Q05306 · COAA1_MOUSE
- ProteinCollagen alpha-1(X) chain
- GeneCol10a1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids680 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 626 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 627 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 633 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 634 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 634 | Ca2+ 2 (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: D |
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 | cell cortex | |
Cellular Component | collagen trimer | |
Cellular Component | collagen type X trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Cellular Component | receptor complex | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Molecular Function | metal ion binding | |
Biological Process | cartilage development | |
Biological Process | endochondral ossification | |
Biological Process | extracellular matrix organization |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-1(X) chain
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ05306
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MLPQIPFLLLMFLTLVHG | ||||||
Chain | PRO_0000005771 | 19-680 | Collagen alpha-1(X) chain | |||
Sequence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|
Post-translational modification
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homotrimer.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 19-56 | Nonhelical region (NC2) | ||||
Sequence: MFYAERYQTPTGIKGPLASPKTQYFIPYAIKSKGIPVR | ||||||
Region | 54-531 | Disordered | ||||
Sequence: PVRGEQGIPGPPGPTGPRGHPGPSGPPGKPGYGSPGLQGEPGLPGPPGISATGKPGLPGPPGKPGERGPYGHKGDIGPAGLPGPRGPPGPPGIPGPAGISVPGKPGQQGLTGAPGPRGFPGEKGAQGAPGVNGRKGETGYGSPGRPGERGLPGPQGPIGPPGPSGVGRRGENGFPGQPGIKGDRGFPGEMGPSGPPGPQGPPGKQGREGIGKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTRGPTGPPGVPGFPGSKGDPGNPGAPGPAGIATKGLNGPTGPPGPPGPRGHSGEPGLPGPPGPPGPPGQAVMPDGFIKAGQR | ||||||
Region | 57-519 | Triple-helical region | ||||
Sequence: GEQGIPGPPGPTGPRGHPGPSGPPGKPGYGSPGLQGEPGLPGPPGISATGKPGLPGPPGKPGERGPYGHKGDIGPAGLPGPRGPPGPPGIPGPAGISVPGKPGQQGLTGAPGPRGFPGEKGAQGAPGVNGRKGETGYGSPGRPGERGLPGPQGPIGPPGPSGVGRRGENGFPGQPGIKGDRGFPGEMGPSGPPGPQGPPGKQGREGIGKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTRGPTGPPGVPGFPGSKGDPGNPGAPGPAGIATKGLNGPTGPPGPPGPRGHSGEPGLPGPPGPPGPPGQA | ||||||
Compositional bias | 60-83 | Pro residues | ||||
Sequence: GIPGPPGPTGPRGHPGPSGPPGKP | ||||||
Compositional bias | 104-118 | Pro residues | ||||
Sequence: ATGKPGLPGPPGKPG | ||||||
Compositional bias | 134-151 | Pro residues | ||||
Sequence: LPGPRGPPGPPGIPGPAG | ||||||
Compositional bias | 488-519 | Pro residues | ||||
Sequence: PTGPPGPPGPRGHSGEPGLPGPPGPPGPPGQA | ||||||
Region | 520-680 | Nonhelical region (NC1) | ||||
Sequence: VMPDGFIKAGQRPRLSGMPLVSANHGVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYTYDEYSKGYLDQASGSAIMELTENDQVWLQLPNAESNGLYSSEYVHSSFSGFLVAPM | ||||||
Domain | 547-680 | C1q | ||||
Sequence: TGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYTYDEYSKGYLDQASGSAIMELTENDQVWLQLPNAESNGLYSSEYVHSSFSGFLVAPM |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length680
- Mass (Da)66,775
- Last updated1995-11-01 v1
- ChecksumFE984CA99AF708E2
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 13 | in Ref. 3; no nucleotide entry | ||||
Sequence: L → F | ||||||
Sequence conflict | 27 | in Ref. 3; no nucleotide entry | ||||
Sequence: T → S | ||||||
Compositional bias | 60-83 | Pro residues | ||||
Sequence: GIPGPPGPTGPRGHPGPSGPPGKP | ||||||
Compositional bias | 104-118 | Pro residues | ||||
Sequence: ATGKPGLPGPPGKPG | ||||||
Compositional bias | 134-151 | Pro residues | ||||
Sequence: LPGPRGPPGPPGIPGPAG | ||||||
Sequence conflict | 248 | in Ref. 3; no nucleotide entry and 4; CAA46237 | ||||
Sequence: P → L | ||||||
Sequence conflict | 286 | in Ref. 2; CAA79736 | ||||
Sequence: A → S | ||||||
Sequence conflict | 306 | in Ref. 3; no nucleotide entry and 4; CAA46237 | ||||
Sequence: L → F | ||||||
Sequence conflict | 417 | in Ref. 3; no nucleotide entry and 4; CAA46237 | ||||
Sequence: T → S | ||||||
Sequence conflict | 451 | in Ref. 5; CAA44741 | ||||
Sequence: R → K | ||||||
Compositional bias | 488-519 | Pro residues | ||||
Sequence: PTGPPGPPGPRGHSGEPGLPGPPGPPGPPGQA | ||||||
Sequence conflict | 500 | in Ref. 3; no nucleotide entry and 4; CAA46237 | ||||
Sequence: H → L | ||||||
Sequence conflict | 567-572 | in Ref. 3; no nucleotide entry and 4; CAA46237 | ||||
Sequence: APIPFD → CPHPIY | ||||||
Sequence conflict | 635 | in Ref. 3; no nucleotide entry and 4; CAA46237 | ||||
Sequence: Q → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X67348 EMBL· GenBank· DDBJ | CAA47763.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z21610 EMBL· GenBank· DDBJ | CAA79736.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X65121 EMBL· GenBank· DDBJ | CAA46237.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X63013 EMBL· GenBank· DDBJ | CAA44741.1 EMBL· GenBank· DDBJ | mRNA |