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UniProtKB/Swiss-Prot entry P29473


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NOS3_BOVIN
Primary accession number P29473
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 23, 2008 (Entry version 107)
Name and origin of the protein
Protein name Nitric oxide synthase, endothelial
Synonyms EC 1.14.13.39
Endothelial NOS
eNOS
EC-NOS
NOS type III
NOSIII
Constitutive NOS
cNOS
Gene name
Name: NOS3
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1378626 [NCBI, ExPASy, EBI, Israel, Japan]
Lamas S., Marsden P.A., Li G.K., Tempst P., Michel T.;
"Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct constitutive enzyme isoform.";
Proc. Natl. Acad. Sci. U.S.A. 89:6348-6352(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1385480 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Molecular cloning and characterization of the constitutive bovine aortic endothelial cell nitric oxide synthase.";
J. Clin. Invest. 90:2092-2096(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aortic endothelium;
PubMed=1379225 [NCBI, ExPASy, EBI, Israel, Japan]
Sessa W.C., Harrison J.K., Barber C.M., Zeng D., Durieux M.E., D'Angelo D.D., Lynch K.R., Peach M.J.;
"Molecular cloning and expression of a cDNA encoding endothelial cell nitric oxide synthase.";
J. Biol. Chem. 267:15274-15276(1992).
[4]
MYRISTOYLATION AT GLY-2.
PubMed=7682550 [NCBI, ExPASy, EBI, Israel, Japan]
Busconi L., Michel T.;
"Endothelial nitric oxide synthase. N-terminal myristoylation determines subcellular localization.";
J. Biol. Chem. 268:8410-8413(1993).
[5]
PALMITOYLATION AT CYS-15 AND CYS-26.
PubMed=8524847 [NCBI, ExPASy, EBI, Israel, Japan]
Robinson L.J., Michel T.;
"Mutagenesis of palmitoylation sites in endothelial nitric oxide synthase identifies a novel motif for dual acylation and subcellular targeting.";
Proc. Natl. Acad. Sci. U.S.A. 92:11776-11780(1995).
[6]
PHOSPHORYLATION AT THR-497; SER-635 AND SER-1179.
DOI=10.1152/ajpheart.00214.2002; PubMed=12384459 [NCBI, ExPASy, EBI, Israel, Japan]
Boo Y.C., Hwang J., Sykes M., Michell B.J., Kemp B.E., Lum H., Jo H.;
"Shear stress stimulates phosphorylation of eNOS at Ser(635) by a protein kinase A-dependent mechanism.";
Am. J. Physiol. 283:H1819-H1828(2002).
[7]
SUBCELLULAR LOCATION.
DOI=10.1152/ajpheart.00990.2006; PubMed=17071725 [NCBI, ExPASy, EBI, Israel, Japan]
Mukhopadhyay S., Xu F., Sehgal P.B.;
"Aberrant cytoplasmic sequestration of eNOS in endothelial cells after monocrotaline, hypoxia, and senescence: live-cell caveolar and cytoplasmic NO imaging.";
Am. J. Physiol. 292:H1373-H1389(2007).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 67-482.
DOI=10.1016/S0092-8674(00)81718-3; PubMed=9875848 [NCBI, ExPASy, EBI, Israel, Japan]
Raman C.S., Li H., Martasek P., Kral V., Masters B.S.S., Poulos T.L.;
"Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.";
Cell 95:939-950(1998).
[9]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 67-482.
DOI=10.1016/S0162-0134(00)00099-4; PubMed=11051558 [NCBI, ExPASy, EBI, Israel, Japan]
Li H., Raman C.S., Martasek P., Kral V., Masters B.S.S., Poulos T.L.;
"Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas.";
J. Inorg. Biochem. 81:133-139(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
DOI=10.1021/bi002658v; PubMed=11331003 [NCBI, ExPASy, EBI, Israel, Japan]
Li H., Raman C.S., Martasek P., Masters B.S.S., Poulos T.L.;
"Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors.";
Biochemistry 40:5399-5406(2001).
[11]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
DOI=10.1021/bi010957u; PubMed=11695891 [NCBI, ExPASy, EBI, Israel, Japan]
Raman C.S., Li H., Martasek P., Southan G., Masters B.S.S., Poulos T.L.;
"Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism.";
Biochemistry 40:13448-13455(2001).
[12]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
DOI=10.1074/jbc.M102255200; PubMed=11331290 [NCBI, ExPASy, EBI, Israel, Japan]
Raman C.S., Li H., Martasek P., Babu B.R., Griffith O.W., Southan G., Masters B.S.S., Poulos T.L.;
"Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase.";
J. Biol. Chem. 276:26486-26491(2001).
[13]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
DOI=10.1074/jbc.M011469200; PubMed=11590164 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Structural basis for pterin antagonism in nitric-oxide synthase. Development of novel 4-oxo-pteridine antagonists of (6R)-5,6,7,8-tetrahydrobiopterin.";
J. Biol. Chem. 276:49133-49141(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M99057; AAA30667.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M89952; AAA30494.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M95674; AAA30669.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38943; A38943.
RefSeq NP_851380.1; -.
UniGene Bt.4662
3D structure databases
PDB
1D0C; X-ray; 1.65 A; A/B=39-482.[ExPASy / RCSB / EBI]
1D0O; X-ray; 1.95 A; A/B=39-482.[ExPASy / RCSB / EBI]
1D1V; X-ray; 1.93 A; A/B=39-482.[ExPASy / RCSB / EBI]
1D1W; X-ray; 2.00 A; A/B=39-482.[ExPASy / RCSB / EBI]
1D1X; X-ray; 2.00 A; A/B=39-482.[ExPASy / RCSB / EBI]
1D1Y; X-ray; 2.20 A; A/B=39-482.[ExPASy / RCSB / EBI]
1DM6; X-ray; 1.95 A; A/B=39-482.[ExPASy / RCSB / EBI]
1DM7; X-ray; 2.10 A; A/B=39-482.[ExPASy / RCSB / EBI]
1DM8; X-ray; 2.25 A; A/B=39-482.[ExPASy / RCSB / EBI]
1DMI; X-ray; 2.00 A; A/B=39-482.[ExPASy / RCSB / EBI]
1DMJ; X-ray; 2.35 A; A/B=39-482.[ExPASy / RCSB / EBI]
1DMK; X-ray; 1.90 A; A/B=39-482.[ExPASy / RCSB / EBI]
1ED4; X-ray; 1.86 A; A/B=39-482.[ExPASy / RCSB / EBI]
1ED5; X-ray; 1.80 A; A/B=39-482.[ExPASy / RCSB / EBI]
1ED6; X-ray; 2.05 A; A/B=39-482.[ExPASy / RCSB / EBI]
1FOI; X-ray; 1.93 A; A/B=39-482.[ExPASy / RCSB / EBI]
1FOJ; X-ray; 2.10 A; A/B=39-482.[ExPASy / RCSB / EBI]
1FOL; X-ray; 2.20 A; A/B=39-482.[ExPASy / RCSB / EBI]
1FOO; X-ray; 2.00 A; A/B=39-482.[ExPASy / RCSB / EBI]
1FOP; X-ray; 2.30 A; A/B=39-482.[ExPASy / RCSB / EBI]
1I83; X-ray; 2.00 A; A/B=39-482.[ExPASy / RCSB / EBI]
1NSE; X-ray; 1.90 A; A/B=39-482.[ExPASy / RCSB / EBI]
1P6L; X-ray; 2.35 A; A/B=67-483.[ExPASy / RCSB / EBI]
1P6M; X-ray; 2.27 A; A/B=67-483.[ExPASy / RCSB / EBI]
1P6N; X-ray; 2.50 A; A/B=67-483.[ExPASy / RCSB / EBI]
1Q2O; X-ray; 1.74 A; A/B=67-482.[ExPASy / RCSB / EBI]
1RS8; X-ray; 2.30 A; A/B=67-482.[ExPASy / RCSB / EBI]
1RS9; X-ray; 2.22 A; A/B=67-482.[ExPASy / RCSB / EBI]
1ZZS; X-ray; 1.85 A; A/B=67-482.[ExPASy / RCSB / EBI]
1ZZT; X-ray; 2.14 A; A/B=67-482.[ExPASy / RCSB / EBI]
2G6O; X-ray; 1.90 A; A/B=67-482.[ExPASy / RCSB / EBI]
2HX2; X-ray; 1.95 A; A/B=67-482.[ExPASy / RCSB / EBI]
2NSE; X-ray; 2.34 A; A/B=39-482.[ExPASy / RCSB / EBI]
3NSE; X-ray; 2.10 A; A/B=39-482.[ExPASy / RCSB / EBI]
4NSE; X-ray; 1.95 A; A/B=39-482.[ExPASy / RCSB / EBI]
5NSE; X-ray; 1.90 A; A/B=39-482.[ExPASy / RCSB / EBI]
6NSE; X-ray; 2.35 A; A/B=39-482.[ExPASy / RCSB / EBI]
7NSE; X-ray; 2.35 A; A/B=39-482.[ExPASy / RCSB / EBI]
8NSE; X-ray; 2.25 A; A/B=39-482.[ExPASy / RCSB / EBI]
9NSE; X-ray; 2.24 A; A/B=39-482.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1D0C; -.
1D0O; -.
1D1V; -.
1D1W; -.
1D1X; -.
1D1Y; -.
1DM6; -.
1DM7; -.
1DM8; -.
1DMI; -.
1DMJ; -.
1DMK; -.
1ED4; -.
1ED5; -.
1ED6; -.
1FOI; -.
1FOJ; -.
1FOL; -.
1FOO; -.
1FOP; -.
1I83; -.
1NSE; -.
1P6L; -.
1P6M; -.
1P6N; -.
1Q2O; -.
1RS8; -.
1RS9; -.
1ZZS; -.
1ZZT; -.
2G6O; -.
2HX2; -.
2NSE; -.
3NSE; -.
4NSE; -.
5NSE; -.
6NSE; -.
7NSE; -.
8NSE; -.
9NSE; -.
ModBase P29473.
Ontologies
GO
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from UniProtKB).
GO:0004517; Molecular function: nitric-oxide synthase activity (inferred from direct assay from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0006527; Biological process: arginine catabolic process (inferred from direct assay from UniProtKB).
GO:0007005; Biological process: mitochondrion organization (inferred from mutant phenotype from UniProtKB).
GO:0006809; Biological process: nitric oxide biosynthetic process (inferred from direct assay from UniProtKB).
GO:0031284; Biological process: positive regulation of guanylate cyclase activity (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003097; FAD-binding_1.
IPR008254; Flavodoxin/NO_synth.
IPR004030; NO_synthase_oxygenase_reg.
IPR012144; NOS.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.
Pfam PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000333; NOS; 1.
PROSITE PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P29473.
Genome annotation databases
Ensembl ENSBTAG00000017680; Bos taurus. [Contig view]
GeneID 287024; -.
KEGG bta:287024; -.
Phylogenomic databases
HOVERGEN P29473; -.
Other
LinkHub P29473; -.
ProtoNet P29473.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Blood coagulation; Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; FAD; FMN; Golgi apparatus; Heme; Iron; Lipoprotein; Membrane; Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed. 
CHAIN   2   1205  1204     Nitric oxide synthase, endothelial. PRO_0000170941
DOMAIN   522    705  184     Flavodoxin-like. 
DOMAIN   758   1004  247     FAD-binding FR-type. 
NP_BIND   651    682  32     FMN (By similarity). 
NP_BIND   795    806  12     FAD (By similarity). 
NP_BIND   937    947  11     FAD (By similarity). 
NP_BIND   1012   1030  19     NADP (By similarity). 
NP_BIND   1110   1125  16     NADP (By similarity). 
REGION   100    488  389     Interaction with NOSIP (By similarity). 
REGION   492    512  21     Calmodulin-binding (Potential). 
METAL   96     96        Zinc. 
METAL   101    101        Zinc. 
METAL   186    186        Iron (heme axial ligand). 
MOD_RES   83     83        Phosphotyrosine (By similarity). 
MOD_RES   143    143        Phosphoserine; by PKA. 
MOD_RES   497    497        Phosphothreonine; by PKA. 
MOD_RES   635    635        Phosphoserine. 
MOD_RES   1177   1177        Phosphothreonine (By similarity). 
MOD_RES   1179   1179        Phosphoserine; by PDPK1 and PKA. 
LIPID   2      2        N-myristoyl glycine. 
LIPID   15     15        S-palmitoyl cysteine. 
LIPID   26     26        S-palmitoyl cysteine. 
CONFLICT   100    100        C -> R (in Ref. 3; AAA30669). 
CONFLICT   165    165        Y -> I (in Ref. 3; AAA30669). 
CONFLICT   318    328        EHPTLEWFAAL -> GAPHTGVVRGP (in Ref. 3; AAA30669). 
CONFLICT   455    455        S -> Y (in Ref. 3; AAA30669). 
CONFLICT   459    459        T -> P (in Ref. 3; AAA30669). 
CONFLICT   741    741        T -> A (in Ref. 3; AAA30669). 
CONFLICT   804    805        CP -> SA (in Ref. 3; AAA30669). 
CONFLICT   857    857        L -> V (in Ref. 3; AAA30669). 
CONFLICT   907    908        WF -> LV (in Ref. 3; AAA30669). 
CONFLICT   1042   1042        A -> H (in Ref. 3; AAA30669). 
STRAND   72     75  4      
TURN   76     79  4      
STRAND   80     83  4      
HELIX   86     89  4      
TURN   109    111  3      
HELIX   122    139  18      
HELIX   146    162  17      
HELIX   169    181  13      
HELIX   189    191  3      
STRAND   196    199  4      
HELIX   206    221  16      
HELIX   222    224  3      
STRAND   229    232  4      
STRAND   247    251  5      
STRAND   255    257  3      
STRAND   263    265  3      
HELIX   267    269  3      
HELIX   270    278  9      
STRAND   286    288  3      
STRAND   293    296  4      
STRAND   303    305  3      
HELIX   309    311  3      
STRAND   314    316  3      
HELIX   323    328  6      
STRAND   331    334  4      
STRAND   342    345  4      
STRAND   348    351  4      
HELIX   361    365  5      
HELIX   367    370  4      
TURN   372    375  4      
HELIX   378    384  7      
HELIX   392    394  3      
HELIX   396    414  19      
HELIX   422    440  19      
HELIX   447    450  4      
STRAND   453    455  3      
HELIX   456    458  3      
HELIX   460    463  4      
STRAND   472    476  5      
Sequence information
Length: 1205 AA [This is the length of the unprocessed precursor] Molecular weight: 133287 Da [This is the MW of the unprocessed precursor] CRC64: 5DC8FF4F25870281 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSR APAPATPHAP DHSPAPNSPT 

        70         80         90        100        110        120 
LTRPPEGPKF PRVKNWELGS ITYDTLCAQS QQDGPCTPRC CLGSLVLPRK LQTRPSPGPP 

       130        140        150        160        170        180 
PAEQLLSQAR DFINQYYSSI KRSGSQAHEE RLQEVEAEVA STGTYHLRES ELVFGAKQAW 

       190        200        210        220        230        240 
RNAPRCVGRI QWGKLQVFDA RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRAPGR 

       250        260        270        280        290        300 
GDFRIWNSQL VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE 

       310        320        330        340        350        360 
APELFVLPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF SAAPFSGWYM 

       370        380        390        400        410        420 
STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA AVEINLAVLH SFQLAKVTIV 

       430        440        450        460        470        480 
DHHAATVSFM KHLDNEQKAR GGCPADWAWI VPPISGSLTP VFHQEMVNYI LSPAFRYQPD 

       490        500        510        520        530        540 
PWKGSATKGA GITRKKTFKE VANAVKISAS LMGTLMAKRV KATILYASET GRAQSYAQQL 

       550        560        570        580        590        600 
GRLFRKAFDP RVLCMDEYDV VSLEHEALVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN 

       610        620        630        640        650        660 
SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC VFGLGSRAYP 

       670        680        690        700        710        720 
HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW AKAAFQASCE TFCVGEEAKA 

       730        740        750        760        770        780 
AAQDIFSPKR SWKRQRYRLS TQAEGLQLLP GLIHVHRRKM FQATVLSVEN LQSSKSTRAT 

       790        800        810        820        830        840 
ILVRLDTAGQ EGLQYQPGDH IGICPPNRPG LVEALLSRVE DPPPPTESVA VEQLEKGSPG 

       850        860        870        880        890        900 
GPPPSWVRDP RLPPCTLRQA LTFFLDITSP PSPRLLRLLS TLAEEPSEQQ ELETLSQDPR 

       910        920        930        940        950        960 
RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPNA HPGEVHLTVA 

       970        980        990       1000       1010       1020 
VLAYRTQDGL GPLHYGVCST WLSQLKTGDP VPCFIRGAPS FRLPPDPYVP CILVGPGTGI 

      1030       1040       1050       1060       1070       1080 
APFRGFWQER LHDIESKGLQ PAPMTLVFGC RCSQLDHLYR DEVQDAQERG VFGRVLTAFS 

      1090       1100       1110       1120       1130       1140 
REPDSPKTYV QDILRTELAA EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME 

      1150       1160       1170       1180       1190       1200 
LDEAGDVIGV LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWAFDPPGP 


DTPGP 

P29473 in FASTA format

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