A0A060XQP6 · OMM64_ONCMY

Function

function

Calcium-binding component of otoliths, a calcium carbonate structure of the inner ear involved in hearing and balance sensing (PubMed:18410381).
Binds calcium (PubMed:18410381, PubMed:28866388).

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 Componentextracellular region

Names & Taxonomy

Protein names

  • Recommended name
    Otolith matrix protein OMM-64
  • Alternative names
    • Otolith matrix macromolecule-64
      (OMM-64
      )

Gene names

    • ORF names
      GSONMT00017137001

Organism names

Accessions

  • Primary accession
    A0A060XQP6
  • Secondary accessions
    • B1Q2L9

Proteomes

Subcellular Location

Note: Accumulates in the ring-like structures of otoliths.

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_500159126421-628Otolith matrix protein OMM-64
Glycosylation318N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

Expression

Tissue specificity

Specifically expressed in otolith matrix-producing cells.

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region43-628Disordered
Compositional bias79-111Polar residues
Compositional bias149-176Basic and acidic residues
Compositional bias177-216Polar residues
Compositional bias235-249Acidic residues
Compositional bias250-264Basic and acidic residues
Compositional bias273-366Basic and acidic residues
Compositional bias388-451Basic and acidic residues
Compositional bias460-475Basic and acidic residues
Compositional bias489-518Basic and acidic residues
Compositional bias519-534Acidic residues
Compositional bias554-568Basic and acidic residues

Domain

The Asp/Glu-rich (acidic) region mediates binding to calcium.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    628
  • Mass (Da)
    66,567
  • Last updated
    2014-09-03 v1
  • Checksum
    9487E9C6E1E5CA20
MLSRLLIVPLIFALAGLAISAPVNDGTEADNDERAASLLVHLKGDKDGGGLTGSPDGVSAGTTDGTDSSKELAGGAVDSSPDTTDTPDASSSDIFPDTNNRDTSVETTGNPDDSDAPDAAESAGSQDTTDAADASEAVAETVDTYDIPDTDGADDREKVSTEVSTEDLDSAGVDKSPESDSTESPGSDSAESPGSDSAESPGSDSTESPGSDSTESPRSDSTDEVLTDVQADSADVTSDDMDEATETDKDDDKSDDKSDADAATDKDDSDEDKDTELDGKAHAEDTQTEEAADSDSKQGAADSDSDTDDDRPEKDVKNDSDDSKDTTEDDKPDKDDKKNRDSADNSNDDSDEMIQVPREELEQQEINLKEGGVIGSQEETVASDMEEGSDVGDQKPGPEDSIEEGSPVGRQDFKHPQDSEEEELEKEAKKEKELEEAEEERTLKTIESDSQEDSVDESEAEPDSNSKKDIGTSDAPEPQEDDSEEDTDDSMMKEPKDSDDAESDKDDKDKNDMDKEDMDKDDMDKDDMDKDDMDKDDVDKDASDSVDDQSESDAEPGADSHTVVDEIDGEETMTPDSEEIMKSGEMDSVVEATEVPADILDQPDQQDDMTQGASQAADAAATALAAQS

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict44in Ref. 1; BAG14384
Compositional bias79-111Polar residues
Compositional bias149-176Basic and acidic residues
Sequence conflict166in Ref. 1; BAG14384
Compositional bias177-216Polar residues
Compositional bias235-249Acidic residues
Compositional bias250-264Basic and acidic residues
Compositional bias273-366Basic and acidic residues
Sequence conflict369in Ref. 1; BAG14384
Compositional bias388-451Basic and acidic residues
Compositional bias460-475Basic and acidic residues
Compositional bias489-518Basic and acidic residues
Compositional bias519-534Acidic residues
Compositional bias554-568Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB213022
EMBL· GenBank· DDBJ
BAG14384.1
EMBL· GenBank· DDBJ
mRNA
FR905797
EMBL· GenBank· DDBJ
CDQ81607.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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