ID   CO1A2_TYREX             Reviewed;          18 AA.
AC   P0C2W4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-NOV-2008, entry version 7.
DE   RecName: Full=Collagen alpha-2(I) chain;
DE   AltName: Full=Alpha-2 type I collagen;
DE   Flags: Fragment;
GN   Name=COL1A2;
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, AND MASS SPECTROMETRY.
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   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   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Collagen; Direct protein sequencing; Extinct organism protein;
KW   Extracellular matrix; Repeat; Secreted.
FT   CHAIN        <1    >18       Collagen alpha-2(I) chain.
FT                                /FTId=PRO_0000286185.
FT   NON_TER       1      1
FT   NON_TER      18     18
SQ   SEQUENCE   18 AA;  1579 MW;  47D5FA729AE23B19 CRC64;
     GLPGESGAVG PAGPIGSR
//