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O62699

- NOS2_CANFA

UniProt

O62699 - NOS2_CANFA

Protein

Nitric oxide synthase, inducible

Gene

NOS2

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

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

    Cofactori

    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.By similarity

    Enzyme regulationi

    Regulated by calcium/calmodulin.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi197 – 1971Iron (heme axial ligand)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi620 – 65132FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi764 – 77512FADBy similarityAdd
    BLAST
    Nucleotide bindingi900 – 91011FADBy similarityAdd
    BLAST
    Nucleotide bindingi975 – 99319NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1073 – 108816NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. FMN binding Source: InterPro
    3. heme binding Source: InterPro
    4. iron ion binding Source: InterPro
    5. NADP binding Source: InterPro
    6. nitric-oxide synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. defense response to bacterium Source: UniProtKB
    2. nitric oxide biosynthetic process Source: InterPro
    3. peptidyl-cysteine S-nitrosylation Source: UniProtKB
    4. superoxide metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Calcium, Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

    Names & Taxonomyi

    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
    Gene namesi
    Name:NOS2
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11541154Nitric oxide synthase, induciblePRO_0000170927Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer. Binds SLC9A3R1 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO62699.
    SMRiO62699. Positions 80-499, 700-1127.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini536 – 674139Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini727 – 967241FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni506 – 52621Calmodulin-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NOS family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4362.
    HOGENOMiHOG000220884.
    HOVERGENiHBG000159.
    KOiK13241.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    3.90.340.10. 1 hit.
    InterProiIPR003097. 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.
    IPR012144. NOS_euk.
    IPR004030. NOS_N.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF02898. NO_synthase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000333. NOS. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF56512. SSF56512. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    PS60001. NOS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O62699-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACPWKFLFR AKFHQYGMKE EKDINNNVEK PPGATPSPST QDDLKNHKHH     50
    NDSPQPLTET VQKLPESLDK LHATPLSRPQ HVRIKNWGNG MTFQDTLHHK 100
    AKGDLACKSK SCLGAIMNPK SLTREPRDKP TPPDELLPQA IEFVNQYYSS 150
    FKEAKIEEHL ARVEAVTKEI ETTGTYQLTG DELIFATKQA WRNAPRCIGR 200
    IQWSNLQVFD ARSCSTAKEM FEHICRHLRY ASNNGNIRSA ITVFPQRTDG 250
    KHDFRVWNAQ LIRYAGYQMP DGTILGDPAS VEFTQLCIDL GWKPKYGRFD 300
    VVPLVLQADG QDPEFFEIPP DLVLEVPMEH PKYEWFRELE LKWYALPAVA 350
    NMLLEVGGLE FPGCPFNGWY MGTEIGVRDF CDVQRYNILE EVGRRMGLET 400
    HKLASLWKDR AVIEINVAVL HSFQKQNVTI MDHHSAAESF MKYMQSEYRS 450
    RGGCPADWIW LVPPISGSIT PVFHQEMLNY VLSPFYYYQV EAWKTHVWQD 500
    EKRRPQRRKI QLKVLVKAVL FASMLMRKTM ASRVRVTILF ATETGKSETL 550
    ARDLGALFSC AFHPKVLCMD EYKLSHLEEE QLLLVVTSTF GNGDSPGNGE 600
    KLKKSLFMLK ELTNKFRYAV FGLGSSMYPQ FCAFAHDIDH KLSHLGASQL 650
    TPGGEGDELN GKEEAFRCWA VQTFKAACDT SDVRGKHCIQ IPRLYTSNVT 700
    WDPHHYRLLQ DSQPLDLNKA LSKMHAKNVF TLRLKSQRNL QSPISNRTTL 750
    QVELSCEDSQ ELSYLPGEHL GVFPGNQLAL VQGILERVVY SPAPLQPVHL 800
    ETLSERGSYW VRNNRLPPCS LSQALTYFLD ITTPPTHLLL RKLAQLAHQY 850
    AERHRLEILC HPSEYNKWKL TNSPTFLEVL EEFPSLRVSA GFLLSQLPIL 900
    KPRYYSISSS RDCTPMEVHL TVAVLVYPTR DGQGPLHHGV CSTWLSNLKP 950
    QDPVPCFVRS AGNFKLPEDP SRPCILIGPG TGIAPFRSFW QQRLHDIKHK 1000
    GLRGSRMTLV FGCRRPDEDH LYREEMLEMA QSGVLHEVHT AYSRLPGQPK 1050
    VYVQDILRQQ LASQVLRMLH EEQGHLYVCG DVRMARDVAH TLKHLVAAKL 1100
    SLSEEQVEDY FFQLKSQKRY HEDIFGAVFP YEVKKDGAAK QPSDPRVPAA 1150
    HGRS 1154
    Length:1,154
    Mass (Da):131,847
    Last modified:September 13, 2005 - v2
    Checksum:iD6AD3A88AE89E995
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 5211DDLKNHKHHND → KCHSLSKHRDE1 PublicationCuratedAdd
    BLAST
    Sequence conflicti56 – 561P → S in AAC15587. 1 PublicationCurated
    Sequence conflicti59 – 646ETVQKL → GTVKTS in AAC15587. 1 PublicationCurated
    Sequence conflicti68 – 8013LDKLH…LSRPQ → TIKPAAPPLACPR1 PublicationCuratedAdd
    BLAST
    Sequence conflicti91 – 922MT → RS in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti102 – 1043KGD → MGV in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti108 – 1081K → T in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti111 – 1155SCLGA → LCMGS in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti119 – 1191P → T in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti125 – 1273EPR → GPS in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti133 – 1342PD → TE in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti149 – 1491S → G in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti169 – 1691E → D in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti394 – 3952RR → SK in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti497 – 4993VWQ → LWL in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti506 – 5083QRR → HRK in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti615 – 6151K → N in AAC78630. (PubMed:9746458)Curated
    Sequence conflicti624 – 6263GSS → RSN in AAC78630. (PubMed:9746458)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077821 mRNA. Translation: AAC78630.1.
    AF032909 mRNA. Translation: AAC15587.1.
    RefSeqiNP_001003186.1. NM_001003186.1.
    UniGeneiCfa.45041.

    Genome annotation databases

    GeneIDi403822.
    KEGGicfa:403822.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077821 mRNA. Translation: AAC78630.1 .
    AF032909 mRNA. Translation: AAC15587.1 .
    RefSeqi NP_001003186.1. NM_001003186.1.
    UniGenei Cfa.45041.

    3D structure databases

    ProteinModelPortali O62699.
    SMRi O62699. Positions 80-499, 700-1127.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403822.
    KEGGi cfa:403822.

    Organism-specific databases

    CTDi 4843.

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.
    KOi K13241.

    Miscellaneous databases

    NextBioi 20817318.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    3.90.340.10. 1 hit.
    InterProi IPR003097. 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.
    IPR012144. NOS_euk.
    IPR004030. NOS_N.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF02898. NO_synthase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000333. NOS. 1 hit.
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMi SSF52218. SSF52218. 1 hit.
    SSF56512. SSF56512. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    PS60001. NOS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiNOS2_CANFA
    AccessioniPrimary (citable) accession number: O62699
    Secondary accession number(s): O97604
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3