FlyBase Gene Report: Dmel\kel

General Information

Symbol

Dmel\kel

Species

D. melanogaster

Name

kelch

Annotation Symbol

CG7210

Feature Type

protein_coding_gene

FlyBase ID

FBgn0001301

Gene Model Status

Current

Stock Availability

10 publicly available

Gene Snapshot

kelch (kel) encodes a substrate targeting component of a Cullin3-RING ubiquitin E3 ligase. It binds F-actin in vitro, while its predominant in vivo function is in the ubiquitin-proteasome pathway. It has an essential role in oogenesis, where it is required for cytoskeletal organization in ovarian ring canals. [Date last reviewed: 2019-03-14]

Other Summaries

Alliance
Auto summary
UniProtKB
Red Book
Interactive Fly

Key Links

Genomic Location

Cytogenetic map

36E5-36E6

Sequence location

2L:18,129,884..18,138,083 [-]

Recombination map

2-53

Sequence

Get Decorated FASTA

Genomic Maps

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Other Genome Views

The following external sites may use different assemblies or annotations than FlyBase.

Function

GO Summary Ribbons

[Detailed GO annotations]

Protein Family (UniProt)

Protein Signatures (InterPro)

Molecular Function (GO)
[Detailed GO annotations]

Experimental Evidence

actin binding

Predictions / Assertions

Summaries

Protein Function (UniProtKB)

Component of ring canals that regulates the flow of cytoplasm between cells. May be involved in the regulation of cytoplasm flow from nurse cells to the oocyte during oogenesis. Binds actin.

(UniProt, Q04652)

Phenotypic Description (Red Book; Lindsley and Zimm 1992)

kel: kelch

Recessive female sterile. Nurse cell cytoplasm not incorporated in oocyte. Small eggs "open" at anterior pole since egg membranes are not deposited around whole oocyte.

Summary (Interactive Fly)

cytoskeletal protein - actin cross-linker - during oogenesis, phosphorylation of Kelch is critical for the proper morphogenesis of actin during ring canal growth - actin cytoskeletal organization in Drosophila germline ring canals depends on Kelch function in a Cullin-RING E3 ligase.

Interactive Fly

Gene Model and Products

Number of Transcripts

Number of Unique Polypeptides

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

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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

Stop-codon suppression (UGA) postulated; FBrf0057892.

gene_with_stop_codon_read_through ; SO:0000697

Stop-codon suppression supported by data in FBrf0216884.

Low-frequency RNA-Seq exon junction(s) not annotated.

Gene model reviewed during 5.51

Sequence Ontology: Class of Gene

gene_with_stop_codon_read_through

(Jungreis et al., 2011, Xue and Cooley, 1993)

nuclear_gene

protein_coding_gene

Transcript Data

Annotated Transcripts

Name

FlyBase ID

RefSeq ID

Length (nt)

Assoc. CDS (aa)

kel-RA

FBtr0081042

NM_165242

5476

689

kel-RB

FBtr0081043

NM_057241

5476

1477

Additional Transcript Data and Comments

Reported size (kB)

6.0 (northern blot)

(Xue and Cooley, 1993)

Comments

External Data

Crossreferences

Polypeptide Data

Annotated Polypeptides

Name

FlyBase ID

Predicted MW (kDa)

Length (aa)

Theoretical pI

RefSeq ID

GenBank

kel-PA

FBpp0080595

76.6

689

5.40

NP_724095

AAF53651

kel-PB

FBpp0080596

160.0

1477

6.46

NP_476589

AAN11182

Polypeptides with Identical Sequences

None of the polypeptides share 100% sequence identity.

Additional Polypeptide Data and Comments

Reported size (kDa)

160, 76 (kD observed)

(Robinson and Cooley, 1997)

787, 688 (aa); 83.5, 76.5 (kD)

(Xue and Cooley, 1993)

Comments

Two kel proteins are produced from a single transcript through stop codon suppression: a shorter 76kD protein (ORF1), and a "full-length" 160 kD (ORF1 + ORF2) protein. Both proteins co-sediment with ring canal complexes, but the ring canal localization determinants lie in the first ORF. Transgenic kel 76kD ORF1 protein, but not 160 kD full-length protein, is able to rescue female fertility and ring canal morphology.

(Robinson and Cooley, 1997)

Two kel proteins are produced from a single transcript through stop codon suppression: a shorter 76kD protein (ORF1), and a "full-length" 160 kD (ORF1 + ORF2) protein. Both proteins co-sediment with ring canal complexes, but the ring canal localization determinants lie in the first ORF (ORF1). Transgenic kel 76kD ORF1 protein, but not 160 kD full-length protein alone, is able to rescue female fertility and ring canal morphology.

(Robinson and Cooley, 1997)

The 787aa kel protein is the second protein predicted from the bicistronic kel transcript. It has not been physically detected.

(Xue and Cooley, 1993)

One of a couple of protein products generated from a bicistronic transcript.

(FlyBase, 1992-)

External Data

Crossreferences

InterPro - A database of protein families, domains and functional sites

Linkouts

Sequences Consistent with the Gene Model

Mapped Features

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

External Data

Crossreferences

Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.

kel_1

Linkouts

Gene Ontology (12 terms)

Molecular Function (1 term)

Terms Based on Experimental Evidence (1 term)

CV Term

Evidence

References

actin binding

inferred from direct assay

(Kelso et al., 2002)

Terms Based on Predictions or Assertions (0 terms)

Biological Process (8 terms)

Terms Based on Experimental Evidence (8 terms)

CV Term

Evidence

References

actin cytoskeleton organization