UniProtKB - P0C2W2 (CO1A1_TYREX)
Protein
Collagen alpha-1(I) chain
Gene
COL1A1
Organism
Tyrannosaurus rex (Tyrant lizard king)
Status
Functioni
Type I collagen is a member of group I collagen (fibrillar forming collagen).
Miscellaneous
These protein fragments where extracted from a 68-million-year-old fossil. The tryptic peptides required multiple purification steps in order to eliminate contaminants and to increase the concentration of peptidic material.
Names & Taxonomyi
Protein namesi | Recommended name: Collagen alpha-1(I) chainAlternative name(s): Alpha-1 type I collagen |
Gene namesi | Name:COL1A1 |
Organismi | Tyrannosaurus rex (Tyrant lizard king) |
Taxonomic identifieri | 436495 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Tyrannosauridae › Tyrannosaurus |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-KW
Other locations
- collagen trimer Source: UniProtKB-KW
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000286177 | ‹1 – ›570 | Collagen alpha-1(I) chainAdd BLAST | ›570 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 6 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 12 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 15 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 30 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 294 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 474 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 480 | 4-hydroxyproline1 Publication | 1 | |
Modified residuei | 567 | 4-hydroxyproline1 Publication | 1 |
Post-translational modificationi
Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication
Keywords - PTMi
HydroxylationProteomic databases
PRIDEi | P0C2W2 |
Interactioni
Subunit structurei
Trimers of one alpha 2(I) and two alpha 1(I) chains.
Family & Domainsi
Sequence similaritiesi
Belongs to the fibrillar collagen family.Curated
Keywords - Domaini
Collagen, Repeati Sequence
Sequence statusi: Fragments.
P0C2W2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
GATGAPGIAG APGFPGARGA PGPQGPSGAP GPKXXXXXXX XXXXXXXXXX
60 70 80 90 100
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
110 120 130 140 150
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
160 170 180 190 200
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
210 220 230 240 250
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
260 270 280 290 300
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGV QGPPGPQGPR
310 320 330 340 350
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
360 370 380 390 400
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
410 420 430 440 450
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
460 470 480 490 500
XXXXXXXXXX XXXXXXXXGS AGPPGATGFP GAAGRXXXXX XXXXXXXXXX
510 520 530 540 550
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
560 570
XXXXXXXXXX XGVVGLPGQR
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 1 | 1 | ||
Non-terminal residuei | 570 | 1 |
Cross-referencesi
3D structure databases
ModBasei | Search... |
Proteomic databases
PRIDEi | P0C2W2 |
Family and domain databases
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CO1A1_TYREX | |
Accessioni | P0C2W2Primary (citable) accession number: P0C2W2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 2007 |
Last sequence update: | November 13, 2007 | |
Last modified: | December 11, 2019 | |
This is version 28 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Extinct organism proteinDocuments
- SIMILARITY comments
Index of protein domains and families