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Q28969

- NOS3_PIG

UniProt

Q28969 - NOS3_PIG

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Protein

Nitric oxide synthase, endothelial

Gene
NOS3, NOS
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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.

Enzyme regulationi

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

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi651 – 68232FMN By similarityAdd
BLAST
Nucleotide bindingi795 – 80612FAD By similarityAdd
BLAST
Nucleotide bindingi937 – 94711FAD By similarityAdd
BLAST
Nucleotide bindingi1012 – 103019NADP By similarityAdd
BLAST
Nucleotide bindingi1110 – 112516NADP By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 12051204Nitric oxide synthase, endothelialPRO_0000170945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Lipidationi15 – 151S-palmitoyl cysteine By similarity
Lipidationi26 – 261S-palmitoyl cysteine By similarity
Modified residuei116 – 1161Phosphoserine; by CDK5 By similarity
Modified residuei143 – 1431Phosphoserine By similarity
Modified residuei497 – 4971Phosphothreonine; by AMPK By similarity
Modified residuei635 – 6351Phosphoserine By similarity
Modified residuei1177 – 11771Phosphothreonine By similarity
Modified residuei1179 – 11791Phosphoserine; by AMPK By 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.

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Expressioni

Inductioni

Repressed by proinflammatory cytokines.

Interactioni

Subunit structurei

Homodimer. Interacts with NOSIP and NOSTRIN By similarity.

Protein-protein interaction databases

BioGridi1149683. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ28969.
SMRiQ28969. Positions 67-482, 731-1164.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini522 – 705184Flavodoxin-likeAdd
BLAST
Domaini758 – 1004247FAD-binding FR-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 488389Interaction with NOSIP By similarityAdd
BLAST
Regioni492 – 51221Calmodulin-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the NOS family.

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: September 3, 2014
This is version 124 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

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