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Q62600

- NOS3_RAT

UniProt

Q62600 - NOS3_RAT

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Protein

Nitric oxide synthase, endothelial

Gene
Nos3
Organism
Rattus norvegicus (Rat)
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.

Catalytic activityi

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

Cofactori

Heme group.
Binds 1 FAD.
Binds 1 FMN.
Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi93 – 931Zinc By similarity
Metal bindingi98 – 981Zinc By similarity
Metal bindingi183 – 1831Iron (heme axial ligand) By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi648 – 67932FMN By similarityAdd
BLAST
Nucleotide bindingi792 – 80312FAD By similarityAdd
BLAST
Nucleotide bindingi1009 – 102719NADP By similarityAdd
BLAST
Nucleotide bindingi1107 – 112216NADP By similarityAdd
BLAST

GO - Molecular functioni

  1. actin binding Source: RGD
  2. beta-catenin binding Source: RGD
  3. cadherin binding Source: RGD
  4. calmodulin binding Source: RGD
  5. flavin adenine dinucleotide binding Source: InterPro
  6. FMN binding Source: InterPro
  7. heme binding Source: InterPro
  8. Hsp90 protein binding Source: RGD
  9. iron ion binding Source: InterPro
  10. NADP binding Source: InterPro
  11. NADPH-hemoprotein reductase activity Source: RefGenome
  12. nitric-oxide synthase activity Source: RGD
  13. nitric-oxide synthase binding Source: RGD
  14. protein binding Source: IntAct
  15. scaffold protein binding Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. bone development Source: RGD
  3. cellular response to cAMP Source: RGD
  4. cellular response to growth factor stimulus Source: RGD
  5. cellular response to heat Source: RGD
  6. cellular response to magnesium ion Source: RGD
  7. cellular response to organic cyclic compound Source: RGD
  8. cellular response to transforming growth factor beta stimulus Source: RGD
  9. cellular response to tumor necrosis factor Source: RGD
  10. female pregnancy Source: RGD
  11. negative regulation of blood pressure Source: RefGenome
  12. negative regulation of smooth muscle cell proliferation Source: RGD
  13. nitric oxide biosynthetic process Source: RGD
  14. nitric oxide mediated signal transduction Source: RefGenome
  15. positive regulation of apoptotic process Source: RGD
  16. positive regulation of guanylate cyclase activity Source: RefGenome
  17. positive regulation of vasodilation Source: RefGenome
  18. response to activity Source: RGD
  19. response to amino acid Source: RGD
  20. response to axon injury Source: RGD
  21. response to candesartan Source: RGD
  22. response to corticosterone Source: RGD
  23. response to cytokine Source: RGD
  24. response to drug Source: RGD
  25. response to estradiol Source: RGD
  26. response to ethanol Source: RGD
  27. response to fructose Source: RGD
  28. response to hyperoxia Source: RGD
  29. response to hypoxia Source: RGD
  30. response to ketone Source: RGD
  31. response to lead ion Source: RGD
  32. response to lipopolysaccharide Source: RGD
  33. response to lipoprotein particle Source: RGD
  34. response to mechanical stimulus Source: RGD
  35. response to metal ion Source: RGD
  36. response to organic cyclic compound Source: RGD
  37. response to peptide Source: RGD
  38. response to peptide hormone Source: RGD
  39. response to salt Source: RGD
  40. response to statin Source: RGD
  41. retina development in camera-type eye Source: RGD
  42. signal transduction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

SABIO-RKQ62600.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3186. Nos3.

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. apical part of cell Source: RGD
  2. caveola Source: UniProtKB-SubCell
  3. cytoplasm Source: BHF-UCL
  4. cytoskeleton Source: UniProtKB-SubCell
  5. cytosol Source: RGD
  6. Golgi apparatus Source: RGD
  7. membrane raft Source: RGD
  8. mitochondrion Source: RGD
  9. nucleolus Source: RGD
  10. nucleus Source: BHF-UCL
  11. plasma membrane Source: RGD
  12. sarcolemma Source: RGD
  13. vesicle membrane Source: RGD
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 – 12021201Nitric oxide synthase, endothelialPRO_0000170946Add
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 residuei140 – 1401Phosphoserine By similarity
Modified residuei494 – 4941Phosphothreonine; by AMPK1 Publication
Modified residuei632 – 6321Phosphoserine By similarity
Modified residuei1174 – 11741Phosphothreonine By similarity
Modified residuei1176 – 11761Phosphoserine; by AMPK1 Publication

Post-translational modificationi

Phosphorylation by AMPK at Ser-1176 in the presence of Ca2+-calmodulin (CaM) activates activity. In absence of Ca2+-calmodulin, AMPK also phosphorylates Thr-494, resulting in inhibition of activity.

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

PRIDEiQ62600.

PTM databases

PhosphoSiteiQ62600.

Expressioni

Tissue specificityi

Expressed constitutively by vascular endothelium. Detected in alveolar and serosal epithelial cells as well as in endothelial cells in one day old rat. In adult lung, detected in rare endothelial cells.

Developmental stagei

Detected at high levels in lung during the late fetal and postnatal period and at lower levels in adult.

Gene expression databases

GenevestigatoriQ62600.

Interactioni

Subunit structurei

Homodimer. Interacts with NOSIP and NOSTRIN By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
CALMP621572EBI-7052018,EBI-397403From a different organism.

Protein-protein interaction databases

DIPiDIP-41833N.
IntActiQ62600. 2 interactions.
MINTiMINT-202608.

Structurei

3D structure databases

ProteinModelPortaliQ62600.
SMRiQ62600. Positions 66-480, 728-1161.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini519 – 702184Flavodoxin-likeAdd
BLAST
Domaini755 – 1001247FAD-binding FR-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 485389Interaction with NOSIP By similarityAdd
BLAST
Regioni489 – 50921Calmodulin-binding Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 6838Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the NOS family.

Phylogenomic databases

eggNOGiCOG4362.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiQ62600.
KOiK13242.
PhylomeDBiQ62600.

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.

Q62600-1 [UniParc]FASTAAdd to Basket

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MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSQ APVPPSPTRP     50
APDHSPPLTR PPDGPKFPRV KNWEVGSITY DTLSAQAQQD GPCTPRRCLG 100
SLVFPRKLQS RPTQGPSPTE QLLGQARDFI NQYYNSIKRS GSQAHEQRLQ 150
EVEAEVVATG TYQLRESELV FGAKQAWRNA PRCVGRIQWG KLQVFDARDC 200
RTAQEMFTYI CNHIKYATNR GNLRSAITVF PQRYAGRGDF RIWNSQLVRY 250
AGYRQQDGSV RGDPANVEIT ELCIQHGWTP GNGRFDVLPL LLQAPDEPPE 300
LFTLPPELVL EVPLEHPTLE WFAALGLRWY ALPAVSNMLL EIGGLEFPAA 350
PFSGWYMSSE IGMRDLCDPH RYNILEDVAV CMDLDTRTTS SLWKDKAAVE 400
INVAVLYSYQ LAKVTIVDHH AATASFMKHL ENEQKARGGC PADWAWIVPP 450
ISGSLTPVFH QEMVNYFLSP AFRYQPDPWK GSAAKGTGIT RKKTFKEVAN 500
AVKISASLMG TVMAKRVKAT ILYGSETGRA QSYAQQLGRL FRKAFDPRVL 550
CMDEYDVVSL EHEALVLVVT STFGNGDPPE NGESFAAALM EMSGPYNSSP 600
RPEQHKSYKI RFNSVSCSDP LVSSWRRKRK ESSNTDSAGA LGTLRFCVFG 650
LGSRAYPHFC AFARAVDTRL EELGGERLLQ LGQGDELCGQ EEAFRGWAQA 700
AFQAACETFC VGEDAKAAAR DIFSPKRSWK RQRYRLSTQA ESLQLLPRLT 750
HVHRRKMFQA TILSVENLQS SKSTRATILV RLDTGSQEGL QYQPGDHIGV 800
CPPNRPGLVE ALLSRVEDPP PSTEPVAVEQ LEKGSPGGPP PGWVRDPRLP 850
PCTLRQALTY FLDITSPPSP RLLRLLSTLA EESSEQQELE ALSQDPRRYE 900
EWKWFRCPTL LEVLEQFPSV ALPAPLILTQ LPLLQPRYYS VSSAPSAHPG 950
EIHLTVAVLA YRTQDGLGPL HYGVCSTWMS QLKAGDPVPC FIRGAPSFRL 1000
PPDPNLPCIL VGPGTGIAPF RGFWQDRLHD IEIKGLQPAP MTLVFGCRCS 1050
QLDHLYRDEV LDAQQRGVFG QVLTAFSRDP GSPKTYVQDL LRTELAAEVH 1100
RVLCLEQGHM FVCGDVTMAT SVLQTVQRIL ATEGSMELDE AGDVIGVLRD 1150
QQRYHEDIFG LTLRTQEVTS RIRTQSFSLQ ERQLRGAVPW SFDPPTQETP 1200
GS 1202
Length:1,202
Mass (Da):133,290
Last modified:January 23, 2007 - v4
Checksum:i52E905C3134E244D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2332QR → PS in AAC34677. 1 Publication
Sequence conflicti249 – 2491R → S in AAC34677. 1 Publication
Sequence conflicti298 – 3047Missing in AAT99567. 1 Publication
Sequence conflicti600 – 6001P → L in CAA09493. 1 Publication
Sequence conflicti735 – 7351R → G in AAT99567. 1 Publication
Sequence conflicti739 – 7391Q → P in AAT99567. 1 Publication
Sequence conflicti748 – 7481R → G in BAD15356. 1 Publication
Sequence conflicti771 – 7711S → T in AAT99567. 1 Publication
Sequence conflicti852 – 8543CTL → GTV in AAA96141. 1 Publication
Sequence conflicti966 – 9661G → V in BAD15356. 1 Publication
Sequence conflicti997 – 9982SF → FL in AAT99567. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB176831 mRNA. Translation: BAD15356.1.
AF085195 mRNA. Translation: AAC34677.1.
AY695391 mRNA. Translation: AAT99567.1.
AJ011115 mRNA. Translation: CAA09493.1.
AJ011116 mRNA. Translation: CAA09494.1.
U02534 mRNA. Translation: AAA96141.1.
AF093837 mRNA. Translation: AAC64178.1.
U18336 mRNA. Translation: AAC52188.1.
PIRiI51917.
I56979.
RefSeqiNP_068610.1. NM_021838.2.
UniGeneiRn.44265.

Genome annotation databases

GeneIDi24600.
KEGGirno:24600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB176831 mRNA. Translation: BAD15356.1 .
AF085195 mRNA. Translation: AAC34677.1 .
AY695391 mRNA. Translation: AAT99567.1 .
AJ011115 mRNA. Translation: CAA09493.1 .
AJ011116 mRNA. Translation: CAA09494.1 .
U02534 mRNA. Translation: AAA96141.1 .
AF093837 mRNA. Translation: AAC64178.1 .
U18336 mRNA. Translation: AAC52188.1 .
PIRi I51917.
I56979.
RefSeqi NP_068610.1. NM_021838.2.
UniGenei Rn.44265.

3D structure databases

ProteinModelPortali Q62600.
SMRi Q62600. Positions 66-480, 728-1161.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-41833N.
IntActi Q62600. 2 interactions.
MINTi MINT-202608.

Chemistry

BindingDBi Q62600.
ChEMBLi CHEMBL1075230.

PTM databases

PhosphoSitei Q62600.

Proteomic databases

PRIDEi Q62600.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24600.
KEGGi rno:24600.

Organism-specific databases

CTDi 4846.
RGDi 3186. Nos3.

Phylogenomic databases

eggNOGi COG4362.
HOGENOMi HOG000220884.
HOVERGENi HBG000159.
InParanoidi Q62600.
KOi K13242.
PhylomeDBi Q62600.

Enzyme and pathway databases

SABIO-RK Q62600.

Miscellaneous databases

NextBioi 603808.

Gene expression databases

Genevestigatori Q62600.

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. "NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity."
    Saitoh F., Tian Q.B., Okano A., Sakagami H., Kondo H., Suzuki T.
    J. Biol. Chem. 279:29461-29468(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Downregulation of endothelial nitric oxide synthase (NOS III) in rat aorta following in-vivo hypoxia."
    Toporsian M., Govindaraju K., Nagi M., Eidelman D., Thibault G., Ward M.E.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-288.
    Strain: Sprague-Dawley.
  3. "Increased resistance to myocardial ischemia in the Brown Norway vs. Dahl S rat: role of nitric oxide synthase and Hsp90."
    Shi Y., Hutchins W., Ogawa H., Chang C.-C., Pritchard K.A. Jr., Zhang C., Khampang P., Lazar J., Jacob H.J., Rafiee P., Baker J.E.
    J. Mol. Cell. Cardiol. 38:625-635(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-1202.
    Strain: SS/JrHsdMcwi.
    Tissue: Heart.
  4. "Cloning and expression of the rat endothelial nitric oxide synthase."
    Seidel B., Jiang L., Wolf G.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 473-672 AND 951-1192.
    Tissue: Brain.
  5. "Differential expression and induction of mRNAs encoding two inducible nitric oxide synthases in rat kidney."
    Mohaupt M.G., Elzie J.L., Ahn K.Y., Clapp W.L., Wilcox C.S., Kone B.C.
    Kidney Int. 46:653-665(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 633-862.
    Strain: Sprague-Dawley.
  6. "Endothelin-1, endothelin receptors and ecNOS mRNA expression in vital organs during traumatic shock in rats."
    Minchenko A.G., Armstead V.E., Opentanova I.L., Lefer A.M.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1015-1132.
    Strain: Sprague-Dawley.
    Tissue: Lung.
  7. "Constitutive endothelial nitric oxide synthase gene expression is regulated during lung development."
    Kawai N., Bloch D.B., Filippov G., Rabkina D., Suen H.C., Losty P.D., Janssens S.P., Zapol W.M., de la Monte S., Bloch K.D.
    Am. J. Physiol. 268:L589-L595(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1018-1080.
    Strain: Sprague-Dawley.
    Tissue: Lung.
  8. Cited for: PHOSPHORYLATION AT THR-494 AND SER-1176.

Entry informationi

Entry nameiNOS3_RAT
AccessioniPrimary (citable) accession number: Q62600
Secondary accession number(s): O88672
, O89041, Q62734, Q68GV6, Q75NE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 138 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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