CO1A2_CANLF
ID CO1A2_CANLF Reviewed; 1366 AA.
AC O46392;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Collagen alpha-2(I) chain;
DE AltName: Full=Alpha-2 type I collagen;
DE Flags: Precursor;
GN Name=COL1A2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=9721184; DOI=10.1006/abbi.1998.0774;
RA Campbell B.G., Wootton J.A.M., MacLeod J.N., Minor R.R.;
RT "Sequence of canine COL1A2 cDNA: nucleotide substitutions affecting the
RT cyanogen bromide peptide map of the alpha 2(I) chain.";
RL Arch. Biochem. Biophys. 357:67-75(1998).
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. {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; AF035120; AAC64485.1; -; mRNA.
DR RefSeq; NP_001003187.1; NM_001003187.1.
DR AlphaFoldDB; O46392; -.
DR ComplexPortal; CPX-3103; Collagen type I trimer.
DR STRING; 9612.ENSCAFP00000029400; -.
DR PaxDb; O46392; -.
DR PRIDE; O46392; -.
DR GeneID; 403824; -.
DR KEGG; cfa:403824; -.
DR CTD; 1278; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; O46392; -.
DR OrthoDB; 1406711at2759; -.
DR Proteomes; UP000002254; 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; 5.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT PROPEP 23..79
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005801"
FT CHAIN 80..1119
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000005802"
FT PROPEP 1120..1366
FT /note="C-terminal propeptide"
FT /id="PRO_0000005803"
FT DOMAIN 1133..1366
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 27..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 84
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 177
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 177
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT DISULFID 1163..1195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1203..1364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1272..1317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ SEQUENCE 1366 AA; 129400 MW; CD936969E080BCD4 CRC64;
MLSFVDTRTL LLLAVTSCLA TCQSLQEATA RKGPTGDRGP RGERGPPGPP GRDGDDGIPG
PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG PPGASGAPGP QGFQGPAGEP
GEPGQTGPAG ARGPPGPPGK AGEDGHPGKP GRPGERGVVG PQGARGFPGT PGLPGFKGIR
GHNGLDGLKG QPGAPGVKGE PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV
GPVGPAGPIG SAGPPGFPGA PGPKGEIGPV GNPGPAGPAG PRGEVGLPGV SGPVGPPGNP
GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGIVGEPGP AGSKGESGNK
GEPGSAGAQG PPGPSGEEGK RGPNGEAGSA GPSGPPGLRG SPGSRGLPGA DGPAGVMGPP
GPRGATGPAG VRGPNGDSGR PGEPGLMGPR GFPGAPGNVG PAGKEGPMGL PGIDGRPGPI
GPAGARGEPG NIGFPGPKGP TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ
GGKGEQGPAG PPGFQGLPGP AGTAGEVGKP GERGLPGEFG LPGPAGPRGE RGPPGESGAA
GPSGPIGSRG PSGPPGPDGN KGEPGVLGAP GTAGASGPGG LPGERGAAGI PGGKGEKGET
GLRGEIGNPG RDGARGAPGA MGAPGPAGAT GDRGEAGPAG PAGPAGPRGT PGERGEVGPA
GPNGFAGPAG AAGQPGAKGE RGTKGPKGEN GPVGPTGPIG SAGPSGPNGP PGPAGSRGDG
GPPGATGFPG AAGRTGPPGP SGITGPPGPP GAAGKEGLRG PRGDQGPVGR TGETGASGPP
GFTGEKGPSG EPGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGS VGEPGPLGIA
GPPGARGPPG AVGAPGVNGA PGEAGRDGNP GNDGPPGRDG QAGHKGERGY PGNIGPVGAV
GAPGPHGPVG PTGKHGNRGE PGPAGSVGPV GAVGPRGPSG PQGIRGDKGE PGEKGPRGLP
GLKGHNGLQG LPGLAGQHGD QGAPGSVGPA GPRGPAGPSG PAGKDGRTGQ PGTVGPAGIR
GSQGSQGPAG PPGPPGPPGP PGPSGGGYDF GYEGDFYRAD QPRSPPSLRP KDYEVDATLK
SLNNQIETLL TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG
ETCIRAQPEN IPAKNWYRNS KVKKHIWLGE TINGGTQFEY NVEGVTTKEM ATQLAFMRLL
ANHASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL VAEGNSRFTY TVLVDGCSKK
TNEWRKTIIE YKTNKPSRLP ILDIAPLDIG DADQEFRVDV GPVCFK
