Q9VGH1 · CP315_DROME

Function

function

Required for CNS development: midline glial cells. Involved in the metabolism of insect hormones: responsible for ecdysteroid C2-hydroxylase activity. May be involved in the breakdown of synthetic insecticides.

Miscellaneous

Member of the Halloween gene group.

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Steroid biosynthesis; ecdysteroid biosynthesis.

Features

Showing features for binding site.

152050100150200250300350400450500
TypeIDPosition(s)Description
Binding site466Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

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 Componentmitochondrial membrane
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Functionecdysteroid 2-hydroxylase activity
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Biological Processcentral nervous system development
Biological Processdorsal closure
Biological Processecdysone biosynthetic process
Biological Processhead involution
Biological Processmidgut development
Biological Processmotor neuron axon guidance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome P450 315a1, mitochondrial
  • EC number
  • Alternative names
    • CYPCCCXVA1
    • Protein shadow

Gene names

    • Name
      sad
    • Synonyms
      Cyp315a1
    • ORF names
      CG14728

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
    Q9VGH1
  • Secondary accessions
    • Q5U131
    • Q8MTR7

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, transit peptide.

TypeIDPosition(s)Description
ChainPRO_0000003631?-520Cytochrome P450 315a1, mitochondrial
Transit peptide1-?Mitochondrion

Proteomic databases

Expression

Tissue specificity

Complex coexpression pattern of dib (disembodied) and sad (shade) in the early embryo that restricts to the prothoracic gland cells of the developing ring gland during late embryogenesis. In larvae and adult, coexpression is seen in prothoracic gland and follicle cells of the ovary. In adults, coexpression is seen in the follicle cells, sad only is expressed in nurse cells.

Gene expression databases

    • FBgn0003312Expressed in prothoracic gland (Drosophila) and 9 other cell types or tissues

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    520
  • Mass (Da)
    59,631
  • Last updated
    2000-05-01 v1
  • Checksum
    6DC4A2CCD8E07BC6
MTEKRERPGPLRWLRHLLDQLLVRILSLSLFRSRCDPPPLQRFPATELPPAVAAKYVPIPRVKGLPVVGTLVDLIAAGGATHLHKYIDARHKQYGPIFRERLGGTQDAVFVSSANLMRGVFQHEGQYPQHPLPDAWTLYNQQHACQRGLFFMEGAEWLHNRRILNRLLLNGNLNWMDVHIESCTRRMVDQWKRRTAEAAAIPLAESGEIRSYELPLLEQQLYRWSIEVLCCIMFGTSVLTCPKIQSSLDYFTQIVHKVFEHSSRLMTFPPRLAQILRLPIWRDFEANVDEVLREGAAIIDHCIRVQEDQRRPHDEALYHRLQAADVPGDMIKRIFVDLVIAAGDTTAFSSQWALFALSKEPRLQQRLAKERATNDSRLMHGLIKESLRLYPVAPFIGRYLPQDAQLGGHFIEKDTMVLLSLYTAGRDPSHFEQPERVLPERWCIGETEQVHKSHGSLPFAIGQRSCIGRRVALKQLHSLLGRCAAQFEMSCLNEMPVDSVLRMVTVPDRTLRLALRPRTE

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict484in Ref. 1; AAL86019
Sequence conflict509in Ref. 1; AAL86019

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY079170
EMBL· GenBank· DDBJ
AAL86019.1
EMBL· GenBank· DDBJ
mRNA
AE014297
EMBL· GenBank· DDBJ
AAF54711.1
EMBL· GenBank· DDBJ
Genomic DNA
BT016061
EMBL· GenBank· DDBJ
AAV36946.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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