Collagen alpha-1(I) chain - Tyrannosaurus rex (Tyrant lizard king)

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Reviewed, UniProtKB/Swiss-Prot P0C2W2 (CO1A1_TYREX)

Last modified July 22, 2008. Version 6. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen

Gene names

Name:

COL1A1

Organism

Tyrannosaurus rex (Tyrant lizard king)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Tyrannosauridae › Tyrannosaurus

Protein attributes

Sequence length	570 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrixBy 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 By similarity.
Miscellaneous	These protein fragments where extracted from a 68 millions 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
Molecular function	Structural protein
PTM	Hydroxylation
Technical term	Direct protein sequencing Extinct organism protein
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

‹1 – ›570

›570

Collagen alpha-1(I) chain

Amino acid modifications

Modified residue

1

4-hydroxyproline

Modified residue

1

4-hydroxyproline

Modified residue

1

4-hydroxyproline

Modified residue

1

4-hydroxyproline

Modified residue

1

4-hydroxyproline

Modified residue

1

4-hydroxyproline

Modified residue

1

4-hydroxyproline

Experimental info

Non-terminal residue

1

Non-terminal residue

1

Sequences

Sequence

Length

Mass (Da)

Tools

P0C2W2-1 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: FE4DE139C463BEBF
Show »

570

61,737

        10         20         30         40         50         60 
GATGAPGIAG APGFPGARGA PGPQGPSGAP GPKXXXXXXX XXXXXXXXXX XXXXXXXXXX 

        70         80         90        100        110        120 
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 

       130        140        150        160        170        180 
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 

       190        200        210        220        230        240 
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 

       250        260        270        280        290        300 
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGV QGPPGPQGPR 

       310        320        330        340        350        360 
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 

       370        380        390        400        410        420 
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 

       430        440        450        460        470        480 
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGS AGPPGATGFP 

       490        500        510        520        530        540 
GAAGRXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 

       550        560        570 
XXXXXXXXXX XXXXXXXXXX XGVVGLPGQR

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. 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

3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR008160. Collagen. [Graphical view]
Pfam	PF01391. Collagen. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

CO1A1_TYREX

Accession

Primary (citable) accession number: P0C2W2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	November 13, 2007
Last modified:	July 22, 2008
This is version 6 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents