ID   CO2A1_TYREX             Reviewed;          14 AA.
AC   P0C2W3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   13-NOV-2007, entry version 5.
DE   Collagen alpha-1(II) chain (Alpha-1 type II collagen) (Fragment).
GN   Name=COL2A1;
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 II collagen is specific for cartilaginous tissues.
CC       It is essential for the normal embryonic development of the
CC       skeleton, for linear growth and for the ability of cartilage to
CC       resist compressive forces (By similarity).
CC   -!- SUBUNIT: Homotrimers of alpha 1(II) chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (G-X-Y) are hydroxylated in some or all of the chains (By
CC       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.
CC   -!- SIMILARITY: Contains 1 VWFC domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
PE   1: Evidence at protein level;
KW   Collagen; Direct protein sequencing; Extinct organism protein;
KW   Extracellular matrix; Repeat; Secreted; Structural protein.
FT   CHAIN        <1    >14       Collagen alpha-1(II) chain.
FT                                /FTId=PRO_0000286184.
FT   NON_TER       1      1
FT   NON_TER      14     14
SQ   SEQUENCE   14 AA;  1292 MW;  3D7835BEF84F9C28 CRC64;
     GLVGAPGLRG LPGK
//