZX-ray2.01A/B40-482[»]
4CU0X-ray2.08A/B40-482[»]
4CU1X-ray1.89A/B40-482[»]
4CULX-ray2.23A/B40-482[»]
4CUMX-ray2.33A/B40-482[»]
4CUNX-ray2.48A/B40-482[»]
4CVGX-ray2.31A/B40-482[»]
4CWVX-ray2.34A/B40-482[»]
4CWWX-ray2.16A/B40-482[»]
4CWXX-ray2.15A/B40-482[»]
4CWYX-ray2.15A/B40-482[»]
4CWZX-ray2.08A/B40-482[»]
4CX0X-ray2.20A/B40-482[»]
4CX1X-ray2.13A/B40-482[»]
4CX2X-ray2.04A/B40-482[»]
4D33X-ray2.09A/B40-482[»]
4D34X-ray2.25A/B40-482[»]
4D35X-ray2.18A/B40-482[»]
4D36X-ray2.05A/B40-482[»]
4D37X-ray2.10A/B40-482[»]
4D38X-ray2.30A/B40-482[»]
4D39X-ray2.00A/B40-482[»]
4D3AX-ray2.25A/B40-482[»]
4IMXX-ray2.25A/B40-482[»]
4JSKX-ray2.28A/B40-482[»]
4JSLX-ray2.04A/B40-482[»]
4JSMX-ray2.25A/B40-482[»]
4K5HX-ray2.25A/B40-482[»]
4K5IX-ray2.08A/B40-482[»]
4K5JX-ray2.36A/B40-482[»]
4K5KX-ray2.00A/B40-482[»]
4KCPX-ray2.07A/B40-482[»]
4KCQX-ray2.03A/B40-482[»]
4KCRX-ray2.09A/B40-482[»]
4KCSX-ray2.05A/B40-482[»]
4LUWX-ray2.25A/B41-482[»]
4NSEX-ray1.95A/B39-482[»]
4UH7X-ray2.23A/B40-482[»]
4UH8X-ray2.30A/B40-482[»]
4UH9X-ray2.14A/B40-482[»]
4UHAX-ray2.20A/B40-482[»]
4UPQX-ray2.03A/B40-482[»]
4UPRX-ray1.93A/B40-482[»]
4UPSX-ray1.95A/B40-482[»]
4UPTX-ray2.20A/B40-482[»]
5ADJX-ray2.22A/B40-482[»]
5ADKX-ray1.80A/B40-482[»]
5ADLX-ray2.21A/B40-482[»]
5ADMX-ray2.20A/B40-482[»]
5ADNX-ray2.00A/B40-482[»]
5FJ2X-ray2.05A/B40-482[»]
5FJ3X-ray2.20A/B40-482[»]
5FVYX-ray2.10A/B40-482[»]
5FVZX-ray2.05A/B40-482[»]
5NSEX-ray1.90A/B39-482[»]
5UODX-ray2.01A/B40-482[»]
5VV6X-ray2.00A/B40-482[»]
5VV7X-ray2.20A/B40-482[»]
5VV8X-ray2.15A/B40-482[»]
5VV9X-ray2.50A/B40-482[»]
5VVAX-ray2.55A/B40-482[»]
5VVGX-ray2.30A/B40-482[»]
5VVNX-ray2.40A/B40-482[»]
6NSEX-ray2.35A/B39-482[»]
7NSEX-ray2.35A/B39-482[»]
8NSEX-ray2.25A/B39-482[»]
9NSEX-ray2.24A/B39-482[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P29473

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P29473

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P29473

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini522 – 705Flavodoxin-likePROSITE-ProRule annotationAdd BLAST184
Domaini758 – 1004FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST247

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni100 – 488Interaction with NOSIPBy similarityAdd BLAST389
Regioni492 – 512Calmodulin-bindingSequence analysisAdd BLAST21

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NOS family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1158 Eukaryota
COG0369 LUCA
COG4362 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220884

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000159

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P29473

Database of Orthologous Groups

More...
OrthoDBi
90349at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.990.10, 1 hit
3.40.50.360, 1 hit
3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003097 CysJ-like_FAD-binding
IPR017927 FAD-bd_FR_type
IPR001094 Flavdoxin-like
IPR008254 Flavodoxin/NO_synth
IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR029039 Flavoprotein-like_sf
IPR039261 FNR_nucleotide-bd
IPR023173 NADPH_Cyt_P450_Rdtase_alpha
IPR012144 NOS_euk
IPR004030 NOS_N
IPR036119 NOS_N_sf
IPR001433 OxRdtase_FAD/NAD-bd
IPR017938 Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00667 FAD_binding_1, 1 hit
PF00258 Flavodoxin_1, 1 hit
PF00175 NAD_binding_1, 1 hit
PF02898 NO_synthase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000333 NOS, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00369 FLAVODOXIN
PR00371 FPNCR

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52218 SSF52218, 1 hit
SSF52343 SSF52343, 1 hit
SSF56512 SSF56512, 1 hit
SSF63380 SSF63380, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51384 FAD_FR, 1 hit
PS50902 FLAVODOXIN_LIKE, 1 hit
PS60001 NOS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P29473-1 [UniParc]FASTAAdd to basket
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        10         20         30         40         50
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSR APAPATPHAP
60 70 80 90 100
DHSPAPNSPT LTRPPEGPKF PRVKNWELGS ITYDTLCAQS QQDGPCTPRC
110 120 130 140 150
CLGSLVLPRK LQTRPSPGPP PAEQLLSQAR DFINQYYSSI KRSGSQAHEE
160 170 180 190 200
RLQEVEAEVA STGTYHLRES ELVFGAKQAW RNAPRCVGRI QWGKLQVFDA
210 220 230 240 250
RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRAPGR GDFRIWNSQL
260 270 280 290 300
VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE
310 320 330 340 350
APELFVLPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF
360 370 380 390 400
SAAPFSGWYM STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA
410 420 430 440 450
AVEINLAVLH SFQLAKVTIV DHHAATVSFM KHLDNEQKAR GGCPADWAWI
460 470 480 490 500
VPPISGSLTP VFHQEMVNYI LSPAFRYQPD PWKGSATKGA GITRKKTFKE
510 520 530 540 550
VANAVKISAS LMGTLMAKRV KATILYASET GRAQSYAQQL GRLFRKAFDP
560 570 580 590 600
RVLCMDEYDV VSLEHEALVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN
610 620 630 640 650
SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC
660 670 680 690 700
VFGLGSRAYP HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW
710 720 730 740 750
AKAAFQASCE TFCVGEEAKA AAQDIFSPKR SWKRQRYRLS TQAEGLQLLP
760 770 780 790 800
GLIHVHRRKM FQATVLSVEN LQSSKSTRAT ILVRLDTAGQ EGLQYQPGDH
810 820 830 840 850
IGICPPNRPG LVEALLSRVE DPPPPTESVA VEQLEKGSPG GPPPSWVRDP
860 870 880 890 900
RLPPCTLRQA LTFFLDITSP PSPRLLRLLS TLAEEPSEQQ ELETLSQDPR
910 920 930 940 950
RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPNA
960 970 980 990 1000
HPGEVHLTVA VLAYRTQDGL GPLHYGVCST WLSQLKTGDP VPCFIRGAPS
1010 1020 1030 1040 1050
FRLPPDPYVP CILVGPGTGI APFRGFWQER LHDIESKGLQ PAPMTLVFGC
1060 1070 1080 1090 1100
RCSQLDHLYR DEVQDAQERG VFGRVLTAFS REPDSPKTYV QDILRTELAA
1110 1120 1130 1140 1150
EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME LDEAGDVIGV
1160 1170 1180 1190 1200
LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWAFDPPGP

DTPGP
Length:1,205
Mass (Da):133,287
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5DC8FF4F25870281
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti100C → R in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti165Y → I in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti318 – 328EHPTLEWFAAL → GAPHTGVVRGP in AAA30669 (PubMed:1379225).CuratedAdd BLAST11
Sequence conflicti455S → Y in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti459T → P in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti741T → A in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti804 – 805CP → SA in AAA30669 (PubMed:1379225).Curated2
Sequence conflicti857L → V in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti907 – 908WF → LV in AAA30669 (PubMed:1379225).Curated2
Sequence conflicti1042A → H in AAA30669 (PubMed:1379225).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M99057 mRNA Translation: AAA30667.1
M89952 mRNA Translation: AAA30494.1
M95674 mRNA Translation: AAA30669.1

Protein sequence database of the Protein Information Resource

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PIRi
A38943

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Bt.4662

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99057 mRNA Translation: AAA30667.1
M89952 mRNA Translation: AAA30494.1
M95674 mRNA Translation: AAA30669.1
PIRiA38943
UniGeneiBt.4662

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D0CX-ray1.65A/B39-482[»]
1D0OX-ray1.95A/B39-482[»]
1D1VX-ray1.93A/B39-482[»]
1D1WX-ray2.00A/B39-482[»]
1D1XX-ray2.00A/B39-482[»]
1D1YX-ray2.20A/B39-482[»]
1DM6X-ray1.95A/B39-482[»]
1DM7X-ray2.10A/B39-482[»]
1DM8X-ray2.25A/B39-482[»]
1DMIX-ray2.00A/B39-482[»]
1DMJX-ray2.35A/B39-482[»]
1DMKX-ray1.90A/B39-482[»]
1ED4X-ray1.86A/B39-482[»]
1ED5X-ray1.80A/B39-482[»]
1ED6X-ray2.05A/B39-482[»]
1FOIX-ray1.93A/B39-482[»]
1FOJX-ray2.10A/B39-482[»]
1FOLX-ray2.20A/B39-482[»]
1FOOX-ray2.00A/B39-482[»]
1FOPX-ray2.30A/B39-482[»]
1I83X-ray2.00A/B39-482[»]
1NSEX-ray1.90A/B39-482[»]
1P6LX-ray2.35A/B67-483[»]
1P6MX-ray2.27A/B67-483[»]
1P6NX-ray2.50A/B67-483[»]
1Q2OX-ray1.74A/B67-482[»]
1RS8X-ray2.30A/B67-482[»]
1RS9X-ray2.22A/B67-482[»]
1ZZSX-ray1.85A/B67-482[»]
1ZZTX-ray2.14A/B67-482[»]
2G6OX-ray1.90A/B67-482[»]
2HX2X-ray1.95A/B67-482[»]
2NSEX-ray2.34A/B39-482[»]
3DQSX-ray2.03A/B67-482[»]
3DQTX-ray2.54A/B67-482[»]
3E7SX-ray2.50A/B57-487[»]
3JWWX-ray2.20A/B39-482[»]
3JWXX-ray2.00A/B39-482[»]
3JWYX-ray2.24A/B39-482[»]
3JWZX-ray2.40A/B39-482[»]
3N5PX-ray2.39A/B39-482[»]
3N5QX-ray2.90A/B39-482[»]
3N5RX-ray2.57A/B39-482[»]
3N5SX-ray2.18A/B39-482[»]
3N5TX-ray2.52A/B39-482[»]
3NLDX-ray2.28A/B39-482[»]
3NLEX-ray1.95A/B39-482[»]
3NLFX-ray2.32A/B39-482[»]
3NLGX-ray2.38A/B39-482[»]
3NLHX-ray2.10A/B39-482[»]
3NLIX-ray1.98A/B39-482[»]
3NLTX-ray2.74A/B39-482[»]
3NLUX-ray2.65A/B39-482[»]
3NSEX-ray2.10A/B39-482[»]
3PNHX-ray1.93A/B67-482[»]
3RQOX-ray2.08A/B40-482[»]
3RQPX-ray2.35A/B40-482[»]
4C3AX-ray2.20A/B40-482[»]
4CARX-ray2.05A/B40-482[»]
4CFTX-ray1.79A/B40-482[»]
4CTYX-ray2.30A/B40-482[»]
4CTZX-ray2.01A/B40-482[»]
4CU0X-ray2.08A/B40-482[»]
4CU1X-ray1.89A/B40-482[»]
4CULX-ray2.23A/B40-482[»]
4CUMX-ray2.33A/B40-482[»]
4CUNX-ray2.48A/B40-482[»]
4CVGX-ray2.31A/B40-482[»]
4CWVX-ray2.34A/B40-482[»]
4CWWX-ray2.16A/B40-482[»]
4CWXX-ray2.15A/B40-482[»]
4CWYX-ray2.15A/B40-482[»]
4CWZX-ray2.08A/B40-482[»]
4CX0X-ray2.20A/B40-482[»]
4CX1X-ray2.13A/B40-482[»]
4CX2X-ray2.04A/B40-482[»]
4D33X-ray2.09A/B40-482[»]
4D34X-ray2.25A/B40-482[»]
4D35X-ray2.18A/B40-482[»]
4D36X-ray2.05A/B40-482[»]
4D37X-ray2.10A/B40-482[»]
4D38X-ray2.30A/B40-482[»]
4D39X-ray2.00A/B40-482[»]
4D3AX-ray2.25A/B40-482[»]
4IMXX-ray2.25A/B40-482[»]
4JSKX-ray2.28A/B40-482[»]
4JSLX-ray2.04A/B40-482[»]
4JSMX-ray2.25A/B40-482[»]
4K5HX-ray2.25A/B40-482[»]
4K5IX-ray2.08A/B40-482[»]
4K5JX-ray2.36A/B40-482[»]
4K5KX-ray2.00A/B40-482[»]
4KCPX-ray2.07A/B40-482[»]
4KCQX-ray2.03A/B40-482[»]
4KCRX-ray2.09A/B40-482[»]
4KCSX-ray2.05A/B40-482[»]
4LUWX-ray2.25A/B41-482[»]
4NSEX-ray1.95A/B39-482[»]
4UH7X-ray2.23A/B40-482[»]
4UH8X-ray2.30A/B40-482[»]
4UH9X-ray2.14A/B40-482[»]
4UHAX-ray2.20A/B40-482[»]
4UPQX-ray2.03A/B40-482[»]
4UPRX-ray1.93A/B40-482[»]
4UPSX-ray1.95A/B40-482[»]
4UPTX-ray2.20A/B40-482[»]
5ADJX-ray2.22A/B40-482[»]
5ADKX-ray1.80A/B40-482[»]
5ADLX-ray2.21A/B40-482[»]
5ADMX-ray2.20A/B40-482[»]
5ADNX-ray2.00A/B40-482[»]
5FJ2X-ray2.05A/B40-482[»]
5FJ3X-ray2.20A/B40-482[»]
5FVYX-ray2.10A/B40-482[»]
5FVZX-ray2.05A/B40-482[»]
5NSEX-ray1.90A/B39-482[»]
5UODX-ray2.01A/B40-482[»]
5VV6X-ray2.00A/B40-482[»]
5VV7X-ray2.20A/B40-482[»]
5VV8X-ray2.15A/B40-482[»]
5VV9X-ray2.50A/B40-482[»]
5VVAX-ray2.55A/B40-482[»]
5VVGX-ray2.30A/B40-482[»]
5VVNX-ray2.40A/B40-482[»]
6NSEX-ray2.35A/B39-482[»]
7NSEX-ray2.35A/B39-482[»]
8NSEX-ray2.25A/B39-482[»]
9NSEX-ray2.24A/B39-482[»]
ProteinModelPortaliP29473
SMRiP29473
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42217N
ELMiP29473
IntActiP29473, 2 interactors
MINTiP29473
STRINGi9913.ENSBTAP00000023515

Chemistry databases

BindingDBiP29473
ChEMBLiCHEMBL4802

PTM databases

iPTMnetiP29473
SwissPalmiP29473

Proteomic databases

PaxDbiP29473
PRIDEiP29473

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1158 Eukaryota
COG0369 LUCA
COG4362 LUCA
HOGENOMiHOG000220884
HOVERGENiHBG000159
InParanoidiP29473
OrthoDBi90349at2759

Enzyme and pathway databases

BRENDAi1.14.13.39 908

Miscellaneous databases

EvolutionaryTraceiP29473

Family and domain databases

Gene3Di1.20.990.10, 1 hit
3.40.50.360, 1 hit
3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR003097 CysJ-like_FAD-binding
IPR017927 FAD-bd_FR_type
IPR001094 Flavdoxin-like
IPR008254 Flavodoxin/NO_synth
IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR029039 Flavoprotein-like_sf
IPR039261 FNR_nucleotide-bd
IPR023173 NADPH_Cyt_P450_Rdtase_alpha
IPR012144 NOS_euk
IPR004030 NOS_N
IPR036119 NOS_N_sf
IPR001433 OxRdtase_FAD/NAD-bd
IPR017938 Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00667 FAD_binding_1, 1 hit
PF00258 Flavodoxin_1, 1 hit
PF00175 NAD_binding_1, 1 hit
PF02898 NO_synthase, 1 hit
PIRSFiPIRSF000333 NOS, 1 hit
PRINTSiPR00369 FLAVODOXIN
PR00371 FPNCR
SUPFAMiSSF52218 SSF52218, 1 hit
SSF52343 SSF52343, 1 hit
SSF56512 SSF56512, 1 hit
SSF63380 SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS51384 FAD_FR, 1 hit
PS50902 FLAVODOXIN_LIKE, 1 hit
PS60001 NOS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNOS3_BOVIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P29473
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 201 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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