ID   CO1A2_BRACN             Reviewed;          36 AA.
AC   P86290;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Collagen alpha-2(I) chain {ECO:0000303|PubMed:19407199};
DE   AltName: Full=Alpha-2 type I collagen {ECO:0000250|UniProtKB:P02467};
DE   Flags: Fragments;
GN   Name=COL1A2 {ECO:0000250|UniProtKB:P02467};
OS   Brachylophosaurus canadensis (Campanian hadrosaur).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Ornithischia; Ornithopoda;
OC   Hadrosauridae; Brachylophosaurus.
OX   NCBI_TaxID=643745;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND HYDROXYLATION AT
RP   PRO-6; PRO-12 AND PRO-33.
RC   TISSUE=Bone {ECO:0000269|PubMed:19407199};
RX   PubMed=19407199; DOI=10.1126/science.1165069;
RA   Schweitzer M.H., Zheng W., Organ C.L., Avci R., Suo Z., Freimark L.M.,
RA   Lebleu V.S., Duncan M.B., Vander Heiden M.G., Neveu J.M., Lane W.S.,
RA   Cottrell J.S., Horner J.R., Cantley L.C., Kalluri R., Asara J.M.;
RT   "Biomolecular characterization and protein sequences of the Campanian
RT   hadrosaur B. canadensis.";
RL   Science 324:626-631(2009).
CC   -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC       forming collagen). {ECO:0000305}.
CC   -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P02467}.
CC   -!- PTM: Proline residues at the third position of the tripeptide repeating
CC       unit (G-X-Y) are hydroxylated in some or all of the chains.
CC       {ECO:0000269|PubMed:19407199, ECO:0000305}.
CC   -!- MISCELLANEOUS: These protein fragments were extracted from an 80-
CC       million-year-old fossil. The tryptic peptides required multiple
CC       purification steps in order to eliminate contaminants and to increase
CC       the concentration of peptidic material.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family. {ECO:0000255}.
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DR   AlphaFoldDB; P86290; -.
DR   SMR; P86290; -.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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.
FT   CHAIN           <1..>36
FT                   /note="Collagen alpha-2(I) chain"
FT                   /id="PRO_0000376866"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:19407199"
FT   MOD_RES         12
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:19407199"
FT   MOD_RES         33
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:19407199"
FT   NON_CONS        18..19
FT                   /evidence="ECO:0000303|PubMed:19407199"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:19407199"
FT   NON_TER         36
FT                   /evidence="ECO:0000303|PubMed:19407199"
SQ   SEQUENCE   36 AA;  3122 MW;  DE9B0B74B9175502 CRC64;
     GSNGEPGSAG PPGPAGLRGL PGESGAVGPA GPPGSR