ID F1LQC7_RAT Unreviewed; 1202 AA. AC F1LQC7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 22-JUL-2015, entry version 36. DE RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333}; DE EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333}; GN Name=Nos3 {ECO:0000313|Ensembl:ENSRNOP00000013058, GN ECO:0000313|RGD:3186}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000013058, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000013058, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000013058, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000013058} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000013058}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000213|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Produces nitric oxide (NO). CC {ECO:0000256|PIRNR:PIRNR000333}. CC -!- CATALYTIC ACTIVITY: 2 L-arginine + 3 NADPH + 4 O(2) = 2 L- CC citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O. CC {ECO:0000256|PIRNR:PIRNR000333}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRNR:PIRNR000333}; CC Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|PIRNR:PIRNR000333}; CC Note=Binds 1 FMN. {ECO:0000256|PIRNR:PIRNR000333}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRNR:PIRNR000333}; CC -!- SIMILARITY: Belongs to the NOS family. CC {ECO:0000256|PIRNR:PIRNR000333}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSRNOP00000013058}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC097312; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 10116.ENSRNOP00000013058; -. DR Ensembl; ENSRNOT00000013058; ENSRNOP00000013058; ENSRNOG00000009348. DR RGD; 3186; Nos3. DR GeneTree; ENSGT00620000087711; -. DR OMA; WGKLQVF; -. DR OrthoDB; EOG79SDW7; -. DR TreeFam; TF324410; -. DR Reactome; REACT_280475; VEGFR2 mediated vascular permeability. DR Reactome; REACT_300515; Phagosomal maturation (early endosomal stage). DR Reactome; REACT_305912; eNOS activation. DR Reactome; REACT_310165; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation. DR Reactome; REACT_323377; Nitric oxide stimulates guanylate cyclase. DR Reactome; REACT_344407; NOSTRIN mediated eNOS trafficking. DR Reactome; REACT_347663; NOSIP mediated eNOS trafficking. DR NextBio; 35576401; -. DR PRO; PR:F1LQC7; -. DR Proteomes; UP000002494; Chromosome 4. DR ExpressionAtlas; F1LQC7; baseline and differential. DR GO; GO:0005901; C:caveola; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0034618; F:arginine binding; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:UniProtKB-EC. DR GO; GO:0034617; F:tetrahydrobiopterin binding; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0006527; P:arginine catabolic process; IEA:Ensembl. DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl. DR GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0051346; P:negative regulation of hydrolase activity; IEA:Ensembl. DR GO; GO:0014740; P:negative regulation of muscle hyperplasia; IEA:Ensembl. DR GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro. DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0050880; P:regulation of blood vessel size; IEA:Ensembl. DR GO; GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl. DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; IEA:Ensembl. DR GO; GO:0003057; P:regulation of the force of heart contraction by chemical signal; IEA:Ensembl. DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl. DR GO; GO:0014806; P:smooth muscle hyperplasia; IEA:Ensembl. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.40.50.360; -; 2. DR Gene3D; 3.90.340.10; -; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR012144; NOS_euk. DR InterPro; IPR004030; NOS_N. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF02898; NO_synthase; 1. DR PIRSF; PIRSF000333; NOS; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52218; SSF52218; 1. DR SUPFAM; SSF56512; SSF56512; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. PE 1: Evidence at protein level; KW Calmodulin-binding {ECO:0000256|PIRNR:PIRNR000333}; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW FAD {ECO:0000256|PIRNR:PIRNR000333}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000333}; KW FMN {ECO:0000256|PIRNR:PIRNR000333}; KW Heme {ECO:0000256|PIRNR:PIRNR000333, ECO:0000256|SAAS:SAAS00278616}; KW Iron {ECO:0000256|PIRNR:PIRNR000333}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000333}; KW NADP {ECO:0000256|PIRNR:PIRNR000333}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000333}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1LQC7}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}. SQ SEQUENCE 1202 AA; 133191 MW; E5B7CA955C906680 CRC64; MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSQ APVPPSPTRP APDHSPPLTR PPDGPKFPRV KNWEVGSITY DTLSAQAQQD GPCTPRRCLG SLVFPRKLQS RPTQGPSPTE QLLGQARDFI NQYYNSIKRS GSQAHEQRLQ EVEAEVVATG TYQLRESELV FGAKQAWRNA PRCVGRIQWG KLQVFDARDC RTAQEMFTYI CNHIKYATNR GNLRSAITVF PQRYAGRGDF RIWNSQLVRY AGYRQQDGSV RGDPANVEIT ELCIQHGWTP GNGRFDVLPL LLQAPDEPPE LFTLPPELVL EVPLEHPTLE WFAALGLRWY ALPAVSNMLL EIGGLEFPAA PFSGWYMSSE IGMRDLCDPH RYNILEDVAV CMDLDTRTTS SLWKDKAAVE INVAVLYSYQ LAKVTIVDHH AATASFMKHL ENEQKARGGC PADWAWIVPP ISGSLTPVFH QEMVNYFLSP AFRYQPDPWK GSAAKGTGIT RKKTFKEVAN AVKISASLMG TVMAKRVKAT ILYGSETGRA QSYAQQLGRL FRKAFDPRVL CMDEYDVVSL EHEALVLVVT STFGNGDPPE NGESFAAALM EMSGPYNSSP RPEQHKSYKI RFNSVSCSDP LVSSWRRKRK ESSNTDSAGA LGTLRFCVFG LGSRAYPHFC AFARAVDTRL EELGGERLLQ LGQGDELCGQ EEAFRGWAQA AFQAACETFC VGEDAKAAAR DIFSPKRSWK RQRYRLSTQA ESLQLLPGLT HVHRRKMFQA TILSVENLQS SKSTRATILV RLDTGSQEGL QYQPGDHIGV CPPNRPGLVE ALLSRVEDPP PSTEPVAVEQ LEKGSPGGPP PGWVRDPRLP PCTLRQALTY FLDITSPPSP RLLRLLSTLA EESSEQQELE ALSQDPRRYE EWKWFRCPTL LEVLEQFPSV ALPAPLILTQ LPLLQPRYYS VSSAPSAHPG EIHLTVAVLA YRTQDGLGPL HYGVCSTWMS QLKAGDPVPC FIRGAPSFRL PPDPNLPCIL VGPGTGIAPF RGFWQDRLHD IEIKGLQPAP MTLVFGCRCS QLDHLYRDEV LDAQQRGVFG QVLTAFSRDP GSPKTYVQDL LRTELAAEVH RVLCLEQGHM FVCGDVTMAT SVLQTVQRIL ATEGSMELDE AGDVIGVLRD QQRYHEDIFG LTLRTQEVTS RIRTQSFSLQ ERQLRGAVPW SFDPPTQETP GS //