ID   CO1A1_TYREX             Reviewed;         570 AA.
AC   P0C2W2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   22-JUL-2008, entry version 6.
DE   RecName: Full=Collagen alpha-1(I) chain;
DE   AltName: Full=Alpha-1 type I collagen;
DE   Flags: Fragments;
GN   Name=COL1A1;
OS   Tyrannosaurus rex (Tyrant lizard king).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria;
OC   Tyrannosauridae; Tyrannosaurus.
OX   NCBI_TaxID=436495;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND HYDROXYLATION.
RC   TISSUE=Bone;
RX   PubMed=17431180; DOI=10.1126/science.1137614;
RA   Asara J.M., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C.;
RT   "Protein sequences from Mastodon and Tyrannosaurus rex revealed by
RT   mass spectrometry.";
RL   Science 316:280-285(2007).
RN   [2]
RP   SEQUENCE REVISION TO 27 AND 470.
RC   TISSUE=Bone;
RA   Asara J.M.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [3]
RP   COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES.
RX   PubMed=17823333; DOI=10.1126/science.317.5843.1324;
RA   Asara J.M., Garavelli J.S., Slatter D.A., Schweitzer M.H.,
RA   Freimark L.M., Phillips M., Cantley L.C.;
RT   "Interpreting sequences from mastodon and T. rex.";
RL   Science 317:1324-1325(2007).
CC   -!- FUNCTION: Type I collagen is a member of group I collagen
CC       (fibrillar forming collagen).
CC   -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- PTM: Proline residues at the third position of the tripeptide
CC       repeating unit (G-X-Y) are hydroxylated in some or all of the
CC       chains (By similarity).
CC   -!- MISCELLANEOUS: These protein fragments where extracted from a 68
CC       millions years old fossil. The tryptic peptides required multiple
CC       purification steps in order to eliminate contaminants and to
CC       increase the concentration of peptidic material.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
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DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01391; Collagen; 1.
PE   1: Evidence at protein level;
KW   Collagen; Direct protein sequencing; Extinct organism protein;
KW   Extracellular matrix; Hydroxylation; Repeat; Secreted;
KW   Structural protein.
FT   CHAIN        <1   >570       Collagen alpha-1(I) chain.
FT                                /FTId=PRO_0000286177.
FT   MOD_RES       6      6       4-hydroxyproline.
FT   MOD_RES      15     15       4-hydroxyproline.
FT   MOD_RES      30     30       4-hydroxyproline.
FT   MOD_RES     294    294       4-hydroxyproline.
FT   MOD_RES     474    474       4-hydroxyproline.
FT   MOD_RES     480    480       4-hydroxyproline.
FT   MOD_RES     567    567       4-hydroxyproline.
FT   NON_TER       1      1
FT   NON_TER     570    570
SQ   SEQUENCE   570 AA;  61737 MW;  FE4DE139C463BEBF CRC64;
     GATGAPGIAG APGFPGARGA PGPQGPSGAP GPKXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGV QGPPGPQGPR
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGS AGPPGATGFP
     GAAGRXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XGVVGLPGQR
//