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Entry version 143 (08 May 2019)
Sequence version 2 (13 Sep 2005)
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Protein

Nitric oxide synthase, inducible

Gene

NOS2

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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 transcript 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

<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

Regulated by calcium/calmodulin.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 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

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
LigandCalcium, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

<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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<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
  • UP000002254 <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

Cytoplasm

<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_00001709271 – 1154Nitric oxide synthase, inducibleAdd BLAST1154

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 residuei572PhosphotyrosineBy 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

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O62699

<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

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000027512

<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
O62699

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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220884

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O62699

KEGG Orthology (KO)

More...
KOi
K13241

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>. 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>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.

O62699-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MACPWKFLFR AKFHQYGMKE EKDINNNVEK PPGATPSPST QDDLKNHKHH
60 70 80 90 100
NDSPQPLTET VQKLPESLDK LHATPLSRPQ HVRIKNWGNG MTFQDTLHHK
110 120 130 140 150
AKGDLACKSK SCLGAIMNPK SLTREPRDKP TPPDELLPQA IEFVNQYYSS
160 170 180 190 200
FKEAKIEEHL ARVEAVTKEI ETTGTYQLTG DELIFATKQA WRNAPRCIGR
210 220 230 240 250
IQWSNLQVFD ARSCSTAKEM FEHICRHLRY ASNNGNIRSA ITVFPQRTDG
260 270 280 290 300
KHDFRVWNAQ LIRYAGYQMP DGTILGDPAS VEFTQLCIDL GWKPKYGRFD
310 320 330 340 350
VVPLVLQADG QDPEFFEIPP DLVLEVPMEH PKYEWFRELE LKWYALPAVA
360 370 380 390 400
NMLLEVGGLE FPGCPFNGWY MGTEIGVRDF CDVQRYNILE EVGRRMGLET
410 420 430 440 450
HKLASLWKDR AVIEINVAVL HSFQKQNVTI MDHHSAAESF MKYMQSEYRS
460 470 480 490 500
RGGCPADWIW LVPPISGSIT PVFHQEMLNY VLSPFYYYQV EAWKTHVWQD
510 520 530 540 550
EKRRPQRRKI QLKVLVKAVL FASMLMRKTM ASRVRVTILF ATETGKSETL
560 570 580 590 600
ARDLGALFSC AFHPKVLCMD EYKLSHLEEE QLLLVVTSTF GNGDSPGNGE
610 620 630 640 650
KLKKSLFMLK ELTNKFRYAV FGLGSSMYPQ FCAFAHDIDH KLSHLGASQL
660 670 680 690 700
TPGGEGDELN GKEEAFRCWA VQTFKAACDT SDVRGKHCIQ IPRLYTSNVT
710 720 730 740 750
WDPHHYRLLQ DSQPLDLNKA LSKMHAKNVF TLRLKSQRNL QSPISNRTTL
760 770 780 790 800
QVELSCEDSQ ELSYLPGEHL GVFPGNQLAL VQGILERVVY SPAPLQPVHL
810 820 830 840 850
ETLSERGSYW VRNNRLPPCS LSQALTYFLD ITTPPTHLLL RKLAQLAHQY
860 870 880 890 900
AERHRLEILC HPSEYNKWKL TNSPTFLEVL EEFPSLRVSA GFLLSQLPIL
910 920 930 940 950
KPRYYSISSS RDCTPMEVHL TVAVLVYPTR DGQGPLHHGV CSTWLSNLKP
960 970 980 990 1000
QDPVPCFVRS AGNFKLPEDP SRPCILIGPG TGIAPFRSFW QQRLHDIKHK
1010 1020 1030 1040 1050
GLRGSRMTLV FGCRRPDEDH LYREEMLEMA QSGVLHEVHT AYSRLPGQPK
1060 1070 1080 1090 1100
VYVQDILRQQ LASQVLRMLH EEQGHLYVCG DVRMARDVAH TLKHLVAAKL
1110 1120 1130 1140 1150
SLSEEQVEDY FFQLKSQKRY HEDIFGAVFP YEVKKDGAAK QPSDPRVPAA

HGRS
Length:1,154
Mass (Da):131,847
Last modified:September 13, 2005 - 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:iD6AD3A88AE89E995
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 conflicti42 – 52DDLKNHKHHND → KCHSLSKHRDE (Ref. 2) CuratedAdd BLAST11
Sequence conflicti56P → S in AAC15587 (Ref. 2) Curated1
Sequence conflicti59 – 64ETVQKL → GTVKTS in AAC15587 (Ref. 2) Curated6
Sequence conflicti68 – 80LDKLH…LSRPQ → TIKPAAPPLACPR (Ref. 2) CuratedAdd BLAST13
Sequence conflicti91 – 92MT → RS in AAC78630 (PubMed:9746458).Curated2
Sequence conflicti102 – 104KGD → MGV in AAC78630 (PubMed:9746458).Curated3
Sequence conflicti108K → T in AAC78630 (PubMed:9746458).Curated1
Sequence conflicti111 – 115SCLGA → LCMGS in AAC78630 (PubMed:9746458).Curated5
Sequence conflicti119P → T in AAC78630 (PubMed:9746458).Curated1
Sequence conflicti125 – 127EPR → GPS in AAC78630 (PubMed:9746458).Curated3
Sequence conflicti133 – 134PD → TE in AAC78630 (PubMed:9746458).Curated2
Sequence conflicti149S → G in AAC78630 (PubMed:9746458).Curated1
Sequence conflicti169E → D in AAC78630 (PubMed:9746458).Curated1
Sequence conflicti394 – 395RR → SK in AAC78630 (PubMed:9746458).Curated2
Sequence conflicti497 – 499VWQ → LWL in AAC78630 (PubMed:9746458).Curated3
Sequence conflicti506 – 508QRR → HRK in AAC78630 (PubMed:9746458).Curated3
Sequence conflicti615K → N in AAC78630 (PubMed:9746458).Curated1
Sequence conflicti624 – 626GSS → RSN in AAC78630 (PubMed:9746458).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF077821 mRNA Translation: AAC78630.1
AF032909 mRNA Translation: AAC15587.1

NCBI Reference Sequences

More...
RefSeqi
NP_001300777.1, NM_001313848.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
403822

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cfa:403822

<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
AF077821 mRNA Translation: AAC78630.1
AF032909 mRNA Translation: AAC15587.1
RefSeqiNP_001300777.1, NM_001313848.1

3D structure databases

SMRiO62699
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9612.ENSCAFP00000027512

Proteomic databases

PRIDEiO62699

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403822
KEGGicfa:403822

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4843

Phylogenomic databases

HOGENOMiHOG000220884
InParanoidiO62699
KOiK13241
OrthoDBi90349at2759

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_CANLF
<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: O62699
Secondary accession number(s): O97604
<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: May 30, 2000
Last sequence update: September 13, 2005
Last modified: May 8, 2019
This is version 143 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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