Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi96Zinc1
Metal bindingi101Zinc1
Metal bindingi186Iron (heme axial ligand)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi651 – 682FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi795 – 806FADBy similarityAdd BLAST12
Nucleotide bindingi937 – 947FADBy similarityAdd BLAST11
Nucleotide bindingi1012 – 1030NADPBy similarityAdd BLAST19
Nucleotide bindingi1110 – 1125NADPBy similarityAdd BLAST16

GO - Molecular functioni

GO - Biological processi

  • arginine catabolic process Source: BHF-UCL
  • blood coagulation Source: UniProtKB-KW
  • cellular response to laminar fluid shear stress Source: BHF-UCL
  • mitochondrion organization Source: BHF-UCL
  • negative regulation of blood pressure Source: GO_Central
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • negative regulation of leukocyte cell-cell adhesion Source: BHF-UCL
  • nitric oxide biosynthetic process Source: BHF-UCL
  • nitric oxide mediated signal transduction Source: GO_Central
  • 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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cell membrane 1 Publication
  • Membranecaveola 1 Publication
  • Cytoplasmcytoskeleton By similarity
  • Golgi apparatus 1 Publication

  • 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

  • caveola Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • Golgi apparatus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001709412 – 1205Nitric oxide synthase, endothelialAdd BLAST1204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi15S-palmitoyl cysteine1 Publication1
Lipidationi26S-palmitoyl cysteine1 Publication1
Modified residuei116Phosphoserine; by CDK5By similarity1
Modified residuei497Phosphothreonine; by AMPK and PKA1 Publication1
Modified residuei617PhosphoserineBy similarity1
Modified residuei635Phosphoserine1 Publication1
Modified residuei640PhosphoserineBy similarity1
Modified residuei838PhosphoserineBy similarity1
Modified residuei1177PhosphothreonineBy similarity1
Modified residuei1179Phosphoserine; by AMPK, PDPK1 and PKA1 Publication1
Modified residuei1181PhosphoserineBy similarity1

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

PaxDbiP29473.
PRIDEiP29473.

PTM databases

iPTMnetiP29473.
SwissPalmiP29473.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP29473.

Structurei

Secondary structure

11205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi67 – 70Combined sources4
Beta strandi72 – 75Combined sources4
Turni76 – 79Combined sources4
Beta strandi80 – 83Combined sources4
Helixi86 – 89Combined sources4
Beta strandi98 – 101Combined sources4
Turni109 – 111Combined sources3
Beta strandi117 – 119Combined sources3
Helixi122 – 139Combined sources18
Helixi146 – 162Combined sources17
Helixi169 – 181Combined sources13
Helixi189 – 191Combined sources3
Beta strandi196 – 199Combined sources4
Helixi206 – 221Combined sources16
Helixi222 – 224Combined sources3
Beta strandi229 – 232Combined sources4
Beta strandi238 – 240Combined sources3
Beta strandi247 – 251Combined sources5
Beta strandi255 – 257Combined sources3
Beta strandi259 – 261Combined sources3
Beta strandi263 – 265Combined sources3
Helixi267 – 269Combined sources3
Helixi270 – 278Combined sources9
Beta strandi286 – 288Combined sources3
Beta strandi293 – 296Combined sources4
Beta strandi303 – 305Combined sources3
Helixi309 – 311Combined sources3
Beta strandi314 – 316Combined sources3
Helixi323 – 328Combined sources6
Beta strandi331 – 334Combined sources4
Beta strandi342 – 345Combined sources4
Beta strandi348 – 351Combined sources4
Helixi361 – 365Combined sources5
Helixi367 – 370Combined sources4
Turni372 – 375Combined sources4
Helixi378 – 384Combined sources7
Helixi392 – 394Combined sources3
Helixi396 – 414Combined sources19
Helixi422 – 440Combined sources19
Helixi447 – 450Combined sources4
Beta strandi453 – 455Combined sources3
Helixi456 – 458Combined sources3
Helixi460 – 463Combined sources4
Beta strandi468 – 470Combined sources3
Beta strandi472 – 476Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4UH7X-ray2.23A/B40-482[»]
4UH8X-ray2.30A/B40-482[»]
4UH9X-ray2.14A/B40-482[»]
4UHAX-ray2.20A/B40-482[»]
4UPQX-ray2.03A/B40-482[»]
4UPRX-ray1.93A/B40-482[»]
4UPSX-ray1.95A/B40-482[»]
4UPTX-ray2.20A/B40-482[»]
5ADJX-ray2.22A/B40-482[»]
5ADKX-ray1.80A/B40-482[»]
5ADLX-ray2.21A/B40-482[»]
5ADMX-ray2.20A/B40-482[»]
5ADNX-ray2.00A/B40-482[»]
5FJ2X-ray2.05A/B40-482[»]
5FJ3X-ray2.20A/B40-482[»]
5FVYX-ray2.10A/B40-482[»]
5FVZX-ray2.05A/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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29473.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini522 – 705Flavodoxin-likePROSITE-ProRule annotationAdd BLAST184
Domaini758 – 1004FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST247

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni100 – 488Interaction with NOSIPBy similarityAdd BLAST389
Regioni492 – 512Calmodulin-bindingSequence analysisAdd BLAST21

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

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
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-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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)DescriptionActionsGraphical viewLength
Sequence conflicti100C → R in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti165Y → I in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti318 – 328EHPTLEWFAAL → GAPHTGVVRGP in AAA30669 (PubMed:1379225).CuratedAdd BLAST11
Sequence conflicti455S → Y in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti459T → P in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti741T → A in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti804 – 805CP → SA in AAA30669 (PubMed:1379225).Curated2
Sequence conflicti857L → V in AAA30669 (PubMed:1379225).Curated1
Sequence conflicti907 – 908WF → LV in AAA30669 (PubMed:1379225).Curated2
Sequence conflicti1042A → H in AAA30669 (PubMed:1379225).Curated1

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
PDB 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[»]
4UH7X-ray2.23A/B40-482[»]
4UH8X-ray2.30A/B40-482[»]
4UH9X-ray2.14A/B40-482[»]
4UHAX-ray2.20A/B40-482[»]
4UPQX-ray2.03A/B40-482[»]
4UPRX-ray1.93A/B40-482[»]
4UPSX-ray1.95A/B40-482[»]
4UPTX-ray2.20A/B40-482[»]
5ADJX-ray2.22A/B40-482[»]
5ADKX-ray1.80A/B40-482[»]
5ADLX-ray2.21A/B40-482[»]
5ADMX-ray2.20A/B40-482[»]
5ADNX-ray2.00A/B40-482[»]
5FJ2X-ray2.05A/B40-482[»]
5FJ3X-ray2.20A/B40-482[»]
5FVYX-ray2.10A/B40-482[»]
5FVZX-ray2.05A/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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP29473.
ChEMBLiCHEMBL4802.

PTM databases

iPTMnetiP29473.
SwissPalmiP29473.

Proteomic databases

PaxDbiP29473.
PRIDEiP29473.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29473.

Enzyme and pathway databases

BRENDAi1.14.13.39. 908.

Miscellaneous databases

EvolutionaryTraceiP29473.

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-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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...

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: November 2, 2016
This is version 183 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

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 one 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.