Reviewed,
UniProtKB/Swiss-Prot P0C2W3 (CO2A1_TYREX)
Last modified
June 16, 2009.
Version 10.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Collagen alpha-1(II) chain Alternative name(s): Alpha-1 type II 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 | 14 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. |
| Subunit structure | Homotrimers of alpha 1(II) chains. |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| 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. |
| 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. Contains 1 VWFC domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Domain | Collagen Repeat |
| Technical term | Direct protein sequencing Extinct organism protein |
| Gene Ontology (GO) | |
| Cellular component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrixInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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. Tissue: Bone. |
| [2] | "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 | CO2A1_TYREX | ||||||||
| Accession | Primary (citable) accession number: P0C2W3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


