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UniProtKB/Swiss-Prot entry Q27571


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

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Entry information
Entry name NOS_DROME
Primary accession number Q27571
Secondary accession numbers A4V0K9 A4V0L0 Q4ABG3 Q4ABG4 Q4ABG5 Q4ABG6 Q4ABG7 Q7YU33 Q9U096 Q9VKP8
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on June 10, 2008 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 84)
Name and origin of the protein
Protein name Nitric oxide synthase
Synonyms EC 1.14.13.39
dNOS
Gene name
Name: Nos
ORFNames: CG6713
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND ENZYME REGULATION.
TISSUE=Head;
PubMed=7568075 [NCBI, ExPASy, EBI, Israel, Japan]
Regulski M., Tully T.;
"Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase.";
Proc. Natl. Acad. Sci. U.S.A. 92:9072-9076(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
TISSUE=Embryo, and Larva;
DOI=10.1074/jbc.M105066200; PubMed=11526108 [NCBI, ExPASy, EBI, Israel, Japan]
Stasiv Y., Regulski M., Kuzin B., Tully T., Enikolopov G.;
"The Drosophila nitric-oxide synthase gene (dNOS) encodes a family of proteins that can modulate NOS activity by acting as dominant negative regulators.";
J. Biol. Chem. 276:42241-42251(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Berkeley;
TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION.
DOI=10.1016/S0006-291X(03)01003-9; PubMed=12804606 [NCBI, ExPASy, EBI, Israel, Japan]
Sengupta R., Sahoo R., Mukherjee S., Regulski M., Tully T., Stuehr D.J., Ghosh S.;
"Characterization of Drosophila nitric oxide synthase: a biochemical study.";
Biochem. Biophys. Res. Commun. 306:590-597(2003).
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
U25117; AAC46882.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215700; AAF25682.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215691; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215692; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215693; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215694; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215695; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215696; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215697; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215698; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF215699; AAF25682.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAF53014.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66450.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66452.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66453.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66454.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66455.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66456.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAZ66457.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT010016; AAQ22485.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T13254; T13254.
RefSeq NP_001027238.1; -.
NP_001027239.1; -.
NP_001027240.1; -.
NP_001027241.1; -.
NP_001027243.1; -.
NP_001027244.1; -.
NP_001027245.1; -.
NP_001027246.1; -.
NP_523541.2; -.
UniGene Dm.2707
3D structure databases
PDB
2I86; Model; -; @=217-629.[ExPASy / RCSB / EBI]
PDBsum 2I86; -.
ModBase Q27571.
Protein-protein interaction databases
IntAct Q27571; -.
Organism-specific databases
FlyBase FBgn0011676; Nos.
Gene expression databases
ArrayExpress Q27571; -.
GermOnline CG6713; Drosophila melanogaster.
Ontologies
GO
GO:0005516; Molecular function: calmodulin binding (non-traceable author statement from FlyBase).
GO:0020037; Molecular function: heme binding (non-traceable author statement from FlyBase).
GO:0004517; Molecular function: nitric-oxide synthase activity (traceable author statement from UniProtKB).
GO:0007444; Biological process: imaginal disc development (traceable author statement from FlyBase).
GO:0008285; Biological process: negative regulation of cell proliferation (traceable author statement from FlyBase).
GO:0008156; Biological process: negative regulation of DNA replication (traceable author statement from FlyBase).
GO:0006809; Biological process: nitric oxide biosynthetic process (traceable author statement from UniProtKB).
GO:0046620; Biological process: regulation of organ growth (traceable author statement from FlyBase).
GO:0007416; Biological process: synaptogenesis (traceable author statement from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
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.
PRINTS PR00369; FLAVODOXIN.
PR00371; FPNCR.
PROSITE PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q27571.
Genome annotation databases
Ensembl CG6713; Drosophila melanogaster. [Contig view]
GeneID 34495; -.
KEGG dme:Dmel_CG6713; -.
Other
ProtoNet Q27571.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Calmodulin-binding; Complete proteome; FAD; FMN; Heme; Iron; Metal-binding; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1349  1349     Nitric oxide synthase. PRO_0000170951
DOMAIN   671    868  198     Flavodoxin-like. 
DOMAIN   928   1167  240     FAD-binding FR-type. 
NP_BIND   814    845  32     FMN (By similarity). 
NP_BIND   957    968  12     FAD (By similarity). 
NP_BIND   1100   1110  11     FAD (By similarity). 
NP_BIND   1175   1193  19     NADP (By similarity). 
NP_BIND   1273   1287  15     NADP (By similarity). 
REGION   641    661  21     Calmodulin-binding (Potential). 
COMPBIAS   24     51  28     Gln-rich. 
COMPBIAS   76     79  4     Poly-Gly. 
COMPBIAS   145    156  12     Poly-Gly. 
METAL   328    328        Iron (heme axial ligand) (By similarity). 
VAR_SEQ   201    214        FMHLDDEGRSLLMR -> RFFPARRPPVRAAL (in isoform 3). VSP_003585
VAR_SEQ   215   1349        Missing (in isoform 3). VSP_003586
VAR_SEQ   417    521        Missing (in isoform 2). VSP_003587
VAR_SEQ   701    746        IYCMSDYDISSIEHEALLIVVASTFGNGDPPENGELFSQE LYAMRV -> CPVGSVSSDPQDPVQLGLVVVLVSSTCVCKKHLPAAWQNK ISCKHL (in isoform 6). VSP_003590
VAR_SEQ   701    704        IYCM -> VSLT (in isoform 5). VSP_003588
VAR_SEQ   705   1349        Missing (in isoform 5). VSP_003589
VAR_SEQ   736    756        LFSQELYAMRVQESSEHGLQD -> VSTPPRKDHTELINGLGPAAF (in isoform 4). VSP_003592
VAR_SEQ   747   1349        Missing (in isoform 6). VSP_003591
VAR_SEQ   757   1349        Missing (in isoform 4). VSP_003593
VAR_SEQ   758   1291        Missing (in isoform 10). VSP_003594
CONFLICT   20     20        S -> A (in Ref. 1; AAC46882). 
CONFLICT   24     24        Q -> QQ (in Ref. 1; AAC46882). 
CONFLICT   105    105        S -> L (in Ref. 1; AAC46882). 
CONFLICT   287    287        S -> C (in Ref. 1; AAC46882). 
CONFLICT   373    373        T -> S (in Ref. 2; AAF25682). 
CONFLICT   1197   1197        S -> R (in Ref. 1; AAC46882 and 2; AAF25682). 
Sequence information
Length: 1349 AA [This is the length of the unprocessed precursor] Molecular weight: 151715 Da [This is the MW of the unprocessed precursor] CRC64: E19D8CBAEFAF76FC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQHFTSIFE NLRFVTIKRS TNAQQQQQQQ QQQLQQQQQQ LQQQKAQTQQ QNSRKIKTQA 

        70         80         90        100        110        120 
TPTLNGNGLL SGNPNGGGGD SSPSHEVDHP GGAQGAQAAG GLPSSSGTPL RHHKRASIST 

       130        140        150        160        170        180 
ASPPIRERRG TNTSIVVELD GSGSGSGSGG GGVGVGQGAG CPPSGSCTAS GKSSRELSPS 

       190        200        210        220        230        240 
PKNQQQPRKM SQDYRSRAGS FMHLDDEGRS LLMRKPMRLK NIEGRPEVYD TLHCKGREIL 

       250        260        270        280        290        300 
SCSKATCTSS IMNIGNAAVE ARKSDLILEH AKDFLEQYFT SIKRTSSTAH ETRWKQVRQS 

       310        320        330        340        350        360 
IETTGHYQLT ETELIYGAKL AWRNSSRCIG RIQWSKLQVF DCRYVTTTSG MFEAICNHIK 

       370        380        390        400        410        420 
YATNKGNLRS AITIFPQRTD AKHDYRIWNN QLISYAGYKQ ADGKIIGDPM NVEFTEVCTK 

       430        440        450        460        470        480 
LGWKSKGSEW DILPLVVSAN GHDPDYFDYP PELILEVPLT HPKFEWFSDL GLRWYALPAV 

       490        500        510        520        530        540 
SSMLFDVGGI QFTATTFSGW YMSTEIGSRN LCDTNRRNML ETVALKMQLD TRTPTSLWKD 

       550        560        570        580        590        600 
KAVVEMNIAV LHSYQSRNVT IVDHHTASES FMKHFENESK LRNGCPADWI WIVPPLSGSI 

       610        620        630        640        650        660 
TPVFHQEMAL YYLKPSFEYQ DPAWRTHVWK KGRGESKGKK PRRKFNFKQI ARAVKFTSKL 

       670        680        690        700        710        720 
FGRALSKRIK ATVLYATETG KSEQYAKQLC ELLGHAFNAQ IYCMSDYDIS SIEHEALLIV 

       730        740        750        760        770        780 
VASTFGNGDP PENGELFSQE LYAMRVQESS EHGLQDSSIG SSKSFMKASS RQEFMKLPLQ 

       790        800        810        820        830        840 
QVKRIDRWDS LRGSTSDTFT EETFGPLSNV RFAVFALGSS AYPNFCAFGQ YVDNILGELG 

       850        860        870        880        890        900 
GERLLRVAYG DEMCGQEQSF RKWAPEVFKL ACETFCLDPE ESLSDASLAL QNDSLTVNTV 

       910        920        930        940        950        960 
RLVPSANKGS LDSSLSKYHN KKVHCCKAKA KPHNLTRLSE GAKTTMLLEI CAPGLEYEPG 

       970        980        990       1000       1010       1020 
DHVGIFPANR TELVDGLLNR LVGVDNPDEV LQLQLLKEKQ TSNGIFKCWE PHDKIPPDTL 

      1030       1040       1050       1060       1070       1080 
RNLLARFFDL TTPPSRQLLT LLAGFCEDTA DKERLELLVN DSSAYEDWRH WRLPHLLDVL 

      1090       1100       1110       1120       1130       1140 
EEFPSCRPPA PLLLAQLTPL QPRFYSISSS PRRVSDEIHL TVAIVKYRCE DGQGDERYGV 

      1150       1160       1170       1180       1190       1200 
CSNYLSGLRA DDELFMFVRS ALGFHLPSDR SRPIILIGPG TGIAPFRSFW QEFQVLSDLD 

      1210       1220       1230       1240       1250       1260 
PTAKLPKMWL FFGCRNRDVD LYAEEKAELQ KDQILDRVFL ALSREQAIPK TYVQDLIEQE 

      1270       1280       1290       1300       1310       1320 
FDSLYQLIVQ ERGHIYVCGD VTMAEHVYQT IRKCIAGKEQ KSEAEVETFL LTLRDESRYH 

      1330       1340 
EDIFGITLRT AEIHTKSRAT ARIRMASQP 

Q27571 in FASTA format

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