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General Information
Symbol
Dmel\BicD
Species
D. melanogaster
Name
Bicaudal D
Annotation Symbol
CG6605
Feature Type
FlyBase ID
FBgn0000183
Gene Model Status
Stock Availability
Gene Snapshot
Bicaudal D (BicD) encodes a cytoplasmic protein that links diverse cargo to the dynein/dynactin motor. Cargos like mRNAs, proteins and organelles are transported along microtubules. Through this mechanism the product of BicDcontrols spatial aspects of gene expression and polarity formation during development. Additionally, it supports physiology of differentiated polar cells and the function of the nervous system. [Date last reviewed: 2019-03-07]
Also Known As
Bic-D
Key Links
Genomic Location
Cytogenetic map
Sequence location
2L:17,459,605..17,473,215 [-]
Recombination map
2-53
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Protein Family (UniProt)
Belongs to the BicD family. (P16568)
Protein Signatures (InterPro)
Summaries
Protein Function (UniProtKB)
This protein is essential for differentiation. It may play a role in localizing of Nanos (a maternal determinant) activity in oocytes. During oogenesis, plays a specific role, together with Rab6 but independently of Sec5, in the polarization of the oocyte microtubule cytoskeleton, in oskar mRNA localization and in the anterodorsal secretion of grk.
(UniProt, P16568)
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
BicD
A maternal-effect semilethal; substantial numbers of embryos produced by BicD/+ mothers give rise to normal larvae; the remainder fail to hatch and vary in phenotype. The array of phenotypes encountered is the same as that produced by BicC/+ females. The incidence and severity of abnormal embryos vary with genetic background and temperature, the incidence being highest at 18, and decreasing at higher temperatures. BicD homozygotes, either homoallelic or heteroallelic, and BicC/BicD heterozygotes are female fertile, although producing eggs with fused or reduced chorionic appendages; the majority of their embryos are abnormal and the influence of temperature, if any, obscure. BicD/+/+ duplication-bearing females produce few if any abnormal embryos, whereas BicD/Df(2L)TW119 females produce more abnormal embryos than BicD/+, i.e., with respect to the severity of phenotype, BicD/0 > BicD/+ > BicD/+/+; however, simply a deficiency of BicD product does not account for the abnormal phenotype, since embryos produced by females carrying one dose of BicD+ over a deficiency develop normally. Embryos produced by homozygous BicD females display symmetrical patterns of cad+ polypeptide distribution during early development (Mlodzik and Gehring, 1987, Cell 48: 465-78). Abnormal embryo production by BicD/+ females enhanced by the heterozygosity for the mutant allele of or deficiency for l(2)49; Mohler and Wieschaus speculate that l(2)49 is an allele of bic In addition, eg, stau, tor, and trk, maternal-effect mutants that affect early anterior but not posterior development, act as dominant enhancer of BicD; other maternal-effect mutants ineffective. Bicaudal embryos exhibit nanos protein at both anterior and posterior poles and the absence of hunchback protein in both ends of the embryo; embryos produced by BicD1/BicD2;osk/osk females do not express nos; display a burst of anterior, bcd-dependent hb expression not seen in bicaudal embryos, which is correlated with a dramatic expansion of kni expression (abdominal) and failure to express Kr (thorax and anterior abdomen). BicD expressed early in oogenesis; in wild type, protein first appears in the cytoplasm of all cells in 16-cell cysts in the middle of the germarium; upon entering the vitellarium, protein begins to accumulate in the oocyte and continues to do so for as long as observations are possible. The early embryos produced by such females show uniform distribution of BicD protein, which becomes localized to the cortical cytoplasm at blastoderm formation; anterior-to-posterior distribution remains uniform. Protein disappears at gastrulation. In BicD1/BicD2 females protein accumulation in the oocyte is precocious and greater than normal and the adjacent nurse cells may become visibly depleted; in the embryo, the protein appears to be concentrated as a cap over the anterior third and uniformly less concentrated in the remainder of the embryo. BicDrv1 females display extreme concentration of product in the presumptive oocyte and virtually none in the nurse cells; however, the presumptive oocyte never develops as an oocyte but remains nurse-cell like until the cyst degenerates.
Summary (Interactive Fly)
Gene Model and Products
Number of Transcripts
4
Number of Unique Polypeptides
3

Please see the GBrowse view of Dmel\BicD or the JBrowse view of Dmel\BicD for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model
Gene model reviewed during 5.44
Stop-codon suppression (UAA) postulated; FBrf0216884.
gene_with_stop_codon_read_through ; SO:0000697
Gene model reviewed during 5.45
Tissue-specific extension of 3' UTRs observed during later stages (FBrf0218523, FBrf0219848); all variants may not be annotated
Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0081002
4149
782
FBtr0305688
3705
750
FBtr0330225
5361
782
FBtr0330226
4149
802
Additional Transcript Data and Comments
Reported size (kB)
5.7, 4.4, 3.8 (northern blot)
4.0, 3.6 (northern blot)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0080555
89.0
782
4.81
FBpp0296968
85.5
750
4.69
FBpp0303258
89.0
782
4.81
FBpp0303259
91.2
802
4.95
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

782 aa isoforms: BicD-PA, BicD-PC
Additional Polypeptide Data and Comments
Reported size (kDa)
Comments
Phosphorylation of BicD protein appears to be essential for accumulation of BicD protein in the oocyte and for oocyte differentiaion.
The predicted amino acid sequence of BicD shows some similarity to the rod region of myosin heavy chain as well as lamin, desmin, keratin, and other intermediate filament proteins.
External Data
Subunit Structure (UniProtKB)
Interacts (via C-terminal domain) with Rab6.
(UniProt, P16568)
Crossreferences
InterPro - A database of protein families, domains and functional sites
Linkouts
Sequences Consistent with the Gene Model
Nucleotide / Polypeptide Records
 
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\BicD using the Feature Mapper tool.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Gene Ontology (25 terms)
Molecular Function (6 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
inferred from physical interaction with FLYBASE:Rab2; FB:FBgn0014009
inferred from physical interaction with FLYBASE:Rab39; FB:FBgn0029959
inferred from physical interaction with FLYBASE:Rab30; FB:FBgn0031882
Terms Based on Predictions or Assertions (3 terms)
CV Term
Evidence
References
inferred from electronic annotation with InterPro:IPR018477
(assigned by InterPro )
inferred from electronic annotation with InterPro:IPR018477
(assigned by InterPro )
non-traceable author statement
non-traceable author statement
Biological Process (15 terms)
Terms Based on Experimental Evidence (12 terms)
CV Term
Evidence
References
inferred from mutant phenotype
inferred from direct assay
inferred from mutant phenotype
inferred from high throughput mutant phenotype
inferred from mutant phenotype
Terms Based on Predictions or Assertions (6 terms)
CV Term
Evidence
References
Cellular Component (4 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
inferred from direct assay
inferred from direct assay
inferred from high throughput direct assay
Terms Based on Predictions or Assertions (2 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN001261414
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN001261414
(assigned by GO_Central )
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
organism

Comment: maternally deposited

northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
4.4kb BicD transcripts are detected in RNA from adult females, dissected ovaries and early embryos. The maternal transcripts disappear by 4-8hr embryos. The 4.4kb transcript reappears after 8 hours and is present at all stages as well as in adult males. BicD transcripts are observed by in situ hybridization in egg chambers from stage 1-2 onward. Up to stage 7, expression is observed in the oocyte concentrated around the nucleus. From stage 8 on, expression is observed in nurse cells as well. During stages 8-10B, BicD transcripts in the oocyte are localized to the anterior end forming a cap. During the last stages of oogenesis and in early embryogenesis, BicD transcripts are uniformly distributed.
Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
In wild-type stage 10 egg chambers, BicD localizes along the oocyte cortex.
BicD protein is detected in the germline throughout oogenesis and is enriched in the oocyte. From stage 2-6, it partially co-localizes with pAbp at the posterior cortex of the oocyte. In early embryos, BicD protein is noticeably enriched apically to the blastoderm nuclei even though large amounts of the protein are also present in the basal cytoplasm. It partially co-localizes with pAbp in the early embryo.
The BicD and egl proteins, as previously described for the orb protein, accumulate in the presumptive oocyte following fusome disassembly in germarium region 2a during oocyte specification and are relocalized to the posterior of the oocyte between germarium regions 2b and 3 during oocyte polarization.
In germarial region 1, all cystocytes stain evenly for BicD. Differential accumulation of the protein can be seen clearly in germarial region 2B and onward with greater amounts in the oocyte. The relative enrichment is much less dramatic than the RNA. In the BicDR26 mutant, protein accumulates in the pro-oocyte at significantly higher levels than in wild type. In BicDr mutants, BicD protein does not localize to the oocyte. FBgn0000183:BicD protein normally accumulates at high levels in the pro-oocyte and persists in the oocyte. This process is affected differently in mutants of FBgn0000183:BicD and eg1@.
BicD protein is uniformly distributed along the anteroposterior axis in newly laid eggs and young embryos. Most of the protein disappears as the blastoderm forms and gastrulation begins. In ovaries, BicD is detected very early in oogenesis in the newly formed 16-cell clusters. The protein is present throughout the cluster but is higher in the prospective oocyte. the protein becomes concentrated in the oocyte relative to the nurse cells.
Marker for
 
Subcellular Localization
CV Term
Evidence
References
inferred from direct assay
inferred from direct assay
inferred from high throughput direct assay
Expression Deduced from Reporters
Stage
Tissue/Position (including subcellular localization)
Reference
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\BicD in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
FlyExpress - Embryonic expression images (BDGP data)
  • Stages(s) 1-3
  • Stages(s) 4-6
  • Stages(s) 7-8
  • Stages(s) 9-10
  • Stages(s) 11-12
  • Stages(s) 13-16
Alleles, Insertions, and Transgenic Constructs
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Sterility
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
embryonic neuroblast & spindle, with BicDHA40.Tag:HA, Df(2L)TW119
embryonic neuroblast & spindle, with BicDR26, Df(2L)TW119
embryonic neuroblast & spindle, with Df(2L)TW119/BicDR26
embryonic neuroblast & spindle (with Df(2L)TW119), with BicDHA40.Tag:HA
microtubule organizing center & oocyte
photoreceptor cell & nucleus (with Df(2L)TW119)
photoreceptor cell | precursor & nucleus
Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (2)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
14 of 15
Yes
Yes
13 of 15
No
Yes
Model Organism Orthologs (via DIOPT v7.1)
Mus musculus (laboratory mouse) (2)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
14 of 15
Yes
Yes
12 of 15
No
Yes
Rattus norvegicus (Norway rat) (2)
11 of 13
Yes
Yes
10 of 13
No
Yes
Xenopus tropicalis (Western clawed frog) (3)
2 of 12
Yes
Yes
1 of 12
No
Yes
1 of 12
No
Yes
Danio rerio (Zebrafish) (5)
12 of 15
Yes
Yes
11 of 15
No
Yes
10 of 15
No
Yes
4 of 15
No
Yes
1 of 15
No
Yes
Caenorhabditis elegans (Nematode, roundworm) (2)
14 of 15
Yes
Yes
1 of 15
No
Yes
Arabidopsis thaliana (thale-cress) (1)
1 of 9
Yes
Yes
Saccharomyces cerevisiae (Brewer's yeast) (1)
1 of 15
Yes
No
Schizosaccharomyces pombe (Fission yeast) (0)
No records found.
Orthologs in Drosophila Species (via OrthoDB v9.1) ( EOG091903IV )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila melanogaster
fruit fly
Drosophila suzukii
Spotted wing Drosophila
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG0915023H )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Lucilia cuprina
Australian sheep blowfly
Mayetiola destructor
Hessian fly
Mayetiola destructor
Hessian fly
Aedes aegypti
Yellow fever mosquito
Anopheles darlingi
American malaria mosquito
Anopheles gambiae
Malaria mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W01VR )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Danaus plexippus
Monarch butterfly
Heliconius melpomene
Postman butterfly
Apis florea
Little honeybee
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Dendroctonus ponderosae
Mountain pine beetle
Tribolium castaneum
Red flour beetle
Pediculus humanus
Human body louse
Rhodnius prolixus
Kissing bug
Rhodnius prolixus
Kissing bug
Rhodnius prolixus
Kissing bug
Cimex lectularius
Bed bug
Acyrthosiphon pisum
Pea aphid
Zootermopsis nevadensis
Nevada dampwood termite
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X0JJN )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( EOG091G01P4 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strongylocentrotus purpuratus
Purple sea urchin
Ciona intestinalis
Vase tunicate
Ciona intestinalis
Vase tunicate
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Paralogs
Paralogs (via DIOPT v7.1)
Drosophila melanogaster (Fruit fly) (0)
No records found.
Human Disease Associations
FlyBase Human Disease Model Reports
Disease Model Summary Ribbon
Disease Ontology (DO) Annotations
Models Based on Experimental Evidence ( 0 )
Allele
Disease
Evidence
References
Potential Models Based on Orthology ( 0 )
Human Ortholog
Disease
Evidence
References
Modifiers Based on Experimental Evidence ( 0 )
Allele
Disease
Interaction
References
Comments on Models/Modifiers Based on Experimental Evidence ( 0 )
 
Disease Associations of Human Orthologs (via DIOPT v7.1 and OMIM)
Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
Functional Complementation Data
Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
Interactions
Summary of Physical Interactions
esyN Network Diagram
Show neighbor-neighbor interactions:
Select Layout:
Legend:
Protein
RNA
Selected Interactor(s)
Interactions Browser

Please see the Physical Interaction reports below for full details
protein-protein
Physical Interaction
Assay
References
RNA-protein
Physical Interaction
Assay
References
Summary of Genetic Interactions
esyN Network Diagram
esyN Network Key:
Suppression
Enhancement

Please look at the allele data for full details of the genetic interactions
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
External Data
Subunit Structure (UniProtKB)
Interacts (via C-terminal domain) with Rab6.
(UniProt, P16568 )
Linkouts
BioGRID - A database of protein and genetic interactions.
DroID - A comprehensive database of gene and protein interactions.
InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
MIST (genetic) - An integrated Molecular Interaction Database
MIST (protein-protein) - An integrated Molecular Interaction Database
Pathways
Gene Group - Pathway Membership (FlyBase)
External Data
Linkouts
Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
Genomic Location and Detailed Mapping Data
Chromosome (arm)
2L
Recombination map
2-53
Cytogenetic map
Sequence location
2L:17,459,605..17,473,215 [-]
FlyBase Computed Cytological Location
Cytogenetic map
Evidence for location
36C9-36C9
Limits computationally determined from genome sequence between P{lacW}Mhck10423&P{lacW}Cask03902 and P{lacW}Aac11k06710
Experimentally Determined Cytological Location
Cytogenetic map
Notes
References
36C-36C
(determined by in situ hybridisation)
Experimentally Determined Recombination Data
Left of (cM)
Right of (cM)
Notes
Mapping based on an estimated four recombinants between dl and BicD out of 4,000.
Stocks and Reagents
Stocks (18)
Genomic Clones (24)
cDNA Clones (269)
 

Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.

cDNA clones, fully sequences
BDGP DGC clones
Other clones
Drosophila Genomics Resource Center cDNA clones

For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

cDNA Clones, End Sequenced (ESTs)
Other clones
RNAi and Array Information
Linkouts
DRSC - Results frm RNAi screens
GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
Antibody Information
Laboratory Generated Antibodies
Commercially Available Antibodies
Other Information
Relationship to Other Genes
Source for database identify of
Source for identity of: BicD CG6605
Source for database merge of
Source for merge of: BicD anon- EST:fe2A11
Additional comments
Other Comments
BicD is required for the rapid transport of grk, bcd AND osk RNAs from nurse cells to the oocyte by a mechanism distinct from the general flow of cytoplasm from nurse cells to oocyte.
BicD promotes the iniation of rapid minus-end directed movement of mRNAs along microtubules.
BicD mediates the apical localisation of insc mRNA in embryonic neuroblasts.
par-1 appears to act on the cytoskeleton to affect polarisation within the oocyte in conjunction with BicD, egl and dynein.
BicD is required for the formation of and cytoskeletal organisation of the egg chamber.
None of the cells in the female germline cyst form synaptonemal complex in BicD null mutants.
Only deletion of the C-terminal heptad repeat results in a BicD protein that has lost zygotic and ovarian functions. Deletion of any other of the heptad repeats results in a protein with full zygotic function but affected ovarian function. The functional importance of each domain is well correlated with its conservation in evolution. Yeast two hybrid assays show that BicD forms homodimers. BicD exists as a multimeric protein complex consisting of egl and at least two BicD monomers.
egl protein colocalises with BicD protein to the oocyte in three stages that correlate with the stepwise polarization of the oocyte. Immunoprecipitation experiments show that both proteins are part of a protein complex. Results propose that the egl-BicD protein complex links microtubule polarity and RNA transport. During early oogenesis the complex is required to transport factors promoting oocyte differentiation; during later stages the complex directs the sorting of RNA molecules required for anterior-posterior and dorsoventral patterning of the embryo.
BicD is required for oocyte growth and both dorsoventral and anterior-posterior patterning of the egg chamber. Results also provide evidence for a prepatterning of follicle cell fates independent of the underlying oocyte.
Anterior localisation of RNA during oogenesis is very sensitive to microtubule inhibitors, taxol and other microtubule depolymerising agents. These results, together with colchicine treatment studies, demonstrate that microtubules are required for RNA transport to the oocyte.
Different processes in early oogenesis require different amounts of BicD activity in a process-specific way and certain later processes can proceed at low levels of BicD.
Recessive mutations at egl and BicD, and microtubule assembly inhibitors, disrupt the formation and maintenance of the single polarized microtubule cytoskeleton that connects the oocyte to the 15 nurse cells at the time the oocyte is determined.
Alleles of egl and BicD were used to show that the differentiation of an oocyte is required for maintainance but not establishment of follicle polarity.
BicD,osk, BicD,vas and BicD,nos embryos suppress all abdominal development: osk, vas and nos genes are critical for the normal and ectopic presence of the posterior signal.
Mutations in maternal anterior class gene BicD interact with RpII140wimp.
The BicD locus affects early oogenesis: mutations cause the production of few, defective germ cells.
Cell biological and genetic evidence suggest that transport of determinants from cystocytes to the pro-oocyte is essential for oocyte determination. Phosphorylation of the BicD protein is essential for its accumulation in the pro-oocyte and this process leads to the gradual localization to the pro-oocyte of the factors required for oocyte differentiation. BicD expression patterns were investigated in egl embryos to determine the relationship between BicD and egl.
In embryos derived from BicD mutant females bcd transcripts localized at the anterior are subjected to ectopic nos activity.
In double mutants BicD, fs(1)N12 all abdominal segments are transformed to the eighth abdominal segment.
Mature follicles are immunologically stained for asymmetric distribution of ecdysteroid-related antigen. During late oogenesis localisation of the antigen changes dramatically suggesting the antigen plays a role in early embryogenesis and, perhaps, in pattern formation.
BicD embryos that have abdominal determinants incorrectly localized to the anterior pole do not show ectopic vas localization. Abdominal development in the anterior depends on the level of vas protein in the embryo.
Mutations at BicD have no effect on vas protein expression.
Mohler and Wieschaus describe a polygenic strain, designated YC67 that parallels the behavior of BicD in all respects except that it is unmappable.
A maternal-effect semi-lethal; substantial numbers of embryos produced by BicD/+ mothers give rise to normal larvae; the remainder fail to hatch and vary in phenotype. The array of phenotypes encountered is the same as that produced by BicC/+ females. The incidence and severity of abnormal embryos vary with genetic background and temperature, the incidence being highest at 18oC and decreasing at higher temperatures. BicD homozygotes, either homoallelic or heteroallelic and BicC/BicD heterozygotes are female fertile, although producing eggs with fused or reduced chorionic appendages; the majority of their embryos are abnormal and the influence of temperature, if any, obscure. BicD/+/+ duplication-bearing females produce few if any abnormal embryos, whereas BicD/Df(2L)TW119 females produce more abnormal embryos than BicD/+, i.e., with respect to the severity of phenotype, BicD/0 > BicD/+ > BicD/+/+; however, simply a deficiency of BicD product does not account for the abnormal phenotype, since embryos produced by females carrying one dose of BicD+ over a deficiency develop normally. Embryos produced by homozygous BicD females display symmetrical patterns of cad+ polypeptide distribution during early development (Mlodzik and Gehring, 1987). Abnormal embryo production by BicD/+ females enhanced by the heterozygosity for the mutant allele of or deficiency for l(2)49; Mohler and Wieschaus (1986) speculate that l(2)49 is an allele of bic In addition, eg, stau, tor, and trk, maternal-effect mutants that affect early anterior but not posterior development, act as dominant enhancer of BicD; other maternal-effect mutants ineffective. Bicaudal embryos exhibit nanos protein at both anterior and posterior poles and the absence of hunchback protein in both ends of the embryo; embryos produced by BicD1/BicD2;osk/osk females do not express nos; display a burst of anterior, bcd-dependent hb expression not seen in bicaudal embryos, which is correlated with a dramatic expansion of kni expression (abdominal) and failure to express Kr (thorax and anterior abdomen). BicD expressed early in oogenesis; in wild type, protein first appears in the cytoplasm of all cells in 16-cell cysts in the middle of the germarium; upon entering the vitellarium, protein begins to accumulate in the oocyte and continues to do so for as long as observations are possible. The early embryos produced by such females show uniform distribution of BicD protein, which becomes localized to the cortical cytoplasm at blastoderm formation; anterior-to-posterior distribution remains uniform. Protein disappears at gastrulation. In BicD1/BicD2 females protein accumulation in the oocyte is precocious and greater than normal and the adjacent nurse cells may become visibly depleted; in the embryo, the protein appears to be concentrated as a cap over the anterior third and uniformly less concentrated in the remainder of the embryo. BicDR26 females display extreme concentration of product in the presumptive oocyte and virtually none in the nurse cells; however, the presumptive oocyte never develops as an oocyte but remains nurse-cell like until the cyst degenerates.
Origin and Etymology
Discoverer
Etymology
Identification
External Crossreferences and Linkouts ( 51 )
Sequence Crossreferences
NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
UniProt/TrEMBL - Automatically annotated and unreviewed records of protein sequence and functional information
Other crossreferences
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
InterPro - A database of protein families, domains and functional sites
KEGG Genes - Molecular building blocks of life in the genomic space.
modMine - A data warehouse for the modENCODE project
Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
Linkouts
BioGRID - A database of protein and genetic interactions.
DroID - A comprehensive database of gene and protein interactions.
DRSC - Results frm RNAi screens
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
FlyMine - An integrated database for Drosophila genomics
Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
MIST (genetic) - An integrated Molecular Interaction Database
MIST (protein-protein) - An integrated Molecular Interaction Database
Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
Synonyms and Secondary IDs (14)
Reported As
Symbol Synonym
Bic-D
(Börner et al., 2016, Vazquez-Pianzola et al., 2014, Vazquez-Pianzola and Suter, 2012, Zhao et al., 2012, Vazquez-Pianzola et al., 2011, Kugler et al., 2010, Ozdowski et al., 2009, Coutelis and Ephrussi, 2007, Houalla and Rao, 2007, Walthall et al., 2007, McCaffrey et al., 2006, Houalla et al., 2005, Koch et al., 2005, Houalla et al., 2004, Horabin et al., 2003, Sardet et al., 2002, Cox et al., 2001, Johnstone and Lasko, 2001, Oh and Steward, 2001, Swan et al., 2001, Vied and Horabin, 2001, Huynh and St. Johnston, 2000, Munn and Steward, 2000, Oh et al., 2000, Pare and Suter, 2000, Oh and Steward, 1999, Stuurman et al., 1999, Swan et al., 1999, Swan et al., 1999, Tan and Schedl, 1999, de Cuevas and Spradling, 1998, Gonzalez-Reyes and St. Johnston, 1998, Hortsch et al., 1998, Oh and Steward, 1998, Pare and Suter, 1998, Styhler et al., 1998, Baens and Marynen, 1997, Capri et al., 1997, Chang-Swain and Schedl, 1997, Hijal et al., 1997, McGrail and Hays, 1997, Nguyen, 1997.4.17, Nguyen and Suter, 1997, Oh and Steward, 1997, Pare and Suter, 1997, Chang-Swain and Schedl, 1996, Digilio et al., 1996, Grunert and St. Johnston, 1996, Li and Kaufman, 1996, Nakamura et al., 1996, Swan and Suter, 1996, Baksa and Steward, 1995, Heino et al., 1995, Mahone et al., 1995, McGrail et al., 1995, Micklem, 1995, Pokrywka and Stephenson, 1995, Sass et al., 1995, Sonnenfeld and Jacobs, 1995, Knowles and Cooley, 1994, Lin et al., 1994, Ran et al., 1994, Theurkauf, 1994, Anonymous, 1993, St. Johnston, 1993, Theurkauf et al., 1993, Theurkauf et al., 1993, Akiyama and Okada, 1992, Lantz et al., 1992, Lasko, 1992, Lehmann, 1992, Ephrussi et al., 1991, Steward and Nusslein-Volhard, 1986)
anon-EST:fe2A11
Secondary FlyBase IDs
  • FBgn0025237
Datasets (0)
Study focus (0)
Experimental Role
Project
Project Type
Title
References (308)