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Reviewed, UniProtKB/Swiss-Prot Q27571 (NOS_DROME)

Last modified June 16, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nitric oxide synthase
    EC=1.14.13.39
Alternative name(s):
    dNOS
Gene names
Name: Nos
ORF Names: CG6713
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. Truncated isoforms (isoform 3-isoform 6) are able to form intracellular complexes with the full length protein and serve as dominant negative inhibitors of the enzyme activity. Ref.1 Ref.2 Ref.6

Catalytic activity

L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+.

Cofactor

Heme group By similarity.

Binds 1 FAD By similarity.

Binds 1 FMN By similarity.

Enzyme regulation

Stimulated by calcium/calmodulin. Ref.1

Developmental stage

Isoform 3 is expressed in larvae only. Isoform 4, isoform 5, isoform 6 and isoform 10 are expressed throughout development from embryos to adults. Ref.2

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Spf45Q7PL831EBI-250663,EBI-163247

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q27571-1)

Also known as: A; C; dNOS-1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q27571-2)

Also known as: dNOS-2; E;

The sequence of this isoform differs from the canonical sequence as follows:
     417-521: Missing.
Isoform 3 (identifier: Q27571-3)

Also known as: dNOS-3;

The sequence of this isoform differs from the canonical sequence as follows:
     201-214: FMHLDDEGRSLLMR → RFFPARRPPVRAAL
     215-1349: Missing.
Isoform 4 (identifier: Q27571-4)

Also known as: B; dNOS-4; F; J;

The sequence of this isoform differs from the canonical sequence as follows:
     736-756: LFSQELYAMRVQESSEHGLQD → VSTPPRKDHTELINGLGPAAF
     757-1349: Missing.
Isoform 5 (identifier: Q27571-5)

Also known as: dNOS-5; H;

The sequence of this isoform differs from the canonical sequence as follows:
     701-704: IYCM → VSLT
     705-1349: Missing.
Isoform 6 (identifier: Q27571-6)

Also known as: dNOS-6; I;

The sequence of this isoform differs from the canonical sequence as follows:
     701-746: IYCMSDYDIS...FSQELYAMRV → CPVGSVSSDP...WQNKISCKHL
     747-1349: Missing.
Isoform 10 (identifier: Q27571-7)

Also known as: dNOS-10; G;

The sequence of this isoform differs from the canonical sequence as follows:
     758-1291: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13491349Nitric oxide synthase
PRO_0000170951

Regions

Domain671 – 868198Flavodoxin-like
Domain928 – 1167240FAD-binding FR-type
Nucleotide binding814 – 84532FMN By similarity
Nucleotide binding957 – 96812FAD By similarity
Nucleotide binding1100 – 111011FAD By similarity
Nucleotide binding1175 – 119319NADP By similarity
Nucleotide binding1273 – 128715NADP By similarity
Region641 – 66121Calmodulin-binding Potential
Compositional bias24 – 5128Gln-rich
Compositional bias76 – 794Poly-Gly
Compositional bias145 – 15612Poly-Gly

Sites

Metal binding3281Iron (heme axial ligand) By similarity

Natural variations

Alternative sequence201 – 21414FMHLD…SLLMR → RFFPARRPPVRAAL in isoform 3.
VSP_003585
Alternative sequence215 – 13491135Missing in isoform 3.
VSP_003586
Alternative sequence417 – 521105Missing in isoform 2.
VSP_003587
Alternative sequence701 – 74646IYCMS…YAMRV → CPVGSVSSDPQDPVQLGLVV VLVSSTCVCKKHLPAAWQNK ISCKHL in isoform 6.
VSP_003590
Alternative sequence701 – 7044IYCM → VSLT in isoform 5.
VSP_003588
Alternative sequence705 – 1349645Missing in isoform 5.
VSP_003589
Alternative sequence736 – 75621LFSQE…HGLQD → VSTPPRKDHTELINGLGPAA F in isoform 4.
VSP_003592
Alternative sequence747 – 1349603Missing in isoform 6.
VSP_003591
Alternative sequence757 – 1349593Missing in isoform 4.
VSP_003593
Alternative sequence758 – 1291534Missing in isoform 10.
VSP_003594

Experimental info

Sequence conflict201S → A in AAC46882. Ref.1
Sequence conflict241Q → QQ in AAC46882. Ref.1
Sequence conflict1051S → L in AAC46882. Ref.1
Sequence conflict2871S → C in AAC46882. Ref.1
Sequence conflict3731T → S in AAF25682. Ref.2
Sequence conflict11971S → R in AAC46882. Ref.1
Sequence conflict11971S → R in AAF25682. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) (C) (dNOS-1) [UniParc].

Last modified June 10, 2008. Version 3.
Checksum: E19D8CBAEFAF76FC

FASTA1,349151,715
        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 

« Hide

Isoform 2 (dNOS-2) (E).

Checksum: AD7AA548C03AE48F
Show »

FASTA1,244139,754
Isoform 3 (dNOS-3).

Checksum: AA970488F5BFBF76
Show »

FASTA21422,460
Isoform 4 (B) (dNOS-4) (F) (J).

Checksum: 1ABA7993149272D0
Show »

FASTA75684,261
Isoform 5 (dNOS-5) (H).

Checksum: EEF32F5F9BB8091E
Show »

FASTA70478,690
Isoform 6 (dNOS-6) (I).

Checksum: 8449B48E111D7132
Show »

FASTA74683,144
Isoform 10 (dNOS-10) (G).

Checksum: 86C08065EBA6C062
Show »

FASTA81591,268

References

« Hide 'large scale' references
[1]"Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase."
Regulski M., Tully T.
Proc. Natl. Acad. Sci. U.S.A. 92:9072-9076(1995) [PubMed: 7568075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME REGULATION.
Tissue: Head.
[2]"The Drosophila nitric-oxide synthase gene (dNOS) encodes a family of proteins that can modulate NOS activity by acting as dominant negative regulators."
Stasiv Y., Regulski M., Kuzin B., Tully T., Enikolopov G.
J. Biol. Chem. 276:42241-42251(2001) [PubMed: 11526108] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE.
Tissue: Embryo and Larva.
[3]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: Berkeley.
Tissue: Embryo.
[6]"Characterization of Drosophila nitric oxide synthase: a biochemical study."
Sengupta R., Sahoo R., Mukherjee S., Regulski M., Tully T., Stuehr D.J., Ghosh S.
Biochem. Biophys. Res. Commun. 306:590-597(2003) [PubMed: 12804606] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

U25117 mRNA. Translation: AAC46882.1.
AF215700 expand/collapse EMBL AC list , AF215691, AF215692, AF215693, AF215694, AF215695, AF215696, AF215697, AF215698, AF215699 Genomic DNA. Translation: AAF25682.1.
AE014134 Genomic DNA. Translation: AAF53014.1.
AE014134 Genomic DNA. Translation: AAZ66450.1.
AE014134 Genomic DNA. Translation: AAZ66451.1.
AE014134 Genomic DNA. Translation: AAZ66452.1.
AE014134 Genomic DNA. Translation: AAZ66453.1.
AE014134 Genomic DNA. Translation: AAZ66454.1.
AE014134 Genomic DNA. Translation: AAZ66455.1.
AE014134 Genomic DNA. Translation: AAZ66456.1.
AE014134 Genomic DNA. Translation: AAZ66457.1.
BT010016 mRNA. Translation: AAQ22485.1.
PIRT13254.
RefSeqNP_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.
UniGeneDm.2707

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2I86model-@217-629[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ27571. 2 interactions.

Genome annotation databases

EnsemblFBgn0011676. Drosophila melanogaster. [Contig view]
GeneID34495.
KEGGdme:Dmel_CG6713.

Organism-specific databases

FlyBaseFBgn0011676. Nos.

Phylogenomic databases

OMAQ27571. KPSFEYQ.

Enzyme and pathway databases

BRENDA1.14.13.39. 48.

Gene expression databases

ArrayExpressQ27571.
GermOnlineCG6713. Drosophila melanogaster.

Family and domain databases

InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012144. Nitric-oxide_synthase.
IPR004030. NO_synthase_oxygenase_reg.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
Gene3DG3DSA:3.90.340.10. NO_synthase_oxygenase_reg. 1 hit.
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio788761.

Entry information

Entry nameNOS_DROME
AccessionPrimary (citable) accession number: Q27571
Secondary accession number(s): A4V0K9 expand/collapse secondary AC list , A4V0L0, Q4ABG3, Q4ABG4, Q4ABG5, Q4ABG6, Q4ABG7, Q7YU33, Q9U096, Q9VKP8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 10, 2008
Last modified: June 16, 2009
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents