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Q28969 (NOS3_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NOS3
Synonyms:NOS
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length1205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

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 regulation

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

Subunit structure

Homodimer. Interacts with NOSIP and NOSTRIN By similarity.

Subcellular location

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.

Induction

Repressed by proinflammatory cytokines.

Post-translational modification

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.

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 12051204Nitric oxide synthase, endothelial
PRO_0000170945

Regions

Domain522 – 705184Flavodoxin-like
Domain758 – 1004247FAD-binding FR-type
Nucleotide binding651 – 68232FMN By similarity
Nucleotide binding795 – 80612FAD By similarity
Nucleotide binding937 – 94711FAD By similarity
Nucleotide binding1012 – 103019NADP By similarity
Nucleotide binding1110 – 112516NADP By similarity
Region100 – 488389Interaction with NOSIP By similarity
Region492 – 51221Calmodulin-binding Potential

Sites

Metal binding961Zinc By similarity
Metal binding1011Zinc By similarity
Metal binding1861Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue1161Phosphoserine; by CDK5 By similarity
Modified residue1431Phosphoserine By similarity
Modified residue4971Phosphothreonine; by AMPK By similarity
Modified residue6351Phosphoserine By similarity
Modified residue11771Phosphothreonine By similarity
Modified residue11791Phosphoserine; by AMPK By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation151S-palmitoyl cysteine By similarity
Lipidation261S-palmitoyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28969 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: C5B8B5E61AADAACF

FASTA1,205133,406
        10         20         30         40         50         60 
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PATPAPEPSR APAPATPHAP EHSPAPNSPT 

        70         80         90        100        110        120 
LTRPPEGPKF PRVKNWEVGS ITYDTLCAQS QQDGPCTPRR CLGSLVLPRK LQSRPSPGPP 

       130        140        150        160        170        180 
PAEQLLSQAR DFINQYYSSI KRSGSQAHEE RLQEVEAEVA TTGTYHLGES ELVFGAKQAW 

       190        200        210        220        230        240 
RNAPRCVGRI QWGKLQVFDA RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRTPGR 

       250        260        270        280        290        300 
GDFRIWNSQL VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE 

       310        320        330        340        350        360 
PPELFALPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF PAAPFSGWYM 

       370        380        390        400        410        420 
STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA AVEINLAVLH SYQLAKVTIV 

       430        440        450        460        470        480 
DHHAATASFM KHLENEQKAR GGCPADWAWI VPPISGSLTP VFHQEMVNYV LSPAFRYQPD 

       490        500        510        520        530        540 
PWKGSAAKGT GIARKKTFKE VANAVKISAS LMATVMPKRV KASILYASET VRAQSYAQQL 

       550        560        570        580        590        600 
GRLFRKAFDP RVLCMDEYDV VSLEHETLVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN 

       610        620        630        640        650        660 
GSPRPEQHRS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC VFGLGSRAYP 

       670        680        690        700        710        720 
HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW AQAAFQASCE TFCVGEDAKA 

       730        740        750        760        770        780 
AARDIFSPKR SWKRQRYRLS AQVEGLQLLP GLVHVHRRKM FQATVLSVEN LQSSKSTRAT 

       790        800        810        820        830        840 
ILVRLDTEGQ EGLQYQPGDH IGICPPNRTG LVEALLSRVE DPTPPTESVG VEQLEKGSPG 

       850        860        870        880        890        900 
GPPPSWVRDP RLPPYTLRQA LTFFLDITSP PSPRLLRVLS TLAEEPSEQQ ELETLSQDPR 

       910        920        930        940        950        960 
RYEEWKWFRC PTLLEVLEQF PSVALPTPLL LTQLALLQPR YYSVSSAPST YPGEIHPTVA 

       970        980        990       1000       1010       1020 
VLAYRTQDGL GPLHYGVCST WLGQLKPGDP VPCFIRAAPS FRLPPDPSLP CILVGPGTGI 

      1030       1040       1050       1060       1070       1080 
APFRGFWQER LHDIESKGLQ PAPMTLVFGC RCSQLDHLYR DEVQDAQQRG VFGRVLTAFS 

      1090       1100       1110       1120       1130       1140 
REPDSPKTYV QDILRTELAA EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGNME 

      1150       1160       1170       1180       1190       1200 
LDEAGDVIGV LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWTFDPPGP 


DTPGP 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59924 mRNA. Translation: AAB39539.1.
U33832 mRNA. Translation: AAA84933.1.
RefSeqNP_999460.1. NM_214295.1.
UniGeneSsc.16364.

3D structure databases

ProteinModelPortalQ28969.
SMRQ28969. Positions 67-482, 731-1164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1149683. 1 interaction.

Chemistry

BindingDBQ28969.
ChEMBLCHEMBL3809.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397557.
KEGGssc:397557.

Organism-specific databases

CTD4846.

Phylogenomic databases

eggNOGCOG4362.
HOGENOMHOG000111088.
HOVERGENHBG000159.
KOK13242.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
3.90.340.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NO_synthase_oxygenase_dom.
IPR012144. NOS_euk.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR19384:SF5. PTHR19384:SF5. 1 hit.
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNOS3_PIG
AccessionPrimary (citable) accession number: Q28969
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families