CO1A1_RABIT
ID CO1A1_RABIT Reviewed; 53 AA.
AC P02456;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 77.
DE RecName: Full=Collagen alpha-1(I) chain;
DE AltName: Full=Alpha-1 type I collagen;
DE Flags: Fragment;
GN Name=COL1A1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4194291; DOI=10.1016/0003-9861(70)90367-x;
RA Bornstein P., Nesse R.;
RT "The comparative biochemistry of collagen: the structure of rabbit skin
RT colllagen and its relevance to immunochemical studies of collagen.";
RL Arch. Biochem. Biophys. 138:443-450(1970).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen).
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts
CC with MRC2. Interacts with TRAM2. Interacts with MFAP4 in a Ca (2+)-
CC dependent manner. {ECO:0000250|UniProtKB:P02452,
CC ECO:0000250|UniProtKB:P02453, ECO:0000250|UniProtKB:P02454}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC In bones the fibrils are mineralized with calcium hydroxyapatite.
CC -!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the third
CC position of the tripeptide repeating unit (G-X-Y) are hydroxylated in
CC some or all of the chains. {ECO:0000250|UniProtKB:P11087}.
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 -!- SIMILARITY: Belongs to the fibrillar collagen family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A02856; CGRB1S.
DR PRIDE; P02456; -.
DR Proteomes; UP000001811; Unplaced.
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; Extracellular matrix; Hydroxylation;
KW Phosphoprotein; Reference proteome; Repeat; Secreted.
FT CHAIN 1..>53
FT /note="Collagen alpha-1(I) chain"
FT /id="PRO_0000059397"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P02453"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02454"
FT MOD_RES 26
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305"
FT MOD_RES 29
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305"
FT MOD_RES 32
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305"
FT MOD_RES 41
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305"
FT MOD_RES 44
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305"
FT MOD_RES 47
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305"
FT NON_TER 53
SQ SEQUENCE 53 AA; 4988 MW; 127582E5E52B87FC CRC64;
SYGYBZKSAG VSVPGPMGPS GPRGLPGPPG APGPZGFZGP PGZPGZPGSS GPM
