Nitric oxide synthase, endothelial

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Q28969 (NOS3_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	NOS3
Synonyms:	NOS

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	1205 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Membrane › caveola By similarity. Cytoplasm › cytoskeleton 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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Golgi apparatus Membrane
Ligand	Calcium Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP Zinc
Molecular function	Oxidoreductase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell caveola Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1205

1205

Nitric oxide synthase, endothelial

PRO_0000170945

Regions

Domain

522 – 705

184

Flavodoxin-like

Domain

758 – 1004

247

FAD-binding FR-type

Nucleotide binding

651 – 682

FMN By similarity

Nucleotide binding

795 – 806

FAD By similarity

Nucleotide binding

937 – 947

FAD By similarity

Nucleotide binding

1012 – 1030

NADP By similarity

Nucleotide binding

1110 – 1125

NADP By similarity

Region

100 – 488

389

Interaction with NOSIP By similarity

Region

492 – 512

Calmodulin-binding Potential

Sites

Metal binding

Zinc By similarity

Metal binding

101

Zinc By similarity

Metal binding

186

Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue

116

Phosphoserine; by CDK5 By similarity

Modified residue

143

Phosphoserine By similarity

Modified residue

497

Phosphothreonine; by AMPK By similarity

Modified residue

635

Phosphoserine By similarity

Modified residue

1177

Phosphothreonine By similarity

Modified residue

1179

Phosphoserine; by AMPK By similarity

Lipidation

N-myristoyl glycine By similarity

Lipidation

S-palmitoyl cysteine By similarity

Lipidation

S-palmitoyl cysteine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q28969 [UniParc].

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

1,205

133,406

        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

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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.
RefSeq	NP_999460.1. NM_214295.1.
UniGene	Ssc.16364.
3D structure databases
ProteinModelPortal	Q28969.
SMR	Q28969. Positions 67-482, 731-1164.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397557.
KEGG	ssc:397557.
Organism-specific databases
CTD	4846.
Phylogenomic databases
eggNOG	COG4362.
HOGENOM	HOG000111088.
HOVERGEN	HBG000159.
KO	K13242.
OrthoDB	EOG4ZS92B.
Family and domain databases
Gene3D	1.20.990.10. 1 hit. 3.90.340.10. 1 hit.
InterPro	IPR003097. 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. IPR026009. NOS. IPR012144. NOS_met. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
PANTHER	PTHR19384:SF5. PTHR19384:SF5. 1 hit.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. PF02898. NO_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF000333. NOS. 1 hit.
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
SUPFAM	SSF56512. NO_synthase_oxygenase_reg. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. PS60001. NOS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q28969.
ChEMBL	CHEMBL3809.

Entry information

Entry name

NOS3_PIG

Accession

Primary (citable) accession number: Q28969

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 116 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents