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P29473

- NOS3_BOVIN

UniProt

P29473 - NOS3_BOVIN

Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.

    Catalytic activityi

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

    Cofactori

    Heme group.
    Binds 1 FAD.
    Binds 1 FMN.
    Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

    Enzyme regulationi

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

    Sites

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

    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: BHF-UCL

    GO - Biological processi

    1. arginine catabolic process Source: BHF-UCL
    2. blood coagulation Source: UniProtKB-KW
    3. cellular response to laminar fluid shear stress Source: BHF-UCL
    4. mitochondrion organization Source: BHF-UCL
    5. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    6. negative regulation of leukocyte cell-cell adhesion Source: BHF-UCL
    7. nitric oxide biosynthetic process Source: BHF-UCL
    8. positive regulation of guanylate cyclase activity Source: BHF-UCL

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Cell membrane 1 Publication. Membranecaveola 1 Publication. Cytoplasmcytoskeleton By similarity. Golgi apparatus 1 Publication
    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: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 12051204Nitric oxide synthase, endothelialPRO_0000170941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi15 – 151S-palmitoyl cysteine1 Publication
    Lipidationi26 – 261S-palmitoyl cysteine1 Publication
    Modified residuei116 – 1161Phosphoserine; by CDK5By similarity
    Modified residuei143 – 1431Phosphoserine; by PKA
    Modified residuei497 – 4971Phosphothreonine; by AMPK and PKA1 Publication
    Modified residuei635 – 6351Phosphoserine1 Publication
    Modified residuei1177 – 11771PhosphothreonineBy similarity
    Modified residuei1179 – 11791Phosphoserine; by AMPK, PDPK1 and PKA1 Publication

    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

    Proteomic databases

    PRIDEiP29473.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-42217N.
    MINTiMINT-1347838.
    STRINGi9913.ENSBTAP00000023515.

    Structurei

    Secondary structure

    1
    1205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi67 – 704
    Beta strandi72 – 754
    Turni76 – 794
    Beta strandi80 – 834
    Helixi86 – 894
    Beta strandi98 – 1014
    Turni109 – 1113
    Beta strandi117 – 1193
    Helixi122 – 13918
    Helixi146 – 16217
    Helixi169 – 18113
    Helixi189 – 1913
    Beta strandi196 – 1994
    Helixi206 – 22116
    Helixi222 – 2243
    Beta strandi229 – 2324
    Beta strandi238 – 2403
    Beta strandi247 – 2515
    Beta strandi255 – 2573
    Beta strandi259 – 2613
    Beta strandi263 – 2653
    Helixi267 – 2693
    Helixi270 – 2789
    Beta strandi286 – 2883
    Beta strandi293 – 2964
    Beta strandi303 – 3053
    Helixi309 – 3113
    Beta strandi314 – 3163
    Helixi323 – 3286
    Beta strandi331 – 3344
    Beta strandi342 – 3454
    Beta strandi348 – 3514
    Helixi361 – 3655
    Helixi367 – 3704
    Turni372 – 3754
    Helixi378 – 3847
    Helixi392 – 3943
    Helixi396 – 41419
    Helixi422 – 44019
    Helixi447 – 4504
    Beta strandi453 – 4553
    Helixi456 – 4583
    Helixi460 – 4634
    Beta strandi468 – 4703
    Beta strandi472 – 4765

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D0CX-ray1.65A/B39-482[»]
    1D0OX-ray1.95A/B39-482[»]
    1D1VX-ray1.93A/B39-482[»]
    1D1WX-ray2.00A/B39-482[»]
    1D1XX-ray2.00A/B39-482[»]
    1D1YX-ray2.20A/B39-482[»]
    1DM6X-ray1.95A/B39-482[»]
    1DM7X-ray2.10A/B39-482[»]
    1DM8X-ray2.25A/B39-482[»]
    1DMIX-ray2.00A/B39-482[»]
    1DMJX-ray2.35A/B39-482[»]
    1DMKX-ray1.90A/B39-482[»]
    1ED4X-ray1.86A/B39-482[»]
    1ED5X-ray1.80A/B39-482[»]
    1ED6X-ray2.05A/B39-482[»]
    1FOIX-ray1.93A/B39-482[»]
    1FOJX-ray2.10A/B39-482[»]
    1FOLX-ray2.20A/B39-482[»]
    1FOOX-ray2.00A/B39-482[»]
    1FOPX-ray2.30A/B39-482[»]
    1I83X-ray2.00A/B39-482[»]
    1NSEX-ray1.90A/B39-482[»]
    1P6LX-ray2.35A/B67-483[»]
    1P6MX-ray2.27A/B67-483[»]
    1P6NX-ray2.50A/B67-483[»]
    1Q2OX-ray1.74A/B67-482[»]
    1RS8X-ray2.30A/B67-482[»]
    1RS9X-ray2.22A/B67-482[»]
    1ZZSX-ray1.85A/B67-482[»]
    1ZZTX-ray2.14A/B67-482[»]
    2G6OX-ray1.90A/B67-482[»]
    2HX2X-ray1.95A/B67-482[»]
    2NSEX-ray2.34A/B39-482[»]
    3DQSX-ray2.03A/B67-482[»]
    3DQTX-ray2.54A/B67-482[»]
    3E7SX-ray2.50A/B57-487[»]
    3JWWX-ray2.20A/B39-482[»]
    3JWXX-ray2.00A/B39-482[»]
    3JWYX-ray2.24A/B39-482[»]
    3JWZX-ray2.40A/B39-482[»]
    3N5PX-ray2.39A/B39-482[»]
    3N5QX-ray2.90A/B39-482[»]
    3N5RX-ray2.57A/B39-482[»]
    3N5SX-ray2.18A/B39-482[»]
    3N5TX-ray2.52A/B39-482[»]
    3NLDX-ray2.28A/B39-482[»]
    3NLEX-ray1.95A/B39-482[»]
    3NLFX-ray2.32A/B39-482[»]
    3NLGX-ray2.38A/B39-482[»]
    3NLHX-ray2.10A/B39-482[»]
    3NLIX-ray1.98A/B39-482[»]
    3NLTX-ray2.74A/B39-482[»]
    3NLUX-ray2.65A/B39-482[»]
    3NSEX-ray2.10A/B39-482[»]
    3PNHX-ray1.93A/B67-482[»]
    3RQOX-ray2.08A/B40-482[»]
    3RQPX-ray2.35A/B40-482[»]
    4C3AX-ray2.20A/B40-482[»]
    4CARX-ray2.05A/B40-482[»]
    4CFTX-ray1.79A/B40-482[»]
    4CTYX-ray2.30A/B40-482[»]
    4CTZX-ray2.01A/B40-482[»]
    4CU0X-ray2.08A/B40-482[»]
    4CU1X-ray1.89A/B40-482[»]
    4CULX-ray2.23A/B40-482[»]
    4CUMX-ray2.33A/B40-482[»]
    4CUNX-ray2.48A/B40-482[»]
    4CVGX-ray2.31A/B40-482[»]
    4IMXX-ray2.25A/B40-482[»]
    4JSKX-ray2.28A/B40-482[»]
    4JSLX-ray2.04A/B40-482[»]
    4JSMX-ray2.25A/B40-482[»]
    4K5HX-ray2.25A/B40-482[»]
    4K5IX-ray2.08A/B40-482[»]
    4K5JX-ray2.36A/B40-482[»]
    4K5KX-ray2.00A/B40-482[»]
    4KCPX-ray2.07A/B40-482[»]
    4KCQX-ray2.03A/B40-482[»]
    4KCRX-ray2.09A/B40-482[»]
    4KCSX-ray2.05A/B40-482[»]
    4LUWX-ray2.25A/B41-482[»]
    4NSEX-ray1.95A/B39-482[»]
    5NSEX-ray1.90A/B39-482[»]
    6NSEX-ray2.35A/B39-482[»]
    7NSEX-ray2.35A/B39-482[»]
    8NSEX-ray2.25A/B39-482[»]
    9NSEX-ray2.24A/B39-482[»]
    ProteinModelPortaliP29473.
    SMRiP29473. Positions 67-482, 731-1164.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29473.

    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.
    InParanoidiP29473.

    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.

    P29473-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSR APAPATPHAP     50
    DHSPAPNSPT LTRPPEGPKF PRVKNWELGS ITYDTLCAQS QQDGPCTPRC 100
    CLGSLVLPRK LQTRPSPGPP PAEQLLSQAR DFINQYYSSI KRSGSQAHEE 150
    RLQEVEAEVA STGTYHLRES ELVFGAKQAW RNAPRCVGRI QWGKLQVFDA 200
    RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRAPGR GDFRIWNSQL 250
    VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE 300
    APELFVLPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF 350
    SAAPFSGWYM STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA 400
    AVEINLAVLH SFQLAKVTIV DHHAATVSFM KHLDNEQKAR GGCPADWAWI 450
    VPPISGSLTP VFHQEMVNYI LSPAFRYQPD PWKGSATKGA GITRKKTFKE 500
    VANAVKISAS LMGTLMAKRV KATILYASET GRAQSYAQQL GRLFRKAFDP 550
    RVLCMDEYDV VSLEHEALVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN 600
    SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC 650
    VFGLGSRAYP HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW 700
    AKAAFQASCE TFCVGEEAKA AAQDIFSPKR SWKRQRYRLS TQAEGLQLLP 750
    GLIHVHRRKM FQATVLSVEN LQSSKSTRAT ILVRLDTAGQ EGLQYQPGDH 800
    IGICPPNRPG LVEALLSRVE DPPPPTESVA VEQLEKGSPG GPPPSWVRDP 850
    RLPPCTLRQA LTFFLDITSP PSPRLLRLLS TLAEEPSEQQ ELETLSQDPR 900
    RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPNA 950
    HPGEVHLTVA VLAYRTQDGL GPLHYGVCST WLSQLKTGDP VPCFIRGAPS 1000
    FRLPPDPYVP CILVGPGTGI APFRGFWQER LHDIESKGLQ PAPMTLVFGC 1050
    RCSQLDHLYR DEVQDAQERG VFGRVLTAFS REPDSPKTYV QDILRTELAA 1100
    EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME LDEAGDVIGV 1150
    LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWAFDPPGP 1200
    DTPGP 1205
    Length:1,205
    Mass (Da):133,287
    Last modified:January 23, 2007 - v3
    Checksum:i5DC8FF4F25870281
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001C → R in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti165 – 1651Y → I in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti318 – 32811EHPTLEWFAAL → GAPHTGVVRGP in AAA30669. (PubMed:1379225)CuratedAdd
    BLAST
    Sequence conflicti455 – 4551S → Y in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti459 – 4591T → P in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti741 – 7411T → A in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti804 – 8052CP → SA in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti857 – 8571L → V in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti907 – 9082WF → LV in AAA30669. (PubMed:1379225)Curated
    Sequence conflicti1042 – 10421A → H in AAA30669. (PubMed:1379225)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M99057 mRNA. Translation: AAA30667.1.
    M89952 mRNA. Translation: AAA30494.1.
    M95674 mRNA. Translation: AAA30669.1.
    PIRiA38943.
    UniGeneiBt.4662.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M99057 mRNA. Translation: AAA30667.1 .
    M89952 mRNA. Translation: AAA30494.1 .
    M95674 mRNA. Translation: AAA30669.1 .
    PIRi A38943.
    UniGenei Bt.4662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D0C X-ray 1.65 A/B 39-482 [» ]
    1D0O X-ray 1.95 A/B 39-482 [» ]
    1D1V X-ray 1.93 A/B 39-482 [» ]
    1D1W X-ray 2.00 A/B 39-482 [» ]
    1D1X X-ray 2.00 A/B 39-482 [» ]
    1D1Y X-ray 2.20 A/B 39-482 [» ]
    1DM6 X-ray 1.95 A/B 39-482 [» ]
    1DM7 X-ray 2.10 A/B 39-482 [» ]
    1DM8 X-ray 2.25 A/B 39-482 [» ]
    1DMI X-ray 2.00 A/B 39-482 [» ]
    1DMJ X-ray 2.35 A/B 39-482 [» ]
    1DMK X-ray 1.90 A/B 39-482 [» ]
    1ED4 X-ray 1.86 A/B 39-482 [» ]
    1ED5 X-ray 1.80 A/B 39-482 [» ]
    1ED6 X-ray 2.05 A/B 39-482 [» ]
    1FOI X-ray 1.93 A/B 39-482 [» ]
    1FOJ X-ray 2.10 A/B 39-482 [» ]
    1FOL X-ray 2.20 A/B 39-482 [» ]
    1FOO X-ray 2.00 A/B 39-482 [» ]
    1FOP X-ray 2.30 A/B 39-482 [» ]
    1I83 X-ray 2.00 A/B 39-482 [» ]
    1NSE X-ray 1.90 A/B 39-482 [» ]
    1P6L X-ray 2.35 A/B 67-483 [» ]
    1P6M X-ray 2.27 A/B 67-483 [» ]
    1P6N X-ray 2.50 A/B 67-483 [» ]
    1Q2O X-ray 1.74 A/B 67-482 [» ]
    1RS8 X-ray 2.30 A/B 67-482 [» ]
    1RS9 X-ray 2.22 A/B 67-482 [» ]
    1ZZS X-ray 1.85 A/B 67-482 [» ]
    1ZZT X-ray 2.14 A/B 67-482 [» ]
    2G6O X-ray 1.90 A/B 67-482 [» ]
    2HX2 X-ray 1.95 A/B 67-482 [» ]
    2NSE X-ray 2.34 A/B 39-482 [» ]
    3DQS X-ray 2.03 A/B 67-482 [» ]
    3DQT X-ray 2.54 A/B 67-482 [» ]
    3E7S X-ray 2.50 A/B 57-487 [» ]
    3JWW X-ray 2.20 A/B 39-482 [» ]
    3JWX X-ray 2.00 A/B 39-482 [» ]
    3JWY X-ray 2.24 A/B 39-482 [» ]
    3JWZ X-ray 2.40 A/B 39-482 [» ]
    3N5P X-ray 2.39 A/B 39-482 [» ]
    3N5Q X-ray 2.90 A/B 39-482 [» ]
    3N5R X-ray 2.57 A/B 39-482 [» ]
    3N5S X-ray 2.18 A/B 39-482 [» ]
    3N5T X-ray 2.52 A/B 39-482 [» ]
    3NLD X-ray 2.28 A/B 39-482 [» ]
    3NLE X-ray 1.95 A/B 39-482 [» ]
    3NLF X-ray 2.32 A/B 39-482 [» ]
    3NLG X-ray 2.38 A/B 39-482 [» ]
    3NLH X-ray 2.10 A/B 39-482 [» ]
    3NLI X-ray 1.98 A/B 39-482 [» ]
    3NLT X-ray 2.74 A/B 39-482 [» ]
    3NLU X-ray 2.65 A/B 39-482 [» ]
    3NSE X-ray 2.10 A/B 39-482 [» ]
    3PNH X-ray 1.93 A/B 67-482 [» ]
    3RQO X-ray 2.08 A/B 40-482 [» ]
    3RQP X-ray 2.35 A/B 40-482 [» ]
    4C3A X-ray 2.20 A/B 40-482 [» ]
    4CAR X-ray 2.05 A/B 40-482 [» ]
    4CFT X-ray 1.79 A/B 40-482 [» ]
    4CTY X-ray 2.30 A/B 40-482 [» ]
    4CTZ X-ray 2.01 A/B 40-482 [» ]
    4CU0 X-ray 2.08 A/B 40-482 [» ]
    4CU1 X-ray 1.89 A/B 40-482 [» ]
    4CUL X-ray 2.23 A/B 40-482 [» ]
    4CUM X-ray 2.33 A/B 40-482 [» ]
    4CUN X-ray 2.48 A/B 40-482 [» ]
    4CVG X-ray 2.31 A/B 40-482 [» ]
    4IMX X-ray 2.25 A/B 40-482 [» ]
    4JSK X-ray 2.28 A/B 40-482 [» ]
    4JSL X-ray 2.04 A/B 40-482 [» ]
    4JSM X-ray 2.25 A/B 40-482 [» ]
    4K5H X-ray 2.25 A/B 40-482 [» ]
    4K5I X-ray 2.08 A/B 40-482 [» ]
    4K5J X-ray 2.36 A/B 40-482 [» ]
    4K5K X-ray 2.00 A/B 40-482 [» ]
    4KCP X-ray 2.07 A/B 40-482 [» ]
    4KCQ X-ray 2.03 A/B 40-482 [» ]
    4KCR X-ray 2.09 A/B 40-482 [» ]
    4KCS X-ray 2.05 A/B 40-482 [» ]
    4LUW X-ray 2.25 A/B 41-482 [» ]
    4NSE X-ray 1.95 A/B 39-482 [» ]
    5NSE X-ray 1.90 A/B 39-482 [» ]
    6NSE X-ray 2.35 A/B 39-482 [» ]
    7NSE X-ray 2.35 A/B 39-482 [» ]
    8NSE X-ray 2.25 A/B 39-482 [» ]
    9NSE X-ray 2.24 A/B 39-482 [» ]
    ProteinModelPortali P29473.
    SMRi P29473. Positions 67-482, 731-1164.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-42217N.
    MINTi MINT-1347838.
    STRINGi 9913.ENSBTAP00000023515.

    Chemistry

    BindingDBi P29473.
    ChEMBLi CHEMBL4802.

    Proteomic databases

    PRIDEi P29473.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.
    InParanoidi P29473.

    Miscellaneous databases

    EvolutionaryTracei P29473.
    NextBioi 20806546.

    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. "Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct constitutive enzyme isoform."
      Lamas S., Marsden P.A., Li G.K., Tempst P., Michel T.
      Proc. Natl. Acad. Sci. U.S.A. 89:6348-6352(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and characterization of the constitutive bovine aortic endothelial cell nitric oxide synthase."
      Nishida K., Harrison D.G., Navas J.P., Fisher A.A., Dockery S.P., Uematsu M., Nerem R.M., Alexander R.W., Murphy T.J.
      J. Clin. Invest. 90:2092-2096(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Molecular cloning and expression of a cDNA encoding endothelial cell nitric oxide synthase."
      Sessa W.C., Harrison J.K., Barber C.M., Zeng D., Durieux M.E., D'Angelo D.D., Lynch K.R., Peach M.J.
      J. Biol. Chem. 267:15274-15276(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Aortic endothelium.
    4. "Endothelial nitric oxide synthase. N-terminal myristoylation determines subcellular localization."
      Busconi L., Michel T.
      J. Biol. Chem. 268:8410-8413(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    5. "Mutagenesis of palmitoylation sites in endothelial nitric oxide synthase identifies a novel motif for dual acylation and subcellular targeting."
      Robinson L.J., Michel T.
      Proc. Natl. Acad. Sci. U.S.A. 92:11776-11780(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-15 AND CYS-26.
    6. "Shear stress stimulates phosphorylation of eNOS at Ser(635) by a protein kinase A-dependent mechanism."
      Boo Y.C., Hwang J., Sykes M., Michell B.J., Kemp B.E., Lum H., Jo H.
      Am. J. Physiol. 283:H1819-H1828(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-497; SER-635 AND SER-1179.
    7. "Aberrant cytoplasmic sequestration of eNOS in endothelial cells after monocrotaline, hypoxia, and senescence: live-cell caveolar and cytoplasmic NO imaging."
      Mukhopadhyay S., Xu F., Sehgal P.B.
      Am. J. Physiol. 292:H1373-H1389(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center."
      Raman C.S., Li H., Martasek P., Kral V., Masters B.S.S., Poulos T.L.
      Cell 95:939-950(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 67-482.
    9. "Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas."
      Li H., Raman C.S., Martasek P., Kral V., Masters B.S.S., Poulos T.L.
      J. Inorg. Biochem. 81:133-139(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 67-482.
    10. "Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors."
      Li H., Raman C.S., Martasek P., Masters B.S.S., Poulos T.L.
      Biochemistry 40:5399-5406(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
    11. "Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism."
      Raman C.S., Li H., Martasek P., Southan G., Masters B.S.S., Poulos T.L.
      Biochemistry 40:13448-13455(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    12. "Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase."
      Raman C.S., Li H., Martasek P., Babu B.R., Griffith O.W., Southan G., Masters B.S.S., Poulos T.L.
      J. Biol. Chem. 276:26486-26491(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
    13. "Structural basis for pterin antagonism in nitric-oxide synthase. Development of novel 4-oxo-pteridine antagonists of (6R)-5,6,7,8-tetrahydrobiopterin."
      Kotsonis P., Frohlich L.G., Raman C.S., Li H., Berg M., Gerwig R., Groehn V., Kang Y., Al-Masoudi N., Taghavi-Moghadam S., Mohr D., Munch U., Schnabel J., Martasek P., Masters B.S.S., Strobel H., Poulos T., Matter H., Pfleiderer W., Schmidt H.H.H.W.
      J. Biol. Chem. 276:49133-49141(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).

    Entry informationi

    Entry nameiNOS3_BOVIN
    AccessioniPrimary (citable) accession number: P29473
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3