Q9VIS1 (CDGAP_DROME) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: GTPase-activating protein CdGAPr Alternative name(s): d-CdGAPr | ||||
| Gene names |
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| Organism | Drosophila melanogaster (Fruit fly) | ||||
| 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 | 1843 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Probably functions as a GTPase-activating protein (GAP) for RAC1 and/or CDC42. Required for optic stalk formation. Ref.6 |
| Tissue specificity | Ubiquitously expressed. Ref.1 |
| Developmental stage | Expressed at all developmental stages, with highest expression at the posterior pole of the early cellular blastoderm, the neuro-ectoderm prior to neuroblast delamination, rows of epidermal cells in the most posterior part of thoracic and first abdominal segments and a ring of epidermal cells at the posterior end of the embryo. Ref.1 |
| Sequence similarities | Contains 1 Rho-GAP domain. Contains 1 SH3 domain. |
| Sequence caution | The sequence AAM49910.1 differs from that shown. Reason: Erroneous initiation. The sequence AAT94493.1 differs from that shown. Reason: Frameshift at position 351. |
Ontologies
| Keywords | |
|---|---|
| Domain | Coiled coil SH3 domain |
| Molecular function | Developmental protein GTPase activation |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | retinal ganglion cell axon guidance Inferred from mutant phenotype Ref.1Ref.6. Source: UniProtKB signal transductionInferred from electronic annotation. Source: InterPro |
| Cellular component | intracellular Inferred from electronic annotation. Source: InterPro |
| Molecular function | GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1843 | 1843 | GTPase-activating protein CdGAPr | PRO_0000320117 | |||||
Regions | |||||||||
| Domain | 295 – 363 | 69 | SH3 | ||||||
| Domain | 424 – 618 | 195 | Rho-GAP | ||||||
| Coiled coil | 1378 – 1404 | 27 | Potential | ||||||
| Compositional bias | 632 – 642 | 11 | Poly-Ala | ||||||
| Compositional bias | 957 – 960 | 4 | Poly-Pro | ||||||
| Compositional bias | 1041 – 1045 | 5 | Poly-Ser | ||||||
| Compositional bias | 1171 – 1174 | 4 | Poly-Gln | ||||||
| Compositional bias | 1244 – 1248 | 5 | Poly-Ala | ||||||
Amino acid modifications | |||||||||
| Modified residue | 166 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 168 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 180 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 837 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 840 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 843 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 851 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 861 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 872 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 876 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1029 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1118 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 1121 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 1125 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1216 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 1281 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1284 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1453 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1456 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 1679 | 1 | Phosphothreonine Ref.8 | ||||||
Experimental info | |||||||||
| Sequence conflict | 1092 | 1 | Missing in AAT94493. Ref.4 | ||||||
| Sequence conflict | 1092 | 1 | Missing in AAM49910. Ref.5 | ||||||
| Sequence conflict | 1818 – 1820 | 3 | NNR → K in AAM49910. Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Dynamic expression of d-CdGAPr, a novel Drosophila melanogaster gene encoding a GTPase activating protein." Sagnier T., Grienenberger A., Mariol M.-C., Berenger H., Pradel J., Graba Y. Mech. Dev. 94:267-270(2000) [PubMed: 10842085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. |
| [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. Strain: Berkeley. |
| [4] | Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo. |
| [5] | "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 1062-1843. Strain: Berkeley. Tissue: Embryo. |
| [6] | "Focal adhesion kinase controls morphogenesis of the Drosophila optic stalk." Murakami S., Umetsu D., Maeyama Y., Sato M., Yoshida S., Tabata T. Development 134:1539-1548(2007) [PubMed: 17360775] [Abstract] Cited for: FUNCTION. |
| [7] | "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1216, MASS SPECTROMETRY. |
| [8] | "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-166; SER-168; SER-180; SER-837; SER-840; THR-843; SER-851; SER-861; SER-872; SER-876; SER-1029; THR-1118; THR-1121; SER-1125; SER-1281; SER-1284; SER-1453; SER-1456 AND THR-1679, MASS SPECTROMETRY. Tissue: Embryo. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF218776 mRNA. Translation: AAF44627.1. AE014134 Genomic DNA. Translation: AAF53844.2. BT015264 mRNA. Translation: AAT94493.1. Frameshift. AY118541 mRNA. Translation: AAM49910.1. Different initiation. |
| RefSeq | NP_610002.1. NM_136158.3. |
| UniGene | Dm.3427. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1XA6 based on UniProtKB P52757. |
| ProteinModelPortal | Q9VIS1. |
| SMR | Q9VIS1. Positions 299-359, 420-620. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-1558952. |
| STRING | Q9VIS1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | FBtr0081318; FBpp0080851; FBgn0032821. |
| GeneID | 35267. |
| KEGG | dme:Dmel_CG10538. |
| NMPDR | fig|7227.3.peg.3052. |
| UCSC | CG10538-RA. d. melanogaster. |
Organism-specific databases | |
| CTD | 35267. |
| FlyBase | FBgn0032821. CdGAPr. |
Phylogenomic databases | |
| eggNOG | inNOG07872. |
| GeneTree | EMGT00050000001404. |
| InParanoid | Q9VIS1. |
| OMA | AMFESRS. |
| OrthoDB | EOG4CNP5W. |
| PhylomeDB | Q9VIS1. |
Gene expression databases | |
| ArrayExpress | Q9VIS1. |
| Bgee | Q9VIS1. |
Family and domain databases | |
| InterPro | IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. IPR011511. SH3_2. IPR001452. SH3_domain. [Graphical view] |
| Gene3D | G3DSA:1.10.555.10. RhoGAP. 1 hit. |
| Pfam | PF00620. RhoGAP. 1 hit. PF07653. SH3_2. 1 hit. [Graphical view] |
| SMART | SM00324. RhoGAP. 1 hit. SM00326. SH3. 1 hit. [Graphical view] |
| SUPFAM | SSF48350. Rho_GAP. 1 hit. SSF50044. SH3. 1 hit. |
| PROSITE | PS50238. RHOGAP. 1 hit. PS50002. SH3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 792708. |
Entry information
| Entry name | CDGAP_DROME | ||||||||
| Accession | Primary (citable) accession number: Q9VIS1 Secondary accession number(s): Q6AWI4, Q8MSV9, Q9NCL1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | 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