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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

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 bindingi93 – 931ZincBy similarity
Metal bindingi98 – 981ZincBy similarity
Metal bindingi183 – 1831Iron (heme axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi648 – 67932FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi792 – 80312FADBy similarityAdd
BLAST
Nucleotide bindingi1009 – 102719NADPBy similarityAdd
BLAST
Nucleotide bindingi1107 – 112216NADPBy 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. 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 mechanical stimulus Source: RGD
  8. cellular response to organic cyclic compound Source: RGD
  9. cellular response to transforming growth factor beta stimulus Source: RGD
  10. cellular response to tumor necrosis factor Source: RGD
  11. female pregnancy Source: RGD
  12. negative regulation of blood pressure Source: RefGenome
  13. negative regulation of smooth muscle cell proliferation Source: RGD
  14. nitric oxide biosynthetic process Source: RGD
  15. nitric oxide mediated signal transduction Source: RefGenome
  16. positive regulation of apoptotic process Source: RGD
  17. positive regulation of guanylate cyclase activity Source: RefGenome
  18. positive regulation of vasodilation Source: RefGenome
  19. response to activity Source: RGD
  20. response to amino acid Source: RGD
  21. response to axon injury Source: RGD
  22. response to candesartan Source: RGD
  23. response to corticosterone Source: RGD
  24. response to cytokine Source: RGD
  25. response to drug Source: RGD
  26. response to estradiol Source: RGD
  27. response to ethanol Source: RGD
  28. response to fructose Source: RGD
  29. response to hyperoxia Source: RGD
  30. response to hypoxia Source: RGD
  31. response to ketone Source: RGD
  32. response to lead ion Source: RGD
  33. response to lipopolysaccharide Source: RGD
  34. response to lipoprotein particle Source: RGD
  35. response to mechanical stimulus Source: RGD
  36. response to metal ion Source: RGD
  37. response to organic cyclic compound Source: RGD
  38. response to peptide Source: RGD
  39. response to peptide hormone Source: RGD
  40. response to salt Source: RGD
  41. response to statin Source: RGD
  42. retina development in camera-type eye Source: RGD
  43. 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. cytoplasm Source: BHF-UCL
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: RGD
  5. Golgi apparatus Source: RGD
  6. membrane raft Source: RGD
  7. mitochondrion Source: RGD
  8. nucleolus Source: RGD
  9. nucleus Source: BHF-UCL
  10. plasma membrane Source: RGD
  11. sarcolemma Source: RGD
  12. 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 – 11RemovedBy similarity
Chaini2 – 12021201Nitric oxide synthase, endothelialPRO_0000170946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi15 – 151S-palmitoyl cysteineBy similarity
Lipidationi26 – 261S-palmitoyl cysteineBy similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei494 – 4941Phosphothreonine; by AMPK1 Publication
Modified residuei632 – 6321PhosphoserineBy similarity
Modified residuei1174 – 11741PhosphothreonineBy 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.1 Publication

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).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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini519 – 702184Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini755 – 1001247FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 485389Interaction with NOSIPBy similarityAdd
BLAST
Regioni489 – 50921Calmodulin-bindingSequence AnalysisAdd
BLAST

Compositional bias

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

« Hide

        10         20         30         40         50
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSQ APVPPSPTRP
60 70 80 90 100
APDHSPPLTR PPDGPKFPRV KNWEVGSITY DTLSAQAQQD GPCTPRRCLG
110 120 130 140 150
SLVFPRKLQS RPTQGPSPTE QLLGQARDFI NQYYNSIKRS GSQAHEQRLQ
160 170 180 190 200
EVEAEVVATG TYQLRESELV FGAKQAWRNA PRCVGRIQWG KLQVFDARDC
210 220 230 240 250
RTAQEMFTYI CNHIKYATNR GNLRSAITVF PQRYAGRGDF RIWNSQLVRY
260 270 280 290 300
AGYRQQDGSV RGDPANVEIT ELCIQHGWTP GNGRFDVLPL LLQAPDEPPE
310 320 330 340 350
LFTLPPELVL EVPLEHPTLE WFAALGLRWY ALPAVSNMLL EIGGLEFPAA
360 370 380 390 400
PFSGWYMSSE IGMRDLCDPH RYNILEDVAV CMDLDTRTTS SLWKDKAAVE
410 420 430 440 450
INVAVLYSYQ LAKVTIVDHH AATASFMKHL ENEQKARGGC PADWAWIVPP
460 470 480 490 500
ISGSLTPVFH QEMVNYFLSP AFRYQPDPWK GSAAKGTGIT RKKTFKEVAN
510 520 530 540 550
AVKISASLMG TVMAKRVKAT ILYGSETGRA QSYAQQLGRL FRKAFDPRVL
560 570 580 590 600
CMDEYDVVSL EHEALVLVVT STFGNGDPPE NGESFAAALM EMSGPYNSSP
610 620 630 640 650
RPEQHKSYKI RFNSVSCSDP LVSSWRRKRK ESSNTDSAGA LGTLRFCVFG
660 670 680 690 700
LGSRAYPHFC AFARAVDTRL EELGGERLLQ LGQGDELCGQ EEAFRGWAQA
710 720 730 740 750
AFQAACETFC VGEDAKAAAR DIFSPKRSWK RQRYRLSTQA ESLQLLPRLT
760 770 780 790 800
HVHRRKMFQA TILSVENLQS SKSTRATILV RLDTGSQEGL QYQPGDHIGV
810 820 830 840 850
CPPNRPGLVE ALLSRVEDPP PSTEPVAVEQ LEKGSPGGPP PGWVRDPRLP
860 870 880 890 900
PCTLRQALTY FLDITSPPSP RLLRLLSTLA EESSEQQELE ALSQDPRRYE
910 920 930 940 950
EWKWFRCPTL LEVLEQFPSV ALPAPLILTQ LPLLQPRYYS VSSAPSAHPG
960 970 980 990 1000
EIHLTVAVLA YRTQDGLGPL HYGVCSTWMS QLKAGDPVPC FIRGAPSFRL
1010 1020 1030 1040 1050
PPDPNLPCIL VGPGTGIAPF RGFWQDRLHD IEIKGLQPAP MTLVFGCRCS
1060 1070 1080 1090 1100
QLDHLYRDEV LDAQQRGVFG QVLTAFSRDP GSPKTYVQDL LRTELAAEVH
1110 1120 1130 1140 1150
RVLCLEQGHM FVCGDVTMAT SVLQTVQRIL ATEGSMELDE AGDVIGVLRD
1160 1170 1180 1190 1200
QQRYHEDIFG LTLRTQEVTS RIRTQSFSLQ ERQLRGAVPW SFDPPTQETP

GS
Length:1,202
Mass (Da):133,290
Last modified:January 23, 2007 - v4
Checksum:i52E905C3134E244D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2332QR → PS in AAC34677. 1 PublicationCurated
Sequence conflicti249 – 2491R → S in AAC34677. 1 PublicationCurated
Sequence conflicti298 – 3047Missing in AAT99567. (PubMed:15808839)Curated
Sequence conflicti600 – 6001P → L in CAA09493. 1 PublicationCurated
Sequence conflicti735 – 7351R → G in AAT99567. (PubMed:15808839)Curated
Sequence conflicti739 – 7391Q → P in AAT99567. (PubMed:15808839)Curated
Sequence conflicti748 – 7481R → G in BAD15356. (PubMed:15105416)Curated
Sequence conflicti771 – 7711S → T in AAT99567. (PubMed:15808839)Curated
Sequence conflicti852 – 8543CTL → GTV in AAA96141. (PubMed:7527874)Curated
Sequence conflicti966 – 9661G → V in BAD15356. (PubMed:15105416)Curated
Sequence conflicti997 – 9982SF → FL in AAT99567. (PubMed:15808839)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 141 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