ID NOS3_MOUSE STANDARD; PRT; 1201 AA. AC P70313; O55056; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE NITRIC-OXIDE SYNTHASE, ENDOTHELIAL (EC 1.14.13.39) (EC-NOS) (NOS, TYPE DE III) (NOSIII) (ENDOTHELIAL NOS) (ENOS) (CONSTITUTIVE NOS) (CNOS). GN NOS3 OR ECNOS. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=FETAL HEART; RX MEDLINE=96350460; PubMed=8764825; RA Gnanapandithen K., Chen Z., Kau C.-L., Gorczynski R.M., Marsden P.A.; RT "Cloning and characterization of murine endothelial constitutive RT nitric oxide synthase."; RL Biochim. Biophys. Acta 1308:103-106(1996). RN [2] RP SEQUENCE OF 1-53 FROM N.A. RC TISSUE=FETAL HEART; RA Gregg A.R., Schauer A., Shi O., Liu Z., Lee C.L., O'Brien W.E.; RT "Limb reduction defects in endothelial nitric oxide synthase deficient RT mice."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION. RX MEDLINE=99061722; PubMed=9843834; RA Gregg A.R., Schauer A., Shi O., Liu Z., Lee C.G.L., O'Brien W.E.; RT "Limb reduction defects in endothelial nitric oxide synthase-deficient RT mice."; RL Am. J. Physiol. 275:H2319-H2324(1998). CC -!- FUNCTION: PRODUCES NITRIC OXIDE (NO) WHICH IS IMPLICATED IN CC VASCULAR SMOOTH MUSCLE RELAXATION THROUGH A CGMP-MEDIATED SIGNAL CC TRANSDUCTION PATHWAY. NO MEDIATES VASCULAR ENDOTHELIAL GROWTH CC FACTOR (VEGF)-INDUCED ANGIOGENESIS IN CORONARY VESSELS AND CC PROMOTES BLOOD CLOTTING THROUGH THE ACTIVATION OF PLATELETS. MAY CC PLAY A SIGNIFICANT ROLE IN NORMAL AND ABNORMAL LIMB DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: L-ARGININE + N NADPH + M O(2) = CITRULLINE + CC NITRIC OXIDE + N NADP(+). CC -!- COFACTOR: HEME. BINDS ONE MOLE EACH OF FAD AND FMN. ALSO REQUIRES CC TETRAHYDROBIOPTERIN (BH4) WHICH MAY STABILIZE THE DIMERIC FORM OF CC THE ENZYME. CC -!- ENZYME REGULATION: STIMULATED BY CALCIUM/CALMODULIN (BY CC SIMILARITY). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE NOS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U53142; AAC52766.1; -. DR EMBL; AF045940; AAC02553.1; -. DR HSSP; P29477; 2NOS. DR MGD; MGI:97362; Nos3. DR INTERPRO; IPR001094; -. DR INTERPRO; IPR001433; -. DR INTERPRO; IPR001709; -. DR INTERPRO; IPR003097; -. DR PFAM; PF00175; oxidored_fad; 1. DR PFAM; PF00667; FAD_binding; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. KW Oxidoreductase; NADP; FAD; FMN; Calmodulin-binding; Myristate; KW Lipoprotein; Palmitate; Calcium-binding; Heme; Zinc; Metal-binding; KW Multigene family. FT INIT_MET 0 0 BY SIMILARITY. FT BINDING 182 182 HEME (BY SIMILARITY). FT DOMAIN 489 508 CALMODULIN-BINDING (POTENTIAL). FT NP_BIND 647 678 FMN (PYRIMIDINE PART) (BY SIMILARITY). FT NP_BIND 791 802 FAD (ADP PART) (BY SIMILARITY). FT NP_BIND 933 943 FAD (FLAVIN PART) (BY SIMILARITY). FT NP_BIND 1008 1026 NADP (RIBOSE PART) (BY SIMILARITY). FT NP_BIND 1106 1121 NADP (ADP PART) (BY SIMILARITY). FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT LIPID 14 14 PALMITATE (BY SIMILARITY). FT LIPID 25 25 PALMITATE (BY SIMILARITY). FT METAL 92 92 ZINC (BY SIMILARITY). FT METAL 97 97 ZINC (BY SIMILARITY). FT CONFLICT 49 49 A -> P (IN REF. 2). SQ SEQUENCE 1201 AA; 132748 MW; DA37ABAC947DABD5 CRC64; GNLKSVGQEP GPPCGLGLGL GLGLCGKQGP ASPAPEPSQA PAPPSPTRAA PDHSPPLTRP PDGPRFPRVK NWEVGSITYD TLSAQAQQDG PCTSRRCLGS LVFPRKLQSR PTQGPSPTEQ LLGQARDFIN QYYNSIKRSG SQAHEQRLQE VEAEVAATGT YQLRESELVF GAKQAWRNAP RCVGRIQWGK LQVFDARDCR TAQEMFTYIC NHIKYATNRG NLRSAITVFP QRCPGRGDFR IWNSQLIRYA GYRQQDGSVR GDPANVEITE LCIQHGWTPG NGRFDVLPLL LQAPDESPEL FTLPPEMVLE VPLEHPTLEW FAALGLRWYA LPAVSNMLLE IGGLEFPAAP FSGWYMSSEI GMRDLCDPHR YNILEDVAVC MDLDTRTTSS LWKDKAAVEI NVAVLHSYQL AKVTIVDHHA ATASFMKHLE NEQKARGGCP ADWAWIVPPI SGSLTPVFHQ EMVNYFLSPA FRYQPDPWKG SAAKGAGITR KKTFKEVANA VKISASLMGT VMAKRVKATI LYGSETGRAQ SYAQQLGRLF RKAFDPRVLC MDEYDVVSLE HEALVLVVTS TFGNGDPPEN GESFAAALME MSGPYNSSPR PEQHKSYKIR FNSVSCSDPL VSSWRRKRKE SSNTDSAGAL GTLRFCVFGL GSRAYPHFCA FARAVDTRLE ELGGERLLQL GQGDELCGQE EAFRGWAQAA FQAACETFCV GEDAKAAARD IFSPKRSWKR QRYRLSTQAE SLQLLPGLTH VHRRKMFQAT ILSVENLQSS KSTRATILVR LDTGGQEGLQ YQPGDHIGVC PPNRPGLVEA LLSRVEDPPP STEPVAVEQL EKGSPGGPPP GWVRDPRLPP CTLRQALTYF LDITSPPSPR LLRLLSTLAE ESSEQQELEA LSQDPRRYEE WKWFSCPTLL EVLEQFPSVA LPAPLILTQL PLLQPRYYSV SSAPSAHPGE IHLTIAVLAY RTQDGLGPLH YGVCSTWMSQ LKAGDPVPCF IRGAPSFRLP PDPNLPCILV GPGTGIAPFR GFWQDRLHDI EIKGLQPAPM TLVFGCRCSQ LDHLYRDEVL DAQQRGVFGQ VLTAFSRDPG SPKTYVQDLL RTELAAEVHR VLCLEQGHMF VCGDVTMATS VLQTVQRILA TEGGMELDEA GDVIGVLRDQ QRYHEDIFGL TLRTQEVTSR IRTQSFSLQE RQLRGAVPWS FDPPGPEIPG S //