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UniProtKB/Swiss-Prot Q27571 (NOS_DROME)
Last modified
November 25, 2008.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin
| Protein names | Recommended name: Nitric oxide synthase EC=1.14.13.39 Alternative name(s): dNOS | ||||
| Gene names |
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| Organism | Drosophila melanogaster (Fruit fly) [Complete proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 1349 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. |
| Catalytic activity | L-arginine + n NADPH + m O(2) = 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. |
| 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. |
| Sequence similarities | Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain. |
Ontologies
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1349 | 1349 | Nitric oxide synthase | PRO_0000170951 | |||||
Regions | |||||||||
| Domain | 671 – 868 | 198 | Flavodoxin-like | ||||||
| Domain | 928 – 1167 | 240 | FAD-binding FR-type | ||||||
| Nucleotide binding | 814 – 845 | 32 | FMN By similarity | ||||||
| Nucleotide binding | 957 – 968 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 1100 – 1110 | 11 | FAD By similarity | ||||||
| Nucleotide binding | 1175 – 1193 | 19 | NADP By similarity | ||||||
| Nucleotide binding | 1273 – 1287 | 15 | NADP By similarity | ||||||
| Region | 641 – 661 | 21 | Calmodulin-binding Potential | ||||||
| Compositional bias | 24 – 51 | 28 | Gln-rich | ||||||
| Compositional bias | 76 – 79 | 4 | Poly-Gly | ||||||
| Compositional bias | 145 – 156 | 12 | Poly-Gly | ||||||
Sites | |||||||||
| Metal binding | 328 | 1 | Iron (heme axial ligand) By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 201 – 214 | 14 | FMHLD…SLLMR → RFFPARRPPVRAAL in isoform 3. | VSP_003585 | |||||
| Alternative sequence | 215 – 1349 | 1135 | Missing in isoform 3. | VSP_003586 | |||||
| Alternative sequence | 417 – 521 | 105 | Missing in isoform 2. | VSP_003587 | |||||
| Alternative sequence | 701 – 746 | 46 | IYCMS…YAMRV → CPVGSVSSDPQDPVQLGLVV VLVSSTCVCKKHLPAAWQNK ISCKHL in isoform 6. | VSP_003590 | |||||
| Alternative sequence | 701 – 704 | 4 | IYCM → VSLT in isoform 5. | VSP_003588 | |||||
| Alternative sequence | 705 – 1349 | 645 | Missing in isoform 5. | VSP_003589 | |||||
| Alternative sequence | 736 – 756 | 21 | LFSQE…HGLQD → VSTPPRKDHTELINGLGPAA F in isoform 4. | VSP_003592 | |||||
| Alternative sequence | 747 – 1349 | 603 | Missing in isoform 6. | VSP_003591 | |||||
| Alternative sequence | 757 – 1349 | 593 | Missing in isoform 4. | VSP_003593 | |||||
| Alternative sequence | 758 – 1291 | 534 | Missing in isoform 10. | VSP_003594 | |||||
Experimental info | |||||||||
| Sequence conflict | 20 | 1 | S → A in AAC46882. Ref.1 | ||||||
| Sequence conflict | 24 | 1 | Q → QQ in AAC46882. Ref.1 | ||||||
| Sequence conflict | 105 | 1 | S → L in AAC46882. Ref.1 | ||||||
| Sequence conflict | 287 | 1 | S → C in AAC46882. Ref.1 | ||||||
| Sequence conflict | 373 | 1 | T → S in AAF25682. Ref.2 | ||||||
| Sequence conflict | 1197 | 1 | S → R in AAC46882. Ref.1 | ||||||
| Sequence conflict | 1197 | 1 | S → R in AAF25682. Ref.2 | ||||||
Sequences
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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. 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., |

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