CO1A1_BRACN
ID CO1A1_BRACN Reviewed; 113 AA.
AC P86289;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Collagen alpha-1(I) chain {ECO:0000303|PubMed:19407199};
DE AltName: Full=Alpha-1 type I collagen {ECO:0000250|UniProtKB:P02457};
DE Flags: Fragments;
GN Name=COL1A1 {ECO:0000250|UniProtKB:P02457};
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; PRO-15; PRO-30; PRO-39; PRO-54; PRO-60; PRO-84; PRO-90 AND
RP PRO-107.
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:P02457}.
CC -!- PTM: Contains mostly 4-hydroxyproline (Probable). Proline residues at
CC the third position of the tripeptide repeating unit (G-X-Y) are
CC hydroxylated in some or all of the chains.
CC {ECO:0000269|PubMed:19407199, ECO:0000305}.
CC -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs
CC on the first proline residue in the sequence motif Gly-Pro-Hyp, where
CC Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P11087}.
CC -!- PTM: Lysine residues at the third position of the tripeptide repeating
CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
CC {ECO:0000250|UniProtKB:P02457}.
CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC glycan consists of a Glc-Gal disaccharide.
CC {ECO:0000250|UniProtKB:P11087}.
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; P86289; -.
DR PRIDE; P86289; -.
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..>113
FT /note="Collagen alpha-1(I) chain"
FT /id="PRO_0000376865"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..57
FT /note="Pro residues"
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 15
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT MOD_RES 30
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT MOD_RES 33
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 39
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT MOD_RES 54
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT MOD_RES 60
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT MOD_RES 72
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 84
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT MOD_RES 90
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT MOD_RES 107
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19407199"
FT NON_CONS 18..19
FT /evidence="ECO:0000303|PubMed:19407199"
FT NON_CONS 33..34
FT /evidence="ECO:0000303|PubMed:19407199"
FT NON_CONS 45..46
FT /evidence="ECO:0000303|PubMed:19407199"
FT NON_CONS 78..79
FT /evidence="ECO:0000303|PubMed:19407199"
FT NON_CONS 95..96
FT /evidence="ECO:0000303|PubMed:19407199"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:19407199"
FT NON_TER 113
FT /evidence="ECO:0000303|PubMed:19407199"
SQ SEQUENCE 113 AA; 9664 MW; CB12357E46AE3DE8 CRC64;
GATGAPGIAG APGFPGARGP SGPQGPSGAP GPKGVQGPPG PQGPRGLTGP IGPPGPAGAP
GDKGEAGPSG PPGPTGARGS AGPPGATGFP GAAGRGETGP AGPAGPPGPA GAR
