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Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

Enzyme and pathway databases

BRENDAi1.14.13.39. 908.

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 Componenti: Unplaced

Subcellular locationi

  1. Cell membrane 1 Publication
  2. Membranecaveola 1 Publication
  3. Cytoplasmcytoskeleton By similarity
  4. Golgi apparatus 1 Publication

  5. 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
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
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 residuei497 – 4971Phosphothreonine; by AMPK and PKA1 Publication
Modified residuei635 – 6351Phosphoserine1 Publication
Modified residuei640 – 6401PhosphoserineBy similarity
Modified residuei838 – 8381PhosphoserineBy similarity
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 – 704Combined sources
Beta strandi72 – 754Combined sources
Turni76 – 794Combined sources
Beta strandi80 – 834Combined sources
Helixi86 – 894Combined sources
Beta strandi98 – 1014Combined sources
Turni109 – 1113Combined sources
Beta strandi117 – 1193Combined sources
Helixi122 – 13918Combined sources
Helixi146 – 16217Combined sources
Helixi169 – 18113Combined sources
Helixi189 – 1913Combined sources
Beta strandi196 – 1994Combined sources
Helixi206 – 22116Combined sources
Helixi222 – 2243Combined sources
Beta strandi229 – 2324Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi263 – 2653Combined sources
Helixi267 – 2693Combined sources
Helixi270 – 2789Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi303 – 3053Combined sources
Helixi309 – 3113Combined sources
Beta strandi314 – 3163Combined sources
Helixi323 – 3286Combined sources
Beta strandi331 – 3344Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi348 – 3514Combined sources
Helixi361 – 3655Combined sources
Helixi367 – 3704Combined sources
Turni372 – 3754Combined sources
Helixi378 – 3847Combined sources
Helixi392 – 3943Combined sources
Helixi396 – 41419Combined sources
Helixi422 – 44019Combined sources
Helixi447 – 4504Combined sources
Beta strandi453 – 4553Combined sources
Helixi456 – 4583Combined sources
Helixi460 – 4634Combined sources
Beta strandi468 – 4703Combined sources
Beta strandi472 – 4765Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4CWVX-ray2.34A/B40-482[»]
4CWWX-ray2.16A/B40-482[»]
4CWXX-ray2.15A/B40-482[»]
4CWYX-ray2.15A/B40-482[»]
4CWZX-ray2.08A/B40-482[»]
4CX0X-ray2.20A/B40-482[»]
4CX1X-ray2.13A/B40-482[»]
4CX2X-ray2.04A/B40-482[»]
4D33X-ray2.09A/B40-482[»]
4D34X-ray2.25A/B40-482[»]
4D35X-ray2.18A/B40-482[»]
4D36X-ray2.05A/B40-482[»]
4D37X-ray2.10A/B40-482[»]
4D38X-ray2.30A/B40-482[»]
4D39X-ray2.00A/B40-482[»]
4D3AX-ray2.25A/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[»]
4UPQX-ray2.03A/B40-482[»]
4UPRX-ray1.93A/B40-482[»]
4UPSX-ray1.95A/B40-482[»]
4UPTX-ray2.20A/B40-482[»]
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

        10         20         30         40         50
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSR APAPATPHAP
60 70 80 90 100
DHSPAPNSPT LTRPPEGPKF PRVKNWELGS ITYDTLCAQS QQDGPCTPRC
110 120 130 140 150
CLGSLVLPRK LQTRPSPGPP PAEQLLSQAR DFINQYYSSI KRSGSQAHEE
160 170 180 190 200
RLQEVEAEVA STGTYHLRES ELVFGAKQAW RNAPRCVGRI QWGKLQVFDA
210 220 230 240 250
RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRAPGR GDFRIWNSQL
260 270 280 290 300
VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE
310 320 330 340 350
APELFVLPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF
360 370 380 390 400
SAAPFSGWYM STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA
410 420 430 440 450
AVEINLAVLH SFQLAKVTIV DHHAATVSFM KHLDNEQKAR GGCPADWAWI
460 470 480 490 500
VPPISGSLTP VFHQEMVNYI LSPAFRYQPD PWKGSATKGA GITRKKTFKE
510 520 530 540 550
VANAVKISAS LMGTLMAKRV KATILYASET GRAQSYAQQL GRLFRKAFDP
560 570 580 590 600
RVLCMDEYDV VSLEHEALVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN
610 620 630 640 650
SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC
660 670 680 690 700
VFGLGSRAYP HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW
710 720 730 740 750
AKAAFQASCE TFCVGEEAKA AAQDIFSPKR SWKRQRYRLS TQAEGLQLLP
760 770 780 790 800
GLIHVHRRKM FQATVLSVEN LQSSKSTRAT ILVRLDTAGQ EGLQYQPGDH
810 820 830 840 850
IGICPPNRPG LVEALLSRVE DPPPPTESVA VEQLEKGSPG GPPPSWVRDP
860 870 880 890 900
RLPPCTLRQA LTFFLDITSP PSPRLLRLLS TLAEEPSEQQ ELETLSQDPR
910 920 930 940 950
RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPNA
960 970 980 990 1000
HPGEVHLTVA VLAYRTQDGL GPLHYGVCST WLSQLKTGDP VPCFIRGAPS
1010 1020 1030 1040 1050
FRLPPDPYVP CILVGPGTGI APFRGFWQER LHDIESKGLQ PAPMTLVFGC
1060 1070 1080 1090 1100
RCSQLDHLYR DEVQDAQERG VFGRVLTAFS REPDSPKTYV QDILRTELAA
1110 1120 1130 1140 1150
EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME LDEAGDVIGV
1160 1170 1180 1190 1200
LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWAFDPPGP

DTPGP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M99057 mRNA. Translation: AAA30667.1.
M89952 mRNA. Translation: AAA30494.1.
M95674 mRNA. Translation: AAA30669.1.
PIRiA38943.
UniGeneiBt.4662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4CWVX-ray2.34A/B40-482[»]
4CWWX-ray2.16A/B40-482[»]
4CWXX-ray2.15A/B40-482[»]
4CWYX-ray2.15A/B40-482[»]
4CWZX-ray2.08A/B40-482[»]
4CX0X-ray2.20A/B40-482[»]
4CX1X-ray2.13A/B40-482[»]
4CX2X-ray2.04A/B40-482[»]
4D33X-ray2.09A/B40-482[»]
4D34X-ray2.25A/B40-482[»]
4D35X-ray2.18A/B40-482[»]
4D36X-ray2.05A/B40-482[»]
4D37X-ray2.10A/B40-482[»]
4D38X-ray2.30A/B40-482[»]
4D39X-ray2.00A/B40-482[»]
4D3AX-ray2.25A/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[»]
4UPQX-ray2.03A/B40-482[»]
4UPRX-ray1.93A/B40-482[»]
4UPSX-ray1.95A/B40-482[»]
4UPTX-ray2.20A/B40-482[»]
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiP29473.
ChEMBLiCHEMBL4802.

Proteomic databases

PRIDEiP29473.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG4362.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29473.

Enzyme and pathway databases

BRENDAi1.14.13.39. 908.

Miscellaneous databases

EvolutionaryTraceiP29473.
NextBioi20806546.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 173 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.