ID F1LQC7_RAT Unreviewed; 1202 AA. AC F1LQC7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 16-MAY-2012, entry version 13. DE RecName: Full=Nitric oxide synthase; DE EC=1.14.13.39; GN Name=Nos3; 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; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; 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] RP IDENTIFICATION. RC STRAIN=Brown Norway; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Produces nitric oxide (NO) (By similarity). CC -!- CATALYTIC ACTIVITY: L-arginine + n NADPH + n H(+) + m O(2) = CC citrulline + nitric oxide + n NADP(+). CC -!- COFACTOR: Binds 1 FAD (By similarity). CC -!- COFACTOR: Binds 1 FMN (By similarity). CC -!- COFACTOR: Heme group (By similarity). CC -!- SIMILARITY: Belongs to the NOS family. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. 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 IPI; IPI01016537; -. DR Ensembl; ENSRNOT00000013058; ENSRNOP00000013058; ENSRNOG00000009348. DR RGD; 3186; Nos3. DR GeneTree; ENSGT00620000087711; -. DR OMA; GPLHYGV; -. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. 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:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:EC. DR Gene3D; G3DSA:1.20.990.10; NADPH_Cyt_P450_Rdtase_dom3; 1. DR Gene3D; G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 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; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR012144; Nitric-oxide_synthase. DR InterPro; IPR004030; NO_synthase_oxygenase_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF5; PTHR19384:SF5; 1. 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; SSF56512; NO_synthase_oxygenase_reg; 1. DR SUPFAM; SSF63380; Riboflavin_synthase_like_b-brl; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. PE 3: Inferred from homology; KW Calmodulin-binding; Complete proteome; FAD; FMN; Heme; Iron; KW Metal-binding; NADP; Oxidoreductase; Reference proteome. 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 //