Reviewed,
UniProtKB/Swiss-Prot Q9VT28 (FRY_DROME)
Last modified
June 16, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein furry | ||||
| 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 | 3479 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Trc/fry signaling pathway plays a key role in maintaining the integrity of polarized cell extensions (arista) during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching. Fry positively regulates trc kinase activity. Ref.1 Ref.5 |
| Tissue specificity | Co-expressed with trc in all da neurons in third instar wild-type larvae; axons and dendritic branches. Ref.5 |
| Developmental stage | Expression is very low in embryonic and early larval stages, increases to be high from third larval instar to adults. Ref.1 |
| Disruption phenotype | Flies exhibit branched arista laterals, branched bristles and a strong multiple hair cell phenotype that consists of clusters of epidermal hairs and branched hairs. Dendrites of fry and trc mutants display excessive terminal branching. Branched laterals in mutant pupae arista are due to the splitting of individual laterals during elongation and abnormally shaped actin bundles. Ref.1 |
| Sequence similarities | Belongs to the furry protein family. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform B Ref.1 (identifier: Q9VT28-1) Also known as: Long; 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 D Ref.1 (identifier: Q9VT28-2) Also known as: Short; The sequence of this isoform differs from the canonical sequence as follows: 1624-1629: EDDKVG → GMRFSY 1630-3479: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3479 | 3479 | Protein furry | PRO_0000282939 | |||||
Regions | |||||||||
| Compositional bias | 174 – 202 | 29 | Gln-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 129 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 1838 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 1841 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 2357 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 2842 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 2845 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 2851 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 2853 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 2999 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 3001 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 3004 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 3018 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 3019 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 3025 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 3027 | 1 | Phosphoserine Ref.6 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1624 – 1629 | 6 | EDDKVG → GMRFSY in isoform D. Ref.1 | VSP_052372 | |||||
| Alternative sequence | 1630 – 3479 | 1850 | Missing in isoform D. Ref.1 | VSP_052373 | |||||
Experimental info | |||||||||
| Sequence conflict | 170 | 1 | E → V in AAG41424. Ref.1 | ||||||
| Sequence conflict | 170 | 1 | E → V in AAK37558. Ref.1 | ||||||
| Sequence conflict | 1876 | 1 | M → I in AAG41424. Ref.1 | ||||||
| Sequence conflict | 1933 | 1 | I → L in AAG41424. Ref.1 | ||||||
| Sequence conflict | 2530 | 1 | T → I in AAG41424. Ref.1 | ||||||
| Sequence conflict | 3375 | 1 | I → V in AAL40005. Ref.4 | ||||||
| Sequence conflict | 3403 | 1 | I → M in AAL40005. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The furry gene of Drosophila is important for maintaining the integrity of cellular extensions during morphogenesis." Cong J., Geng W., He B., Liu J., Charlton J., Adler P.N. Development 128:2793-2802(2001) [PubMed: 11526084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Tissue: Imaginal disk. |
| [2] | "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. |
| [3] | "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. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. |
| [4] | "A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2555-3479. Strain: Berkeley. Tissue: Embryo. |
| [5] | "Control of dendritic branching and tiling by the Tricornered-kinase/Furry signaling pathway in Drosophila sensory neurons." Emoto K., He Y., Ye B., Grueber W.B., Adler P.N., Jan L.Y., Jan Y.-N. Cell 119:245-256(2004) [PubMed: 15479641] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY. |
| [6] | "Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-1838; SER-1841; SER-2357; THR-2842; SER-2845; SER-2851; SER-2853; SER-2999; SER-3001; THR-3004; SER-3018; SER-3019; SER-3025 AND SER-3027, MASS SPECTROMETRY. Tissue: Embryo. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF310159 mRNA. Translation: AAG41424.1. AF351187 mRNA. Translation: AAK37558.1. AE014296 Genomic DNA. Translation: AAF50228.2. AE014296 Genomic DNA. Translation: ABI31247.1. AY069860 mRNA. Translation: AAL40005.1. Different initiation. | |
| RefSeq | NP_001036598.1. NP_729520.1. |
| UniGene | Dm.1919 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9VT28. 16 interactions. |
Genome annotation databases | |
| Ensembl | FBgn0016081. Drosophila melanogaster. [Contig view] |
| GeneID | 39122. |
| KEGG | dme:Dmel_CG32045. |
| NMPDR | fig|7227.3.peg.9107. |
Organism-specific databases | |
| FlyBase | FBgn0016081. fry. |
Phylogenomic databases | |
| OMA | Q9VT28. DDTASEQ. |
Gene expression databases | |
| ArrayExpress | Q9VT28. |
Family and domain databases | |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 812033. |
Entry information
| Entry name | FRY_DROME | ||||||||
| Accession | Primary (citable) accession number: Q9VT28 Secondary accession number(s): Q0E8G4 Q9GPT8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


