Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q06518 (NOS2_RAT)

Entry version 195 (11 Dec 2019)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Nitric oxide synthase, inducible

Gene

Nos2

Organism
Rattus norvegicus (Rat)
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 a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8.By similarity

Caution

sequence Was originally thought to originate from human but appears to be from rat.1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Not stimulated by calcium/calmodulin. Aspirin inhibits expression and function of this enzyme and effects may be exerted at the level of translational/post-translational modification and directly on the catalytic activity (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi107ZincBy similarity1
Metal bindingi112ZincBy similarity1
Metal bindingi197Iron (heme axial ligand)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi620 – 651FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi764 – 775FADBy similarityAdd BLAST12
Nucleotide bindingi900 – 910FADBy similarityAdd BLAST11
Nucleotide bindingi975 – 993NADPBy similarityAdd BLAST19
Nucleotide bindingi1073 – 1088NADPBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
LigandFAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.14.13.39 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-1222556 ROS and RNS production in phagocytes
R-RNO-392154 Nitric oxide stimulates guanylate cyclase
R-RNO-9033241 Peroxisomal protein import

<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, inducible (EC:1.14.13.39)
Alternative name(s):
Inducible NO synthase
Short name:
Inducible NOS
Short name:
iNOS
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2
<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:Nos2
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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

Organism-specific databases

Rat genome database

More...RGDi		3185 Nos2

<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

Cytoplasm

<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		CHEMBL3051

<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 ‘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_00001709371 – 1147Nitric oxide synthase, inducibleAdd BLAST1147

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei564PhosphothreonineCombined sources1
Modified residuei572PhosphotyrosineCombined sources1

<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

Polyubiquitinated; mediated by SPSB1, SPSB2 and SPSB4, leading to proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		Q06518

PRoteomics IDEntifications database

More...PRIDEi		Q06518

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q06518

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q06518

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

In normal kidney, expressed primarily in the medullary thick ascending limb, with minor amounts in the medullary collecting duct and vasa recta bundle.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By interferon gamma and lipopolysaccharides (LPS).

<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 (By similarity).

Interacts with SLC9A3R1 (By similarity).

Interacts with GAPDH (By similarity).

Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9 transnitrosylase complex (By similarity).

Interacts with SPSB1, SPSB2 and SPSB4 (By similarity).

Interacts with ELOC and CUL5 in the presence of SPSB1 or SPSB2 or SPSB4 (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Q7TQN43EBI-15919967,EBI-1187180

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q06518

Database of interacting proteins

More...DIPi		DIP-59942N

Protein interaction database and analysis system

More...IntActi		Q06518, 1 interactor

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000067662

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q06518

<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

3D structure databases

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

More...SMRi		Q06518

Database of comparative protein structure models

More...ModBasei		Search...

<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>Domaini536 – 674Flavodoxin-likePROSITE-ProRule annotationAdd BLAST139
Domaini727 – 967FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST241

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>Regioni506 – 526Calmodulin-bindingSequence analysisAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi23 – 27DINNN-motif; mediates interaction with SPSB1, SPSB2 and SPSB4By similarity5

<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

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q06518

KEGG Orthology (KO)

More...KOi		K13241

Database of Orthologous Groups

More...OrthoDBi		90349at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q06518

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q06518-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MACPWKFLFR VKSYQGDLKE EKDINNNVEK TPGAIPSPTT QDDPKSHKHQ 
        60         70         80         90        100
NGFPQFLTGT AQNVPESLDK LHVTPSTRPQ HVRIKNWGNG EIFHDTLHHK 
       110        120        130        140        150
ATSDISCKSK LCMGSIMNSK SLTRGPRDKP TPVEELLPQA IEFINQYYGS 
       160        170        180        190        200
FKEAKIEEHL ARLEAVTKEI ETTGTYQLTL DELIFATKMA WRNAPRCIGR 
       210        220        230        240        250
IQWSNLQVFD ARSCSTASEM FQHICRHILY ATNSGNIRSA ITVFPQRSDG 
       260        270        280        290        300
KHDFRIWNSQ LIRYAGYQMP DGTIRGDPAT LEFTQLCIDL GWKPRYGRFD 
       310        320        330        340        350
VLPLVLQAHG QDPEVFEIPP DLVLEVTMEH PKYEWFQELG LKWYALPAVA 
       360        370        380        390        400
NMLLEVGGLE FPACPFNGWY MGTEIGVRDF CDTQRYNILE EVGRRMGLET 
       410        420        430        440        450
HTLASLWKDR AVTEINAAVL HSFQKQNVTI MDHHTASESF MKHMQNEYRA 
       460        470        480        490        500
RGGCPADWIW LVPPVSGSIT PVFHQEMLNY VLSPFYYYQI EPWKTHIWQD 
       510        520        530        540        550
EKLRPRRREI RFTVLVKAVF FASVLMRKVM ASRVRATVLF ATETGKSEAL 
       560        570        580        590        600
ARDLAALFSY AFNTKVVCME QYKANTLEEE QLLLVVTSTF GNGDCPSNGQ 
       610        620        630        640        650
TLKKSLFMMK ELGHTFRYAV FGLGSSMYPQ FCAFAHDIDQ KLSHLGASQL 
       660        670        680        690        700
APTGEGDELS GQEDAFRSWA VQTFRAACET FDVRSKHCIQ IPKRYTSNAT 
       710        720        730        740        750
WEPEQYKLTQ SPESLDLNKA LSSIHAKNVF TMRLKSLQNL QSEKSSRTTL 
       760        770        780        790        800
LVQLTFEGSR GPSYLPGEHL GIFPGNQTAL VQGILERVVD CSSPDQTVCL 
       810        820        830        840        850
EVLDESGSYW VKDKRLPPCS LRQALTYFLD ITTPPTQLQL HKLARFATEE 
       860        870        880        890        900
THRQRLEALC QPSEYNDWKF SNNPTFLEVL EEFPSLRVPA AFLLSQLPIL 
       910        920        930        940        950
KPRYYSISSS QDHTPSEVHL TVAVVTYRTR DGQGPLHHGV CSTWINNLKP 
       960        970        980        990       1000
EDPVPCFVRS VSGFQLPEDP SQPCILIGPG TGIAPFRSFW QQRLHDSQHR 
      1010       1020       1030       1040       1050
GLKGGRMTLV FGCRHPEEDH LYQEEMQEMV RKGVLFQVHT GYSRLPGKPK 
      1060       1070       1080       1090       1100
VYVQDILQKE LADEVFSVLH GEQGHLYVCG DVRMARDVAT TLKKLVAAKL 
      1110       1120       1130       1140 
NLSEEQVEDY FFQLKSQKRY HEDIFGAVFS YGAKKGNTLE EPKGTRL
Length:1,147
Mass (Da):130,628
Last modified:October 1, 1996 - v2
<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:i77C77432DD8AB0A9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0RDG2M0RDG2_RAT
Nitric oxide synthase
Nos2
1,147Annotation 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>
F1LSH9F1LSH9_RAT
Nitric oxide synthase
LOC497963 Nos2
1,111Annotation score:

Annotation score:3 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 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 conflicti10R → K in BAA07994 (Ref. 7) Curated1
Sequence conflicti72H → Y in BAA03138 (PubMed:7680561).Curated1
Sequence conflicti107C → R in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti128D → V in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti130P → H in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti171E → G in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti195P → S in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti248S → N in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti248S → T (PubMed:7513765).Curated1
Sequence conflicti248S → T (PubMed:7682072).Curated1
Sequence conflicti264Y → I in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti271D → A in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti277D → E in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti348A → P in BAA03138 (PubMed:7680561).Curated1
Sequence conflicti349V → A in CAA54208 (PubMed:7519448).Curated1
Sequence conflicti380F → L (PubMed:7540573).Curated1
Sequence conflicti380F → L (Ref. 7) Curated1
Sequence conflicti380F → L (PubMed:8913516).Curated1
Sequence conflicti380F → L in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti380F → L in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti395R → S in BAA02090 (PubMed:7693462).Curated1
Sequence conflicti399E → G in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti412V → A in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti477M → I (Ref. 13) Curated1
Sequence conflicti513T → R in AAB18620 (Ref. 11) Curated1
Sequence conflicti515L → W in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti545G → R in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti551A → R in AAB18620 (Ref. 11) Curated1
Sequence conflicti556A → S in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti559S → T in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti559S → T in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti564T → N in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti570E → D in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti583L → P (PubMed:7682072).Curated1
Sequence conflicti583L → P (PubMed:9535415).Curated1
Sequence conflicti591G → A in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti591G → V (PubMed:7680561).Curated1
Sequence conflicti591G → V (PubMed:7519448).Curated1
Sequence conflicti619A → R in AAA85861 (PubMed:7540573).Curated1
Sequence conflicti640Q → P in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti664D → G in AAB18620 (Ref. 11) Curated1
Sequence conflicti679 – 680ET → VP in BAA03138 (PubMed:7680561).Curated2
Sequence conflicti690Q → P in AAB18620 (Ref. 11) Curated1
Sequence conflicti711S → N in AAB18620 (Ref. 11) Curated1
Sequence conflicti714 – 715SL → TR in AAB18620 (Ref. 11) Curated2
Sequence conflicti714S → P (PubMed:7540573).Curated1
Sequence conflicti714S → P (Ref. 7) Curated1
Sequence conflicti714S → P (PubMed:8913516).Curated1
Sequence conflicti714S → P in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti714S → P in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti714S → P in AAC16401 (PubMed:9535415).Curated1
Sequence conflicti719K → R in AAB18620 (Ref. 11) Curated1
Sequence conflicti721L → P (PubMed:7519448).Curated1
Sequence conflicti722S → R (PubMed:7680561).Curated1
Sequence conflicti722S → R (PubMed:7519448).Curated1
Sequence conflicti722S → R (Ref. 11) Curated1
Sequence conflicti724 – 726IHA → FLN (Ref. 11) Curated3
Sequence conflicti730F → I in AAB18620 (Ref. 11) Curated1
Sequence conflicti731T → A in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti740L → P in CAA54208 (PubMed:7519448).Curated1
Sequence conflicti779A → G in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti834P → S in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti844A → G in BAA03138 (PubMed:7680561).Curated1
Sequence conflicti895S → L in BAA02090 (PubMed:7693462).Curated1
Sequence conflicti911Q → L in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti925V → D in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti937H → N in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti999H → R (PubMed:7540573).Curated1
Sequence conflicti999H → R (Ref. 7) Curated1
Sequence conflicti999H → R in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti999H → R in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1008 – 1009TL → NF in AAC83554 (PubMed:9851365).Curated2
Sequence conflicti1016P → R (PubMed:7682072).Curated1
Sequence conflicti1016P → S (PubMed:8913516).Curated1
Sequence conflicti1017E → R (PubMed:7682072).Curated1
Sequence conflicti1017E → R (PubMed:8913516).Curated1
Sequence conflicti1024E → K in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1076L → I in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti1084M → I in CAA54208 (PubMed:7519448).Curated1
Sequence conflicti1129F → V in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1133A → V (PubMed:7540573).Curated1
Sequence conflicti1133A → V (Ref. 7) Curated1
Sequence conflicti1133A → V in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti1133A → V in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1138T → A (PubMed:7540573).Curated1
Sequence conflicti1138T → A (Ref. 7) Curated1
Sequence conflicti1138T → A in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti1138T → A in AAC83554 (PubMed:9851365).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D14051 mRNA Translation: BAA03138.1
U26686 mRNA Translation: AAA85861.1
U03699 mRNA Translation: AAC13747.1
D12520 mRNA Translation: BAA02090.1
L12562 mRNA Translation: AAA41720.1
X76881 mRNA Translation: CAA54208.1
D44591 mRNA Translation: BAA07994.1
D83661 mRNA Translation: BAA12035.1
AF049656 mRNA Translation: AAC83553.1
AF051164 mRNA Translation: AAC83554.1
AF006619 mRNA Translation: AAC16401.1
AF006620 mRNA Translation: AAC16402.1
U48829 mRNA Translation: AAB18620.1
S71597 mRNA Translation: AAB31028.2
L36063 mRNA Translation: AAC02242.1

Protein sequence database of the Protein Information Resource

More...PIRi		I53165
I56575
JC5027
S38253
S47647

NCBI Reference Sequences

More...RefSeqi		NP_036743.3, NM_012611.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24599

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24599

<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
D14051 mRNA Translation: BAA03138.1
U26686 mRNA Translation: AAA85861.1
U03699 mRNA Translation: AAC13747.1
D12520 mRNA Translation: BAA02090.1
L12562 mRNA Translation: AAA41720.1
X76881 mRNA Translation: CAA54208.1
D44591 mRNA Translation: BAA07994.1
D83661 mRNA Translation: BAA12035.1
AF049656 mRNA Translation: AAC83553.1
AF051164 mRNA Translation: AAC83554.1
AF006619 mRNA Translation: AAC16401.1
AF006620 mRNA Translation: AAC16402.1
U48829 mRNA Translation: AAB18620.1
S71597 mRNA Translation: AAB31028.2
L36063 mRNA Translation: AAC02242.1
PIRiI53165
I56575
JC5027
S38253
S47647
RefSeqiNP_036743.3, NM_012611.3

3D structure databases

SMRiQ06518
ModBaseiSearch...

Protein-protein interaction databases

CORUMiQ06518
DIPiDIP-59942N
IntActiQ06518, 1 interactor
STRINGi10116.ENSRNOP00000067662

Chemistry databases

BindingDBiQ06518
ChEMBLiCHEMBL3051

PTM databases

iPTMnetiQ06518
PhosphoSitePlusiQ06518

Proteomic databases

PaxDbiQ06518
PRIDEiQ06518

Genome annotation databases

GeneIDi24599
KEGGirno:24599

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4843
RGDi3185 Nos2

Phylogenomic databases

eggNOGiKOG1158 Eukaryota
COG0369 LUCA
COG4362 LUCA
InParanoidiQ06518
KOiK13241
OrthoDBi90349at2759
PhylomeDBiQ06518

Enzyme and pathway databases

BRENDAi1.14.13.39 5301
ReactomeiR-RNO-1222556 ROS and RNS production in phagocytes
R-RNO-392154 Nitric oxide stimulates guanylate cyclase
R-RNO-9033241 Peroxisomal protein import

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q06518

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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiNOS2_RAT
<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: Q06518
Secondary accession number(s): O35765
, O35766, O60591, O60604, P97774, Q63267, Q64005, Q64558
<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: June 1, 1994
Last sequence update: October 1, 1996
Last modified: December 11, 2019
This is version 195 of the entry and version 2 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again