A5PN28 · OTO1A_DANRE
- ProteinOtolin-1-A
- Geneotol1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
Acts as a scaffold for biomineralization by sequestering calcium (PubMed:29076638).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | calcium ion binding | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Biological Process | extracellular matrix organization | |
Biological Process | otolith development | |
Biological Process | otolith mineralization | |
Biological Process | protein complex oligomerization |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameOtolin-1-A
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionA5PN28
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized in both the surrounding otoconial matrix and otoconia.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MPNILHPFIIIMTLLVVATGNQA | ||||||
Chain | PRO_0000332217 | 24-489 | Otolin-1-A | |||
Sequence: SIDKTTQWPRMKPTKKPPPRDEGPSKLGSISTTVSPTAIGITEEVTDAMMDAYTITSTGSTTFSSDTYSADYHTEAMVPPGVGPGNYTLDYNECFFNFCECCPPERGPPGPVGEKGLPGIPGGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDKGDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDKGDCPFGEKGQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPPGQRGMPGMKGTRGLKGARGIRGFKGFKGEPAVQKRSAFSVGLFPSRSFPPPGLPIRFDKIIYNEEAHWDPNASKFNCTHGGVYVFSYYITVRNRPLRAALVVNGIRKLRTRDSLYGQDIDQASNMAVLRLSSGDQVWLETLRDWNGVYSSSEDDSTFSGFLLYADATKD | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 225 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 287 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 391 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 396 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 27-57 | Disordered | ||||
Sequence: KTTQWPRMKPTKKPPPRDEGPSKLGSISTTV | ||||||
Region | 133-335 | Disordered | ||||
Sequence: GPVGEKGLPGIPGGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDKGDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDKGDCPFGEKGQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPPGQRGMPGMKGTRGLK | ||||||
Domain | 145-204 | Collagen-like 1 | ||||
Sequence: GGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDK | ||||||
Domain | 205-255 | Collagen-like 2 | ||||
Sequence: GDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDK | ||||||
Domain | 264-323 | Collagen-like 3 | ||||
Sequence: GQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPPGQR | ||||||
Compositional bias | 307-321 | Pro residues | ||||
Sequence: KQGEPGPPGPQGPPG | ||||||
Domain | 351-488 | C1q | ||||
Sequence: AVQKRSAFSVGLFPSRSFPPPGLPIRFDKIIYNEEAHWDPNASKFNCTHGGVYVFSYYITVRNRPLRAALVVNGIRKLRTRDSLYGQDIDQASNMAVLRLSSGDQVWLETLRDWNGVYSSSEDDSTFSGFLLYADATK |
Domain
The C1q domain mediates calcium-binding.
Sequence similarities
Belongs to the OTOL1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length489
- Mass (Da)50,792
- Last updated2007-07-10 v1
- Checksum4D41DE52604C7625
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10-11 | in Ref. 2; BAD61006 | ||||
Sequence: II → ML | ||||||
Sequence conflict | 26 | in Ref. 2; BAD61006 | ||||
Sequence: D → A | ||||||
Sequence conflict | 48 | in Ref. 2; BAD61006 | ||||
Sequence: S → P | ||||||
Sequence conflict | 70 | in Ref. 2; BAD61006 | ||||
Sequence: D → G | ||||||
Sequence conflict | 82-83 | in Ref. 2; BAD61006 | ||||
Sequence: GS → DC | ||||||
Sequence conflict | 118 | in Ref. 2; BAD61006 | ||||
Sequence: F → L | ||||||
Sequence conflict | 167 | in Ref. 2; BAD61006 | ||||
Sequence: T → P | ||||||
Sequence conflict | 185 | in Ref. 2; BAD61006 | ||||
Sequence: I → F | ||||||
Compositional bias | 307-321 | Pro residues | ||||
Sequence: KQGEPGPPGPQGPPG | ||||||
Sequence conflict | 315 | in Ref. 2; BAD61006 | ||||
Sequence: G → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX927289 EMBL· GenBank· DDBJ | CAN88052.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB124554 EMBL· GenBank· DDBJ | BAD61006.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |