CO1A2_LITCT
ID CO1A2_LITCT Reviewed; 1355 AA.
AC O42350;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Collagen alpha-2(I) chain;
DE AltName: Full=Alpha-2 type I collagen;
DE Flags: Precursor;
GN Name=COL1A2;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tail;
RX PubMed=9272872; DOI=10.1016/s0378-1119(97)00210-2;
RA Asahina K., Oofusa K., Obara M., Yoshizato K.;
RT "Cloning and characterization of the full length cDNA encoding alpha2 type
RT I collagen of bullfrog Rana catesbeiana.";
RL Gene 194:283-289(1997).
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; D88764; BAA22380.1; -; mRNA.
DR AlphaFoldDB; O42350; -.
DR PRIDE; O42350; -.
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; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT PROPEP 23..71
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005818"
FT CHAIN 72..1110
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000005819"
FT PROPEP 1111..1355
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005820"
FT DOMAIN 1120..1355
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 26..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1176
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 72
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 77
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 168
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 168
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 1206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1150..1182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1190..1353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1261..1306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ SEQUENCE 1355 AA; 127644 MW; CB793AD5D6F41D2A CRC64;
MLSFVDLRSV LLLAVTLYLV TCQEVRRGPR GDKGPPGEQG PPGIPGRDGE DGLPGLPGPP
GVPGLGGNFA AQYDPSKSAE PGQQGIMGPR GPPGPPGSPG SQGFQGLPGE NGEPGQTGPV
GSRGPSGAPG KAGEDGHPGK SGRPGERGPV GPQGARGFPG TPGLPGFKGI RGHTGSDGQK
GAPGAAGVKG ENGANGDNGS PGQAGARGLP GERGRIGPAG SAGSRGSDGS SGPVGPAGPI
GSAGAPGLPG APGAKGELGP AGNNGPTGAA GGRGEPGPPG SLGPAGPPGN PGTNGVNGAK
GTAGLPGVGG APGLPGGRGI PGPAGPAGPS GARGLAGDPG IAGGKGDTGS KGEPGSVGQQ
GPAGPSGEEG KRGPNGEAGS SGPSGNAGIR GVPGTRGLPG PDGRAGGIGP AGSRGSSGPP
GARGPNGDAG RPGEPGLLGA RGLPGFSGSN GPQGKEGPAG PQGIEGRSGA AGPAGARGEP
GAIGFPGPKG PNGEPGKNGD KGNQGPSGNR GAPGPDGNNG AQGPAGLGGA TGEKGEQGPS
GAPGFQGLPG PGGPPGEVGK PGERGAPGDF GPPGSAGTRG ERGAPGESGG AGPHGPSGSR
GPSGAPGPDG QKGEPGAAGL NGGLGPSGPA GIPGERGTAG TPGTKGEKGD AGNSGDYGNP
GRDGARGPAG AAGAPGPAGG PGDRGESGPA GPSGVAGPRG APGERGEAGP AGPTGFAGPP
GAAGHTGAKG DRGAKGPKGE AGSPGPLGAH GSAGPAGPNG PAGSTGARGD AGPSGATGFP
GPAGRAGAPG PPGNVGPSGP TGHPGKDGSR GPRGDSGPVG RPGEQGQHGP VGLAGDKGPS
GEAGPAGPPG AAGPSGVLGA RGILGLPGTR GERGLPGGPG SNGEPGPSGL AGSSGPRGPP
GSVGSPGPVG HSGEAGRDGH PGNDGPPGRD GLPGAKGERG YPGNTGPSGL AGAPGPAGSA
GPAGKSGNRG EGGPSGPAGI TGPSGPRGPA GPQGVRGDKG EAGERGARGL DGRKGHNGLS
GLPGPSGTPG ETGPSGSVGP VGPRGPSGPS GPPGKEGRSG HPGAMGPVGP RGPAGFTGPA
GPPGPPGPPG HAGPSGGGYD GGDGGEYYRA DQPERKPKDY EVDATLKSLN QQIEVILTPE
GSRKNPARTC RDLRLSHPEW TSGFYWIDPN QGCTSDAIRV FCDFSSGETC IHANPDEITQ
KNWYINTSNK DKKHLWFGEI LNGGTQFEYH DEGLTAKDMA TQLAFMRLLA NQASQNITYH
CKNSIAYMDE ETGNLKKAVI LQGSNDVELR AEGNTRFTYS VLEDGCTKHT GEWGKTVIEY
RTNKPSRLPI LDIAPLDIGG HDQEIGFEIG PVCFK
