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UniProtKB/Swiss-Prot entry P0C2W2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CO1A1_TYREX
Primary accession number P0C2W2
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 2007
Sequence was last modified on November 13, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 6)
Name and origin of the protein
Protein name Collagen alpha-1(I) chain [Fragments]
Synonym Alpha-1 type I collagen
Gene name
Name: COL1A1
From
Tyrannosaurus rex (Tyrant lizard king) [TaxID: 436495] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Tyrannosauridae; Tyrannosaurus.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE, MASS SPECTROMETRY, AND HYDROXYLATION.
TISSUE=Bone;
DOI=10.1126/science.1137614; PubMed=17431180 [NCBI, ExPASy, EBI, Israel, Japan]
Asara J.M., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C.;
"Protein sequences from Mastodon and Tyrannosaurus rex revealed by mass spectrometry.";
Science 316:280-285(2007).
[2]
SEQUENCE REVISION TO 27 AND 470.
TISSUE=Bone;
Asara J.M.;
Submitted (SEP-2007) to UniProtKB.
[3]
COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES.
DOI=10.1126/science.317.5843.1324; PubMed=17823333 [NCBI, ExPASy, EBI, Israel, Japan]
Asara J.M., Garavelli J.S., Slatter D.A., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C.;
"Interpreting sequences from mastodon and T. rex.";
Science 317:1324-1325(2007).
Comments
  • FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
  • SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains (By similarity).
  • SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity).
  • PTM: 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.
  • SIMILARITY: Belongs to the fibrillar collagen family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
3D structure databases
ModBase P0C2W2.
Family and domain databases
InterPro IPR008160; Collagen.
Graphical view of domain structure.
Pfam PF01391; Collagen; 1.
Pfam graphical view of domain structure.
BLOCKS P0C2W2.
Other
ProtoNet P0C2W2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Collagen; Direct protein sequencing; Extinct organism protein; Extracellular matrix; Hydroxylation; Repeat; Secreted; Structural protein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   <1   >570  >570     Collagen alpha-1(I) chain. PRO_0000286177
MOD_RES   6      6        4-hydroxyproline. 
MOD_RES   15     15        4-hydroxyproline. 
MOD_RES   30     30        4-hydroxyproline. 
MOD_RES   294    294        4-hydroxyproline. 
MOD_RES   474    474        4-hydroxyproline. 
MOD_RES   480    480        4-hydroxyproline. 
MOD_RES   567    567        4-hydroxyproline. 
NON_TER   1      1         
NON_TER   570    570         
Sequence information
Length: 570 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 61737 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: FE4DE139C463BEBF [This is a checksum on the sequence]
        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 

P0C2W2 in FASTA format

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