ID   CO1A2_ONCMY             Reviewed;        1356 AA.
AC   O93484;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Collagen alpha-2(I) chain;
DE   AltName: Full=Alpha-2 type I collagen;
DE   Flags: Precursor;
GN   Name=col1a2;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11358497; DOI=10.1046/j.1432-1327.2001.02160.x;
RA   Saito M., Takenouchi Y., Kunisaki N., Kimura S.;
RT   "Complete primary structure of rainbow trout type I collagen consisting of
RT   alpha1(I)alpha2(I)alpha3(I) heterotrimers.";
RL   Eur. J. Biochem. 268:2817-2827(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 417-1356.
RC   TISSUE=Fibroblast;
RA   Saito M., Kunisaki N., Hirono I., Aoki T., Ishida M., Urano N., Kimura S.;
RT   "Partial characterization of cDNA clones encoding the three distinct pro
RT   alpha chains of type I collagen from rainbow trout.";
RL   Fish. Sci. 64:780-786(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; AB052837; BAB55663.1; -; mRNA.
DR   EMBL; AB008372; BAA33379.1; -; mRNA.
DR   RefSeq; NP_001117679.1; NM_001124207.1.
DR   AlphaFoldDB; O93484; -.
DR   SMR; O93484; -.
DR   Allergome; 8977; Onc m alpha2I.
DR   PRIDE; O93484; -.
DR   GeneID; 100135811; -.
DR   KEGG; omy:100135811; -.
DR   OrthoDB; 1406711at2759; -.
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; 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..72
FT                   /note="N-terminal propeptide"
FT                   /evidence="ECO:0000250|UniProtKB:P08123"
FT                   /id="PRO_0000005821"
FT   CHAIN           73..1113
FT                   /note="Collagen alpha-2(I) chain"
FT                   /evidence="ECO:0000250|UniProtKB:P08123"
FT                   /id="PRO_0000005822"
FT   PROPEP          1114..1356
FT                   /note="C-terminal propeptide"
FT                   /evidence="ECO:0000250|UniProtKB:P08123"
FT                   /id="PRO_0000005823"
FT   DOMAIN          1123..1356
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          22..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         1174
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   BINDING         1179
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         73
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P08123"
FT   MOD_RES         78
FT                   /note="Allysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08123"
FT   MOD_RES         171
FT                   /note="5-hydroxylysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08123"
FT   CARBOHYD        171
FT                   /note="O-linked (Gal...) hydroxylysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08123"
FT   CARBOHYD        1257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1153..1185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1193..1354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1262..1307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ   SEQUENCE   1356 AA;  126985 MW;  7BB2F1F80DB10C93 CRC64;
     MLSFVDNRIL LLLAVTSLLA SCQSGGLKGP RGAKGPRGDR GPQGPNGRDG KAGLPGIAGP
     PGPPGLGGNF AAQFDGGKGS DPGPGPMGLM GSRGPNGPPG APGPQGFTGH AGEPGEPGQT
     GSIGARGPTG SAGKPGEDGN NGRPGKPGDR GGPGTQGARG FPGTPGLPGM KGHRGYNGLD
     GRKGESGTAG AKGETGAHGA NGSPGPAGSR GLNGERGRAG PAGPAGARGA DGSTGPAGPA
     GPLGAAGPPG FPGAPGPKGE IGGAGSNGPS GPQGGRGEPG INGAVGPVGP VGNPGNNGIN
     GAKGAAGLPG VAGAPGFPGP RGGPGPQGPQ GSTGARGLGG DPGPSGQKGD SGAKGEPGHS
     GVQGAAGPAG EEGKRGSTGE VGATGPAGLR GARGGAGTRG LPGLEGRGGP IGMPGARGAT
     GPGGIRGAPG DAGRAGESGL TGARGLPGNS GQGGPPGKEG PPGAAGLDGR TGPPGPTGPR
     GQPGNIGFPG PKGPGGEAGK GGDKGPTGAT GLRGGPGADG NNGAPGPAGV VGNTGEKGEQ
     GPAGAPGFQG LPGPAGPAGE AGKAGNQGMP GDQGLPGPAG VKGERGNSGP AGSAGSQGAI
     GARGPAGTPG PDGGKGEPGS VGIVGAAGHQ GPGGMPGERG AGGTPGPKGE KGEGGHRGLE
     GNMGRDGARG GPGPSGPPGP SGANGEKGES GSFGPAGPAG LRGPSGERGE GGPAGLPGFA
     GPPGSDGQSG PRGEKGPAGG KGDVGPAGPA GPSGQSGPSG ASGPAGPPGG RGDAGPSGLT
     GFPGAAGRVG GPGPAGIAGP PGSAGPAGKD GPRGLRGDPG PGGPQGEQGV VGPAGISGDK
     GPSGESGPPG APGTAGPQGV LGPSGFVGLP GSRGDKGLPG GPGAVGEPGR LGPAGASGPR
     GPAGNIGMPG MTGTQGEAGR EGNSGNDGPP GRPGAAGFKG DRGEPGSPGA LGSSGQPGPN
     GPAGSAGRPG NRGESGPTGN GGPVGAVGAR GAPGPAGPRG EKGGAGEKGD RGMKGLRGHG
     GLQGMPGPNG PSGETGSAGI TGPAGPRGPA GPHGPPGKDG RAGGHGAIGP VGHRGSPGHL
     GPAGPPGSPG LPGPAGPAGG GYDQSGGYDE YRADQPSFRA KDYEVDATIK SLNSQIENLL
     TPEGSKKNPA RTCRDIRLSH PDWSSGFYWI DPNQGCIADA IKAYCDFSTG HTCIHPHPES
     IARKNWYRSS ENKKHVWFGE TINGGTEFAY NDETLSPQSM ATQLAFMRLL ANQATQNITY
     HCKNSVAYMD GENGNLKKAV LLQGSNDVEL RAEGNSRFTF NVLEDGCTRH TGQWSKTVIE
     YRTNKPSRLP ILDIAPLDIG EADQEFGLDI GPVCFK