Q0E908 · HIL_DROME

Function

function

May act as a modulator of septin function during cytokinesis in the developing nervous system.

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 Componentcell cortex
Cellular Componentcleavage furrow
Molecular Functionmetal ion binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Hillarin
  • Alternative names
    • D-Hillarin
      (D-hil
      )

Gene names

    • Name
      Hil
    • ORF names
      CG30147

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
    Q0E908
  • Secondary accessions
    • Q960G2

Proteomes

Organism-specific databases

Subcellular Location

Cleavage furrow
Note: During mitosis, detected at the cell cortex in metaphase but is concentrated at the cleavage furrow at telophase. Colocalizes with pnut at the cell cortex.

Keywords

Phenotypes & Variants

Disruption phenotype

Mutants are viable with a 98.4% hatch rate which is close to the wild-type hatch rate. No apparent defects in the central nervous system.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004371381-818Hillarin

Proteomic databases

Expression

Tissue specificity

Localizes to the neuropil of the embryonic central nervous system (at protein level). Also detected in third instar larval brain (at protein level).

Developmental stage

Very low levels detected in 0-6 hour embryos with expression up-regulated after 12 hours of embryogenesis and persisting into adult stages (at protein level).

Gene expression databases

Interaction

Subunit

Interacts with pnut.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias, coiled coil.

Type
IDPosition(s)Description
Domain9-76LIM zinc-binding
Region97-141Disordered
Compositional bias114-141Polar residues
Coiled coil216-272

Sequence similarities

Belongs to the transglutaminase-like superfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    818
  • Mass (Da)
    94,465
  • Last updated
    2006-10-17 v1
  • Checksum
    4833D507336884F7
MYRPNFYESTCLRCSETVYQVDRVGPLKDFTFFHSGCFKCVHCGTKLTLKTYFNNQHKQDDKEVYCSSHVPKSGPGHLDQTSVGIRQALNAPRTNKFVNEQIRGTRSEVDGGPLGGSRQSTPNGYGSREISSPSQNDSDYKYGRFDASALHIAHALKQTEIQKAYNKAREKPIDFYLAREEQAHLEMKHRKEEDDLYRKFASKRAEEDRKIQDEFQDEWERELQRLTHKFEKELATSRRSRDEANILTMRHEQQKEDLEKNMTLRRSKKKESITRKMLEHERYETAALVDRQSSEMLELISARRSEYMQSESIFLDDEFSEGAVPVEYPLNAPIPAPPAVSKFQIYTDPIEFEDVDRIAISVAQEDQKTFTDLVRQLVGRCTTDIEKARTIFRWITVKNLNAMHFDDDLRGDTPMGLLRGIKYGTESYHVLFKRLCSYAGLHCVVIKGYSKSAGYQPGVKFQDSRFRNSWNAVYVAGAWRFVQCNWGARHLVNAKEAPKQGRGKNDSLRYEYDDHYFLTDPREFIYEFYPLQEEWQLLKRPITLREFENLPFVRSLFFRYGLHFADEGYGAVVFTDDTGAATVRIAMPTDMQSCLIFHYNLKFYDSDEELSYDGVSLKRFVMQSVIGNIVAFRVHAPCSGAFLLDIFANAVTPQEYLTGEPMKFKSVCKFKICCEELQTVMVPLPDCASGEWGPTKATRLFGLIPITHQDPLIFAGRSLDLQFRMSRPLTDFMATLHKNGIEEKKLAKYVTHSTLDDIVTFIINFPEEGQYGLDIYTRELGGPQHHHHHNNNNSSSSSGEKHLLTHCCKYLINSSKRN

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias114-141Polar residues
Sequence conflict788in Ref. 3; AAK93501
Sequence conflict794in Ref. 3; AAK93501

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE013599
EMBL· GenBank· DDBJ
AAF57448.2
EMBL· GenBank· DDBJ
Genomic DNA
AE013599
EMBL· GenBank· DDBJ
AAF57449.2
EMBL· GenBank· DDBJ
Genomic DNA
AY052077
EMBL· GenBank· DDBJ
AAK93501.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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