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O62699 (NOS2_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:NOS2
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length1154 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2 By similarity.

Catalytic activity

2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

Cofactor

Heme group By similarity.

Binds 1 FAD By similarity.

Binds 1 FMN By similarity.

Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme By similarity.

Enzyme regulation

Regulated by calcium/calmodulin By similarity.

Subunit structure

Homodimer. Binds SLC9A3R1 By similarity.

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11541154Nitric oxide synthase, inducible
PRO_0000170927

Regions

Domain536 – 674139Flavodoxin-like
Domain727 – 967241FAD-binding FR-type
Nucleotide binding620 – 65132FMN By similarity
Nucleotide binding764 – 77512FAD By similarity
Nucleotide binding900 – 91011FAD By similarity
Nucleotide binding975 – 99319NADP By similarity
Nucleotide binding1073 – 108816NADP By similarity
Region506 – 52621Calmodulin-binding Potential

Sites

Metal binding1971Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict42 – 5211DDLKNHKHHND → KCHSLSKHRDE Ref.2
Sequence conflict561P → S in AAC15587. Ref.2
Sequence conflict59 – 646ETVQKL → GTVKTS in AAC15587. Ref.2
Sequence conflict68 – 8013LDKLH…LSRPQ → TIKPAAPPLACPR Ref.2
Sequence conflict91 – 922MT → RS in AAC78630. Ref.1
Sequence conflict102 – 1043KGD → MGV in AAC78630. Ref.1
Sequence conflict1081K → T in AAC78630. Ref.1
Sequence conflict111 – 1155SCLGA → LCMGS in AAC78630. Ref.1
Sequence conflict1191P → T in AAC78630. Ref.1
Sequence conflict125 – 1273EPR → GPS in AAC78630. Ref.1
Sequence conflict133 – 1342PD → TE in AAC78630. Ref.1
Sequence conflict1491S → G in AAC78630. Ref.1
Sequence conflict1691E → D in AAC78630. Ref.1
Sequence conflict394 – 3952RR → SK in AAC78630. Ref.1
Sequence conflict497 – 4993VWQ → LWL in AAC78630. Ref.1
Sequence conflict506 – 5083QRR → HRK in AAC78630. Ref.1
Sequence conflict6151K → N in AAC78630. Ref.1
Sequence conflict624 – 6263GSS → RSN in AAC78630. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O62699 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: D6AD3A88AE89E995

FASTA1,154131,847
        10         20         30         40         50         60 
MACPWKFLFR AKFHQYGMKE EKDINNNVEK PPGATPSPST QDDLKNHKHH NDSPQPLTET 

        70         80         90        100        110        120 
VQKLPESLDK LHATPLSRPQ HVRIKNWGNG MTFQDTLHHK AKGDLACKSK SCLGAIMNPK 

       130        140        150        160        170        180 
SLTREPRDKP TPPDELLPQA IEFVNQYYSS FKEAKIEEHL ARVEAVTKEI ETTGTYQLTG 

       190        200        210        220        230        240 
DELIFATKQA WRNAPRCIGR IQWSNLQVFD ARSCSTAKEM FEHICRHLRY ASNNGNIRSA 

       250        260        270        280        290        300 
ITVFPQRTDG KHDFRVWNAQ LIRYAGYQMP DGTILGDPAS VEFTQLCIDL GWKPKYGRFD 

       310        320        330        340        350        360 
VVPLVLQADG QDPEFFEIPP DLVLEVPMEH PKYEWFRELE LKWYALPAVA NMLLEVGGLE 

       370        380        390        400        410        420 
FPGCPFNGWY MGTEIGVRDF CDVQRYNILE EVGRRMGLET HKLASLWKDR AVIEINVAVL 

       430        440        450        460        470        480 
HSFQKQNVTI MDHHSAAESF MKYMQSEYRS RGGCPADWIW LVPPISGSIT PVFHQEMLNY 

       490        500        510        520        530        540 
VLSPFYYYQV EAWKTHVWQD EKRRPQRRKI QLKVLVKAVL FASMLMRKTM ASRVRVTILF 

       550        560        570        580        590        600 
ATETGKSETL ARDLGALFSC AFHPKVLCMD EYKLSHLEEE QLLLVVTSTF GNGDSPGNGE 

       610        620        630        640        650        660 
KLKKSLFMLK ELTNKFRYAV FGLGSSMYPQ FCAFAHDIDH KLSHLGASQL TPGGEGDELN 

       670        680        690        700        710        720 
GKEEAFRCWA VQTFKAACDT SDVRGKHCIQ IPRLYTSNVT WDPHHYRLLQ DSQPLDLNKA 

       730        740        750        760        770        780 
LSKMHAKNVF TLRLKSQRNL QSPISNRTTL QVELSCEDSQ ELSYLPGEHL GVFPGNQLAL 

       790        800        810        820        830        840 
VQGILERVVY SPAPLQPVHL ETLSERGSYW VRNNRLPPCS LSQALTYFLD ITTPPTHLLL 

       850        860        870        880        890        900 
RKLAQLAHQY AERHRLEILC HPSEYNKWKL TNSPTFLEVL EEFPSLRVSA GFLLSQLPIL 

       910        920        930        940        950        960 
KPRYYSISSS RDCTPMEVHL TVAVLVYPTR DGQGPLHHGV CSTWLSNLKP QDPVPCFVRS 

       970        980        990       1000       1010       1020 
AGNFKLPEDP SRPCILIGPG TGIAPFRSFW QQRLHDIKHK GLRGSRMTLV FGCRRPDEDH 

      1030       1040       1050       1060       1070       1080 
LYREEMLEMA QSGVLHEVHT AYSRLPGQPK VYVQDILRQQ LASQVLRMLH EEQGHLYVCG 

      1090       1100       1110       1120       1130       1140 
DVRMARDVAH TLKHLVAAKL SLSEEQVEDY FFQLKSQKRY HEDIFGAVFP YEVKKDGAAK 

      1150 
QPSDPRVPAA HGRS 

« Hide

References

[1]"Induction and cDNA sequence of inducible nitric oxide synthase from canine aortic smooth muscle cells."
Wang X., McGregor C.G.A., Miller V.M.
Am. J. Physiol. 275:H1122-H1129(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Aorta.
[2]"The canine inducible NO synthase."
Haerter L., Straubinger R.K., Appel M.J.G.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-632.
Tissue: Alveolar macrophage.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF077821 mRNA. Translation: AAC78630.1.
AF032909 mRNA. Translation: AAC15587.1.
RefSeqNP_001003186.1. NM_001003186.1.
UniGeneCfa.45041.

3D structure databases

ProteinModelPortalO62699.
SMRO62699. Positions 80-499, 700-1127.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403822.
KEGGcfa:403822.

Organism-specific databases

CTD4843.

Phylogenomic databases

eggNOGCOG4362.
HOGENOMHOG000220884.
HOVERGENHBG000159.
KOK13241.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
3.90.340.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NO_synthase_oxygenase_dom.
IPR012144. NOS_euk.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20817318.

Entry information

Entry nameNOS2_CANFA
AccessionPrimary (citable) accession number: O62699
Secondary accession number(s): O97604
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families