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Reviewed, UniProtKB/Swiss-Prot P0C2W2 (CO1A1_TYREX)

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

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Collagen alpha-1(I) chain
Alternative name(s):
    Alpha-1 type I collagen
Gene names
Name: COL1A1
OrganismTyrannosaurus rex (Tyrant lizard king)
Taxonomic identifier436495 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaTyrannosauridaeTyrannosaurus

Protein attributes

Sequence length570 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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 componentExtracellular matrix
Secreted
   DomainCollagen
Repeat
   Molecular functionStructural protein
   PTMHydroxylation
   Technical termDirect protein sequencing
Extinct organism protein

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain‹1 – ›570›570Collagen alpha-1(I) chain

Amino acid modifications

Modified residue614-hydroxyproline
Modified residue1514-hydroxyproline
Modified residue3014-hydroxyproline
Modified residue29414-hydroxyproline
Modified residue47414-hydroxyproline
Modified residue48014-hydroxyproline
Modified residue56714-hydroxyproline

Experimental info

Non-terminal residue11
Non-terminal residue5701

Sequences

Sequence LengthMass (Da)Tools
P0C2W2-1 [UniParc].

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

FASTA57061,737
        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 

« Hide

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

ModBaseSearch...

Family and domain databases

InterProIPR008160. Collagen.
[Graphical view]
PfamPF01391. Collagen. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameCO1A1_TYREX
AccessionPrimary (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 statusReviewed (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