A5PN28 · OTO1A_DANRE

Function

function

Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear (PubMed:15905077, PubMed:29076638).
Acts as a scaffold for biomineralization by sequestering calcium (PubMed:29076638).

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 Componentcollagen trimer
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Molecular Functionextracellular matrix structural constituent conferring tensile strength
Biological Processextracellular matrix organization
Biological Processotolith development
Biological Processotolith mineralization
Biological Processprotein complex oligomerization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Otolin-1-A
  • Alternative names
    • zOtolin1

Gene names

    • Name
      otol1a
    • Synonyms
      otol1
    • ORF names
      si:dkey-119f1.2

Organism names

  • Taxonomic identifier
  • Strain
    • Tuebingen
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    A5PN28
  • Secondary accessions
    • Q60HI2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000033221724-489Otolin-1-A
Glycosylation109N-linked (GlcNAc...) asparagine
Glycosylation225N-linked (GlcNAc...) asparagine
Glycosylation287N-linked (GlcNAc...) asparagine
Glycosylation391N-linked (GlcNAc...) asparagine
Glycosylation396N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homooligomer; disulfide-linked; probably forms homotrimers (PubMed:29076638).
Interacts with otomp (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region27-57Disordered
Region133-335Disordered
Domain145-204Collagen-like 1
Domain205-255Collagen-like 2
Domain264-323Collagen-like 3
Compositional bias307-321Pro residues
Domain351-488C1q

Domain

The C1q domain mediates calcium-binding.

Sequence similarities

Belongs to the OTOL1 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
    489
  • Mass (Da)
    50,792
  • Last updated
    2007-07-10 v1
  • Checksum
    4D41DE52604C7625
MPNILHPFIIIMTLLVVATGNQASIDKTTQWPRMKPTKKPPPRDEGPSKLGSISTTVSPTAIGITEEVTDAMMDAYTITSTGSTTFSSDTYSADYHTEAMVPPGVGPGNYTLDYNECFFNFCECCPPERGPPGPVGEKGLPGIPGGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDKGDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDKGDCPFGEKGQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPPGQRGMPGMKGTRGLKGARGIRGFKGFKGEPAVQKRSAFSVGLFPSRSFPPPGLPIRFDKIIYNEEAHWDPNASKFNCTHGGVYVFSYYITVRNRPLRAALVVNGIRKLRTRDSLYGQDIDQASNMAVLRLSSGDQVWLETLRDWNGVYSSSEDDSTFSGFLLYADATKD

Sequence caution

The sequence BAD61006.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict10-11in Ref. 2; BAD61006
Sequence conflict26in Ref. 2; BAD61006
Sequence conflict48in Ref. 2; BAD61006
Sequence conflict70in Ref. 2; BAD61006
Sequence conflict82-83in Ref. 2; BAD61006
Sequence conflict118in Ref. 2; BAD61006
Sequence conflict167in Ref. 2; BAD61006
Sequence conflict185in Ref. 2; BAD61006
Compositional bias307-321Pro residues
Sequence conflict315in Ref. 2; BAD61006

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX927289
EMBL· GenBank· DDBJ
CAN88052.1
EMBL· GenBank· DDBJ
Genomic DNA
AB124554
EMBL· GenBank· DDBJ
BAD61006.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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