Q9VZ21 · RTRV_DROME

Function

function

Required for chitin fiber assembly and organization involved in cuticle formation and tracheal development.

Miscellaneous

The name 'retroactive' likely refers to the propensity of hyperactive larvae to change orientation within the egg case.

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 Componentplasma membrane
Cellular Componentside of membrane
Biological Processchitin-based embryonic cuticle biosynthetic process
Biological Processopen tracheal system development
Biological Processpositive regulation of voltage-gated potassium channel activity
Biological Processregulation of synaptic transmission, cholinergic
Biological Processregulation of tube architecture, open tracheal system
Biological Processregulation of tube diameter, open tracheal system
Biological Processsleep

Names & Taxonomy

Protein names

  • Recommended name
    UPAR/Ly6 domain-containing protein rtv
  • Alternative names
    • Protein retroactive

Gene names

    • Name
      rtv
    • Synonyms
      l(1)L1
    • ORF names
      CG1397

Organism names

  • Taxonomic identifier
  • Strains
    • ZBMEL377
    • ZBMEL384
    • ZBMEL398
    • MEL01
    • MEL02
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VZ21
  • Secondary accessions
    • M9PJI2

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Lipid-anchor, GPI-anchor

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain20-125Extracellular
Transmembrane126-146Helical
Topological domain147-151Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Larval lethal as larvae are unable to hatch (PubMed:15844167).
Larvae are hyperactive and occasionally change orientation in the egg case (PubMed:15844167).
Tissues that produce a chitin cuticle, such as the skull and the trachea, fail to form properly (PubMed:15844167, PubMed:16339194).
Disorganization of chitin fibers in the cuticle and in the trachea (PubMed:15844167, PubMed:16339194, PubMed:19502482).
Elongated and convoluted tracheal dorsal trunk with tracheal lumen expansion defects in stage 14 to 16 embryos, possibly due to uncoordinated apical cell surface expansion (PubMed:16339194, PubMed:19502482).
Detachment of the cuticle from the underlying epidermis allowing it to expand giving a bloated phenotype (PubMed:15844167).

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-19
ChainPRO_501502017820-121UPAR/Ly6 domain-containing protein rtv
Disulfide bond26↔65
Disulfide bond29↔38
Glycosylation45N-linked (GlcNAc...) asparagine
Disulfide bond60↔88
Disulfide bond100↔113
Disulfide bond115↔120
Lipidation121GPI-anchor amidated asparagine
PropeptidePRO_0000459700122-151Removed in mature form

Keywords

Proteomic databases

PTM databases

Expression

Developmental stage

Expression coincides with formation of the procuticle in the developing head skeleton, pharynx and trachea at stage 16 and 17 of embryogenesis, and in epidermal cells at stage 17.

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the quiver family.

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.

Q9VZ21-1

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.

  • Name
    A
  • Synonyms
    B
    , D
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    151
  • Mass (Da)
    16,843
  • Last updated
    2000-05-01 v1
  • Checksum
    06D78037E46FC8B1
MQFTSLLLAVIFLISLVSIDGLLRRCYQCRSRGELGSCKDPFTFNATDVEQEPGVAAIPCASGWCGKVIEGGGTYAIDDYDLAIQRMCVQRGPDDNMDRCADTIYNYKKVYMCFCQGDLCNGARSWSSAPQMILITMLPLLGSWLLQRMRN

Q9VZ21-2

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

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0622391-86in isoform C

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM999233
EMBL· GenBank· DDBJ
CAQ53595.1
EMBL· GenBank· DDBJ
Genomic DNA
AM999234
EMBL· GenBank· DDBJ
CAQ53596.1
EMBL· GenBank· DDBJ
Genomic DNA
AM999235
EMBL· GenBank· DDBJ
CAQ53597.1
EMBL· GenBank· DDBJ
Genomic DNA
FM246338
EMBL· GenBank· DDBJ
CAR94264.1
EMBL· GenBank· DDBJ
Genomic DNA
FM246339
EMBL· GenBank· DDBJ
CAR94265.1
EMBL· GenBank· DDBJ
Genomic DNA
FM246340
EMBL· GenBank· DDBJ
CAR94266.1
EMBL· GenBank· DDBJ
Genomic DNA
FM246341
EMBL· GenBank· DDBJ
CAR94267.1
EMBL· GenBank· DDBJ
Genomic DNA
FM246343
EMBL· GenBank· DDBJ
CAR94269.1
EMBL· GenBank· DDBJ
Genomic DNA
FM246344
EMBL· GenBank· DDBJ
CAR94270.1
EMBL· GenBank· DDBJ
Genomic DNA
FM246345
EMBL· GenBank· DDBJ
CAR94271.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAF48010.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AGB95285.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AGB95286.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AHN59584.1
EMBL· GenBank· DDBJ
Genomic DNA
AY061126
EMBL· GenBank· DDBJ
AAL28674.1
EMBL· GenBank· DDBJ
mRNA
KX531353
EMBL· GenBank· DDBJ
ANY27163.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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