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Q28969

- NOS3_PIG

UniProt

Q28969 - NOS3_PIG

Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 4 (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 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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: 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_0000170945Add
    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

    Expressioni

    Inductioni

    Repressed by proinflammatory cytokines.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi1149683. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ28969.
    SMRiQ28969. 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.
    HOGENOMiHOG000111088.
    HOVERGENiHBG000159.
    KOiK13242.

    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.

    Q28969-1 [UniParc]FASTAAdd to Basket

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    MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PATPAPEPSR APAPATPHAP     50
    EHSPAPNSPT LTRPPEGPKF PRVKNWEVGS ITYDTLCAQS QQDGPCTPRR 100
    CLGSLVLPRK LQSRPSPGPP PAEQLLSQAR DFINQYYSSI KRSGSQAHEE 150
    RLQEVEAEVA TTGTYHLGES ELVFGAKQAW RNAPRCVGRI QWGKLQVFDA 200
    RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRTPGR 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 LSPAFRYQPD PWKGSAAKGT GIARKKTFKE 500
    VANAVKISAS LMATVMPKRV KASILYASET VRAQSYAQQL GRLFRKAFDP 550
    RVLCMDEYDV VSLEHETLVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN 600
    GSPRPEQHRS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC 650
    VFGLGSRAYP HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW 700
    AQAAFQASCE TFCVGEDAKA AARDIFSPKR SWKRQRYRLS AQVEGLQLLP 750
    GLVHVHRRKM FQATVLSVEN LQSSKSTRAT ILVRLDTEGQ EGLQYQPGDH 800
    IGICPPNRTG LVEALLSRVE DPTPPTESVG VEQLEKGSPG GPPPSWVRDP 850
    RLPPYTLRQA LTFFLDITSP PSPRLLRVLS TLAEEPSEQQ ELETLSQDPR 900
    RYEEWKWFRC PTLLEVLEQF PSVALPTPLL LTQLALLQPR YYSVSSAPST 950
    YPGEIHPTVA VLAYRTQDGL GPLHYGVCST WLGQLKPGDP VPCFIRAAPS 1000
    FRLPPDPSLP CILVGPGTGI APFRGFWQER LHDIESKGLQ PAPMTLVFGC 1050
    RCSQLDHLYR DEVQDAQQRG VFGRVLTAFS REPDSPKTYV QDILRTELAA 1100
    EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGNME LDEAGDVIGV 1150
    LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWTFDPPGP 1200
    DTPGP 1205
    Length:1,205
    Mass (Da):133,406
    Last modified:January 23, 2007 - v4
    Checksum:iC5B8B5E61AADAACF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59924 mRNA. Translation: AAB39539.1.
    U33832 mRNA. Translation: AAA84933.1.
    RefSeqiNP_999460.1. NM_214295.1.
    UniGeneiSsc.16364.

    Genome annotation databases

    GeneIDi397557.
    KEGGissc:397557.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59924 mRNA. Translation: AAB39539.1 .
    U33832 mRNA. Translation: AAA84933.1 .
    RefSeqi NP_999460.1. NM_214295.1.
    UniGenei Ssc.16364.

    3D structure databases

    ProteinModelPortali Q28969.
    SMRi Q28969. Positions 67-482, 731-1164.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1149683. 1 interaction.

    Chemistry

    BindingDBi Q28969.
    ChEMBLi CHEMBL3809.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397557.
    KEGGi ssc:397557.

    Organism-specific databases

    CTDi 4846.

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000111088.
    HOVERGENi HBG000159.
    KOi K13242.

    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. "Molecular cloning, characterization and expression of a nitric oxide synthase from porcine pulmonary artery endothelial cells."
      Zhang J., Patel J.M., Block E.R.
      Comp. Biochem. Physiol. 116B:485-491(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Tissue: Pulmonary artery.
    2. Patel J.M., Block E.R.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1032-1205.

    Entry informationi

    Entry nameiNOS3_PIG
    AccessioniPrimary (citable) accession number: Q28969
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 4 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