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Q9TUX8

- NOS3_CANFA

UniProt

Q9TUX8 - NOS3_CANFA

Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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 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

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi96 – 961ZincBy similarity
    Metal bindingi101 – 1011ZincBy similarity
    Metal bindingi186 – 1861Iron (heme axial ligand)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi651 – 68232FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi795 – 80612FADBy similarityAdd
    BLAST
    Nucleotide bindingi937 – 94711FADBy similarityAdd
    BLAST
    Nucleotide bindingi1012 – 103019NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1110 – 112516NADPBy 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. nitric oxide biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Names & Taxonomyi

    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
    Gene namesi
    Name:NOS3
    Synonyms:NOS
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Membranecaveola By similarity. Cytoplasmcytoskeleton By similarity. Golgi apparatus By similarity. Cell membrane By similarity
    Note: Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle, which is favored by interaction with NOSIP and results in a reduced enzymatic activity.By similarity

    GO - Cellular componenti

    1. caveola Source: UniProtKB-SubCell
    2. cytoskeleton Source: UniProtKB-SubCell
    3. Golgi apparatus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 12051204Nitric oxide synthase, endothelialPRO_0000289580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi15 – 151S-palmitoyl cysteineBy similarity
    Lipidationi26 – 261S-palmitoyl cysteineBy similarity
    Modified residuei116 – 1161Phosphoserine; by CDK5By similarity
    Modified residuei143 – 1431PhosphoserineBy similarity
    Modified residuei497 – 4971Phosphothreonine; by AMPKBy similarity
    Modified residuei635 – 6351PhosphoserineBy similarity
    Modified residuei1177 – 11771PhosphothreonineBy similarity
    Modified residuei1179 – 11791Phosphoserine; by AMPKBy similarity

    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

    Interactioni

    Subunit structurei

    Homodimer. Interacts with NOSIP and NOSTRIN By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000006985.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9TUX8.
    SMRiQ9TUX8. Positions 67-482, 731-1164.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini522 – 705184Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini758 – 1004247FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni100 – 488389Interaction with NOSIPBy similarityAdd
    BLAST
    Regioni492 – 51221Calmodulin-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.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 2 hits.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9TUX8-1 [UniParc]FASTAAdd to Basket

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    MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPTSEPSR APALAPPPSP     50
    PPAPDHSSPP LTRPPDGPKF PRVKNWEVGS ITYDTLSAQS QQDGPCTPRR 100
    CLGSLVFPRK LQSRPSQNPA PPEQLLSQAR DFISQYYSSI KRSGSQAHEQ 150
    RLQEVEAEVA ATGTYQLRES ELVFGAKQAW RNAPRCVGRI QWGKLQVFDA 200
    RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRASGR GDFRIWNSQL 250
    VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE 300
    PPELFALPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF 350
    PAAPFSGWYM STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA 400
    AVEINLAVLH SYQLAKVTIV DHHAATASFM KHLENEQKAR GGCPADWAWI 450
    VPPISGSLTP VFHQEMVNYV LSPAFRYQTD PWKGSASKGA GVTRKKTFKE 500
    VANAVKISAS LMGTVMAKRV KATILYGSET GRAQSYAQQL GRLFRKAFDP 550
    RVLCMDEYDV VSLEHETLVL VVTSTFGNGD PPENGESFAA ALMEMSGSYN 600
    SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESRNTDS AGALGTLRFC 650
    VFGLGSRAYP HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFGGW 700
    AQAAFQASWE TFCVGEDAKA AARDIFSPKR TWKRQRYRLS AQAEGLQLLP 750
    GLIHVHRRKM VQATVLAVEN LQSSKSTRAT ILVRLDTGSQ EALQYQPGDH 800
    IGICPPNRPG LVEALLSRVE DPPPPGEPVA VEQLEKGSPG GPPPSWVRDP 850
    RLPPCTLRQA LTFFLDITSP PSPQLLRLLS TLAEESSEQQ ELESLSQDPR 900
    RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPSA 950
    HPGEIHLTVA VLAYRTQDGL GPLHYGVCST WLSQLKAGDP VPCFIRGAPS 1000
    FRLPPDPSLP CILVGPGTGI APFRGFWQGR LHDIYSKGLQ PAPMTLVFGC 1050
    RCSQLDHLYR DEVQDAQQRG VFGRVLTAFS REPDSPKTYV QDILRTELAA 1100
    EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME LDEAGDVIGV 1150
    LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWALDPPGP 1200
    DTVGP 1205
    Length:1,205
    Mass (Da):133,046
    Last modified:May 1, 2000 - v1
    Checksum:iC150CDEB01685BA5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143503 mRNA. Translation: AAD52161.1.
    UniGeneiCfa.108.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143503 mRNA. Translation: AAD52161.1 .
    UniGenei Cfa.108.

    3D structure databases

    ProteinModelPortali Q9TUX8.
    SMRi Q9TUX8. Positions 67-482, 731-1164.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000006985.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.

    Miscellaneous databases

    NextBioi 20817281.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 2 hits.
    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. "Assembly and characterization of canine heart endothelial nitric oxide synthase cDNA and 5'-flanking sequence by homology (RT-)PCR cloning."
      Schwemmer M., Bassenge E.
      Nitric Oxide 3:254-264(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.

    Entry informationi

    Entry nameiNOS3_CANFA
    AccessioniPrimary (citable) accession number: Q9TUX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 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