Q9VB46 · APMAP_DROME

Function

function

Transmembrane mucin that may be involved in cellular adhesion and the innate immune response (PubMed:12769978, PubMed:8662683).
Membrane-tethered mucins are involved in many cell surface functions and form a physical barrier around cells to regulate cell-cell and/or cell-substrate interactions, and protect against pathogens or harmful extracellular conditions (PubMed:11164341, PubMed:12769978, PubMed:8662683).
This mucin likely acts in hemocyte adhesion as it is released from hemocytes during coagulation and is also able to bind lipophorin particles which form part of the hemocyte coagulogen (PubMed:12769978).
Able to induce expression of the antibacterial proteins in the presence of GalNAc-specific lectins and so probably also functions in the innate immune response (PubMed:8662683).

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 surface
Cellular Componentendomembrane system
Cellular Componentplasma membrane
Molecular Functionarylesterase activity
Molecular Functionhydrolase activity
Molecular Functionstrictosidine synthase activity
Biological Processbiosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Adipocyte plasma membrane-associated protein Hemomucin
  • Alternative names
    • Protein Hemomucin

Gene names

    • Name
      Hmu
    • Synonyms
      Rbp5
      , rrm5
      , SPH210
    • ORF names
      CG3373

Organism names

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

Accessions

  • Primary accession
    Q9VB46
  • Secondary accessions
    • D2NUG9
    • Q24160
    • Q8MT56

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass membrane protein
Note: Detected on membrane of hemocytes.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-6Cytoplasmic
Transmembrane7-29Helical
Topological domain30-579Extracellular

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004542301-579Adipocyte plasma membrane-associated protein Hemomucin
Glycosylation213N-linked (GlcNAc...) asparagine
Glycosylation217N-linked (GlcNAc...) asparagine

Post-translational modification

O-glycosylated. Glycosylated in the ovary of 4 day old females.
Phosphorylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in ovaries (at protein level) (PubMed:11164341).
In larvae, detected in the fat body, salivary glands, imaginal disks and gut (at protein level) (PubMed:11164341).
In adults, expressed in the cardia, and in regions of the ventriculus including the area posterior to the cardia (PubMed:8662683).
In females also expressed in follicle cells (PubMed:8662683).

Induction

By ecdysone; in embryonic cell lines.

Developmental stage

Detected throughout development and in adults (at protein level) (PubMed:11164341).
Expressed in embryos, larvae and adults (PubMed:8662683).

Gene expression databases

Interaction

Subunit

Interacts with sturkopf.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region427-579Disordered
Compositional bias443-525Polar residues
Compositional bias539-571Basic and acidic residues

Sequence similarities

Belongs to the strictosidine synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    579
  • Mass (Da)
    63,416
  • Last updated
    2000-05-01 v1
  • Checksum
    7584B7C08D31490B
MGLLYALRVRIMNFMIFFLLIILMPGLPPRTTFPFKDYIVTPPKDLKGALESNFHLEGAERLLEGRVYGPECLIARNNEIYTGIHGGEVIKLTSNHVTHVTKIGQPCEDIYEESRCGRPLGLAFDTQGNNLIIADAYYGLWQVDLGTNKKTLLVSPAQELAGKSINRPAKIFNGVTVSKEGDVYWTDSSSDFTIEDLVFASFANPSGRLFKYNRSKNVSEVLLDELAFANGLALSPNEDFIVVAETGAMRLTKYHLKGAKAGQSEVFVDGLPGLPDNLTPDAEGIWVPLVQSADSEHPNGFTLFTRFPSVRLFLARMLALFELPFRYLNSVYPNKFSQRFVHFVGHMESITVLAPKRTTVVRVDWNGNIVGSLHGFDKSAATVSHVLEFQDFLFLGSPTNQYLARVKSPKAKQPTLKVRNVRVEGEGLEASIGVPPSKATPKPKAAPSTTTPKPTTTTTTTTPKPTTKTTTTTTTPKPTTTTTTKKPTTTTTTTTTTPKPTTTKPPTAKPSTTTTTTTTPKPTTTTTPTTPTPEPSKPKVKRTVPEKPAPVEEDIPSDTQPPKKEKLKVINKQGVNVEL

Sequence caution

The sequence ADB25328.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict207in Ref. 5; ADB25328
Sequence conflict255in Ref. 4; AAM48401
Sequence conflict341in Ref. 1; AAC47118
Sequence conflict383in Ref. 1; AAC47118
Sequence conflict387in Ref. 5; ADB25328
Compositional bias443-525Polar residues
Sequence conflict516in Ref. 1; AAC47118
Sequence conflict532in Ref. 1; AAC47118
Compositional bias539-571Basic and acidic residues
Sequence conflict554in Ref. 1; AAC47118

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U42014
EMBL· GenBank· DDBJ
AAC47118.1
EMBL· GenBank· DDBJ
mRNA
AE014297
EMBL· GenBank· DDBJ
AAF56697.1
EMBL· GenBank· DDBJ
Genomic DNA
AY118372
EMBL· GenBank· DDBJ
AAM48401.1
EMBL· GenBank· DDBJ
mRNA
BT120112
EMBL· GenBank· DDBJ
ADB25328.1
EMBL· GenBank· DDBJ
mRNA Frameshift
BT133185
EMBL· GenBank· DDBJ
AFA28426.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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