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P0C2W2 (CO1A1_TYREX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaTyrannosauridaeTyrannosaurus

Protein attributes

Sequence length570 AA.
Sequence statusFragments.
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.

Subcellular location

Secretedextracellular spaceextracellular 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-year-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
   PTMHydroxylation
   Technical termDirect protein sequencing
Extinct organism protein
Gene Ontology (GO)
   Cellular_componentcollagen

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›570›570Collagen alpha-1(I) chain
PRO_0000286177

Amino acid modifications

Modified residue614-hydroxyproline Ref.1
Modified residue1214-hydroxyproline Ref.1
Modified residue1514-hydroxyproline Ref.1
Modified residue3014-hydroxyproline Ref.1
Modified residue29414-hydroxyproline Ref.1
Modified residue47414-hydroxyproline Ref.1
Modified residue48014-hydroxyproline Ref.1
Modified residue56714-hydroxyproline Ref.1

Experimental info

Non-terminal residue11
Non-terminal residue5701

Sequences

Sequence LengthMass (Da)Tools
P0C2W2 [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES.
[4]"Comment on 'Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry'."
Buckley M., Walker A., Ho S.Y., Yang Y., Smith C., Ashton P., Oates J.T., Cappellini E., Koon H., Penkman K., Elsworth B., Ashford D., Solazzo C., Andrews P., Strahler J., Shapiro B., Ostrom P., Gandhi H. expand/collapse author list , Miller W., Raney B., Zylber M.I., Gilbert M.T., Prigodich R.V., Ryan M., Rijsdijk K.F., Janoo A., Collins M.J.
Science 319:33-33(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Response to comment on 'Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry'."
Asara J.M., Schweitzer M.H., Cantley L.C., Cottrell J.S.
Science 319:33-33(2008)
Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Comment on 'Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry'."
Pevzner P.A., Kim S., Ng J.
Science 321:1040-1040(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Response to comment on 'Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry'."
Asara J.M., Schweitzer M.H., Cantley L.C., Cottrell J.S.
Science 321:1040-1040(2008)
Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Reanalysis of Tyrannosaurus rex mass spectra."
Bern M., Phinney B.S., Goldberg D.
J. Proteome Res. 8:4328-4332(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

3D structure databases

ProteinModelPortalP0C2W2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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: April 16, 2014
This is version 18 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families