ID   CO1A2_RABIT             Reviewed;         526 AA.
AC   Q28668;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Collagen alpha-2(I) chain;
DE   AltName: Full=Alpha-2 type I collagen;
DE   Flags: Precursor; Fragment;
GN   Name=COL1A2;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Calvaria;
RA   Inoue S., Okazaki T.;
RT   "Alpha 2 type I collagen gene expression in the rabbit knee ligaments:
RT   variations during the newborn development and in the adult age.";
RL   Biomed. Res. 16:219-227(1995).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC   -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC       In bones the fibrils are mineralized with calcium hydroxyapatite.
CC   -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC       crucial roles in tissue growth and repair by controlling both the
CC       intracellular assembly of procollagen molecules and the extracellular
CC       assembly of collagen fibrils. It binds a calcium ion which is essential
CC       for its function (By similarity). {ECO:0000250}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC       (G-X-Y) are hydroxylated in some or all of the chains.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR   EMBL; D49399; BAA08391.1; -; mRNA.
DR   PIR; I46677; I46677.
DR   AlphaFoldDB; Q28668; -.
DR   SMR; Q28668; -.
DR   STRING; 9986.ENSOCUP00000010575; -.
DR   PRIDE; Q28668; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   InParanoid; Q28668; -.
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   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   SMART; SM00038; COLFI; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Collagen; Disulfide bond; Extracellular matrix; Hydroxylation;
KW   Metal-binding; Reference proteome; Repeat; Secreted.
FT   CHAIN           <1..262
FT                   /note="Collagen alpha-2(I) chain"
FT                   /id="PRO_0000005810"
FT   PROPEP          263..526
FT                   /note="C-terminal propeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005811"
FT   DOMAIN          293..526
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          1..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..262
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         341
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        323..355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        363..524
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        432..477
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   NON_TER         1
SQ   SEQUENCE   526 AA;  53129 MW;  7CA8F0FA6953846D CRC64;
     GFPGEKGPSG EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA LGEPGPLGIA
     GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GSDGPPGRDG QPGHKGERGY PGNAGPVGAA
     GAPGPQGSVG PTGKHGNRGE PGPAGSIGPV GAAGPRGPSG PQGIRGDKGE PGDKGPRGLP
     GIKGHNGLQG LPGLAGQHGD QGAPGAVGPA GPRGPAGPTG PAGKDGRSGH PGTVGPAGLR
     GSQGSQGPAG PPGPPGPPGP PGASGGGYDF GYDGDFYRAD QPRSPPSLRP KDYEVDATLK
     SLNNQIETLL TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG
     ETCIRAQPEN ISVKNWYKSS KAKKHVWLGE TINGGTQFEY NVEGVTSKEM ATQLAFMRLL
     ANHASQNITY HCKNSIAYMD EETGNLNKAV ILQGSNDVEL VAEGNSRFTY TVLVDGCTKK
     TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG GADQEFYVDV GPVCFK