Q9VW71 · FAT2_DROME

Function

function

Required for the planar polarity of actin filament orientation at the basal side of ovarian follicle cells (PubMed:19906848, PubMed:23369713).
Required for proper egg chamber shape and elongation of the egg chamber during oogenesis (PubMed:19906848, PubMed:23369713).
Required for the correct planar polarization of Rab10 within the basal follicle cell epithelium and is therefore indirectly involved in the Rab10-dependent remodeling of the basal membrane during egg chamber elongation (PubMed:23369713).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentactin-based cell projection
Cellular Componentbasal plasma membrane
Cellular Componentcell trailing edge
Cellular Componentfocal adhesion
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Molecular Functioncell adhesion molecule binding
Molecular Functionprotein-containing complex binding
Biological Processcalcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules
Biological Processcell-cell adhesion
Biological Processcell-cell adhesion mediated by cadherin
Biological Processcentripetally migrating follicle cell migration
Biological Processdefense response to Gram-negative bacterium
Biological Processestablishment of planar polarity of follicular epithelium
Biological Processestablishment or maintenance of actin cytoskeleton polarity
Biological Processforegut morphogenesis
Biological Processgrowth of a germarium-derived egg chamber
Biological Processhindgut morphogenesis
Biological Processhomophilic cell adhesion via plasma membrane adhesion molecules
Biological Processoogenesis
Biological Processopen tracheal system development
Biological Processpositive regulation of filopodium assembly
Biological Processpositive regulation of innate immune response
Biological Processprotein localization to cell leading edge
Biological Processsalivary gland development

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Fat-like cadherin-related tumor suppressor homolog
  • Alternative names
    • Protein kugelei

Gene names

    • Name
      kug
    • Synonyms
      fat2
    • ORF names
      CG7749

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VW71
  • Secondary accessions
    • A4V252
    • Q95S51

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane ; Single-pass type I membrane protein
Note: Accumulates on cell membranes where the planar oriented actin filaments terminate.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain39-4285Extracellular
Transmembrane4286-4306Helical
Topological domain4307-4699Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Defects in actin filament orientation correlate with a failure of egg chambers to elongate during oogenesis (PubMed:19906848).
In follicle cells, Rab10 protein polarizes normally along the apical-basal axis, but is mislocalized within the epithelial plane (PubMed:23369713).
Epithelia migration is impaired and the structure of the basal membrane is disrupted (PubMed:23369713).

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-38
ChainPRO_000000401639-4699
Glycosylation68N-linked (GlcNAc...) asparagine
Glycosylation159N-linked (GlcNAc...) asparagine
Glycosylation367N-linked (GlcNAc...) asparagine
Glycosylation782N-linked (GlcNAc...) asparagine
Glycosylation846N-linked (GlcNAc...) asparagine
Glycosylation926N-linked (GlcNAc...) asparagine
Glycosylation1109N-linked (GlcNAc...) asparagine
Glycosylation1201N-linked (GlcNAc...) asparagine
Glycosylation1315N-linked (GlcNAc...) asparagine
Glycosylation1442N-linked (GlcNAc...) asparagine
Glycosylation1476N-linked (GlcNAc...) asparagine
Glycosylation1514N-linked (GlcNAc...) asparagine
Disulfide bond3807↔3819
Disulfide bond3814↔3851
Disulfide bond3853↔3862
Disulfide bond3869↔3880
Disulfide bond3874↔3891
Disulfide bond3893↔3902
Disulfide bond4071↔4105
Disulfide bond4117↔4128
Disulfide bond4122↔4138
Disulfide bond4140↔4149
Disulfide bond4156↔4167
Disulfide bond4161↔4177
Disulfide bond4179↔4188
Disulfide bond4194↔4205
Disulfide bond4199↔4214
Disulfide bond4216↔4224
Disulfide bond4231↔4242
Disulfide bond4236↔4251
Disulfide bond4253↔4262

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Localizes where basal actin filaments terminate.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain63-183Cadherin 1
Domain184-291Cadherin 2
Domain288-400Cadherin 3
Domain401-507Cadherin 4
Domain508-613Cadherin 5
Domain614-716Cadherin 6
Domain773-877Cadherin 7
Domain878-980Cadherin 8
Domain981-1088Cadherin 9
Domain1089-1198Cadherin 10
Domain1194-1299Cadherin 11
Domain1300-1405Cadherin 12
Domain1408-1506Cadherin 13
Domain1507-1612Cadherin 14
Domain1613-1717Cadherin 15
Domain1718-1815Cadherin 16
Domain1816-1932Cadherin 17
Domain1933-2033Cadherin 18
Domain2034-2140Cadherin 19
Domain2141-2241Cadherin 20
Domain2242-2341Cadherin 21
Domain2342-2449Cadherin 22
Domain2450-2551Cadherin 23
Domain2552-2654Cadherin 24
Domain2655-2763Cadherin 25
Domain2764-2860Cadherin 26
Domain2861-2967Cadherin 27
Domain2968-3072Cadherin 28
Domain3068-3169Cadherin 29
Domain3170-3273Cadherin 30
Domain3274-3378Cadherin 31
Domain3379-3483Cadherin 32
Domain3484-3588Cadherin 33
Domain3589-3696Cadherin 34
Domain3865-3903EGF-like 1
Domain3921-4105Laminin G-like
Domain4113-4150EGF-like 2
Domain4152-4189EGF-like 3
Domain4190-4225EGF-like 4
Domain4227-4263EGF-like 5

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q9VW71-1

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.

  • Length
    4,699
  • Mass (Da)
    523,781
  • Last updated
    2014-05-14 v3
  • Checksum
    1798A54345758C36

Q9VW71-2

  • Name
    C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
X2JCN4X2JCN4_DROMEkug4689

Sequence caution

The sequence AAL28503.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAM50035.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAM50035.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict3946in Ref. 3; AAL28503
Alternative sequenceVSP_0544504601-4611in isoform C

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014296
EMBL· GenBank· DDBJ
AAF49078.3
EMBL· GenBank· DDBJ
Genomic DNA
AE014296
EMBL· GenBank· DDBJ
AAZ66056.2
EMBL· GenBank· DDBJ
Genomic DNA
AY060955
EMBL· GenBank· DDBJ
AAL28503.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AY118666
EMBL· GenBank· DDBJ
AAM50035.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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