Reviewed,
UniProtKB/Swiss-Prot P0C2W2 (CO1A1_TYREX)
Last modified
January 19, 2010.
Version 12.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Collagen alpha-1(I) chain Alternative name(s): Alpha-1 type I collagen | ||
| Gene names |
| ||
| Organism | Tyrannosaurus rex (Tyrant lizard king) | ||
| Taxonomic identifier | 436495 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Tyrannosauridae › Tyrannosaurus |
Protein attributes
| Sequence length | 570 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Type I collagen is a member of group I collagen (fibrillar forming collagen). |
| Subunit structure | Trimers of one alpha 2(I) and two alpha 1(I) chains. |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Post-translational modification | Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. |
| Miscellaneous | These protein fragments where extracted from a 68 million years old fossil. The tryptic peptides required multiple purification steps in order to eliminate contaminants and to increase the concentration of peptidic material. |
| Sequence similarities | Belongs to the fibrillar collagen family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Domain | Collagen Repeat |
| PTM | Hydroxylation |
| Technical term | Direct protein sequencing Extinct organism protein |
| Gene Ontology (GO) | |
| Cellular component | proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›570 | ›570 | Collagen alpha-1(I) chain | PRO_0000286177 | |||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | 4-hydroxyproline Ref.1 | ||||||
| Modified residue | 12 | 1 | 4-hydroxyproline Ref.1 | ||||||
| Modified residue | 15 | 1 | 4-hydroxyproline Ref.1 | ||||||
| Modified residue | 30 | 1 | 4-hydroxyproline Ref.1 | ||||||
| Modified residue | 294 | 1 | 4-hydroxyproline Ref.1 | ||||||
| Modified residue | 474 | 1 | 4-hydroxyproline Ref.1 | ||||||
| Modified residue | 480 | 1 | 4-hydroxyproline Ref.1 | ||||||
| Modified residue | 567 | 1 | 4-hydroxyproline Ref.1 | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 570 | 1 | |||||||
Sequences
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References
| [1] | "Protein sequences from Mastodon and Tyrannosaurus rex revealed by mass spectrometry." Asara J.M., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C. Science 316:280-285(2007) [PubMed: 17431180] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, HYDROXYLATION AT PRO-6; PRO-12; PRO-15; PRO-30; PRO-294; PRO-474; PRO-480 AND PRO-567. Tissue: Bone. |
| [2] | Asara J.M. Submitted (SEP-2007) to UniProtKB Cited for: SEQUENCE REVISION TO 27 AND 470. Tissue: Bone. |
| [3] | "Interpreting sequences from mastodon and T. rex." Asara J.M., Garavelli J.S., Slatter D.A., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C. Science 317:1324-1325(2007) [PubMed: 17823333] [Abstract] Cited for: COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES. |
Cross-references
Entry information
| Entry name | CO1A1_TYREX | ||||||||
| Accession | Primary (citable) accession number: P0C2W2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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