BioPAX pathway converted from "Association of procollagen type I" in the Reactome database.LEFT-TO-RIGHTAssociation of procollagen type IThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>L7N2N3tbc1d31COL1A1(23-1464)Reactome DB_ID: 10358103endoplasmic reticulum lumenGENE ONTOLOGYGO:0005788UniProt:L7N2N3tbc1d31Xenopus tropicalisNCBI Taxonomy8364UniProtL7N2N323EQUAL1464EQUALReactome Database ID Release 7510358103Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10358103ReactomeR-XTR-16507771Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-XTR-1650777.1Reactomehttp://www.reactome.org2raver23x4Hyp-3Hyp-GalHyl-COL1A2(25-1366)F6WIQ8Reactome DB_ID: 10360859UniProt:F6WIQ8raver2UniProtF6WIQ8(2S,4R)-4-hydroxyprolineMODMOD:00039(2S,3S)-3-hydroxyprolineMODMOD:00038O5-galactosyl-L-hydroxylysineMODMOD:0191425EQUAL1366EQUALReactome Database ID Release 7510360859Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10360859ReactomeR-XTR-20235581Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-XTR-2023558.1C-linked procollagen type I trimerReactome DB_ID: 1036187821Reactome Database ID Release 7510361878Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10361878ReactomeR-XTR-20256691Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-XTR-2025669.1Reactome Database ID Release 7510403629Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10403629ReactomeR-XTR-89442141Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-XTR-8944214.1The C-propeptides are essential for the association of three alpha chains into a trimeric non-helical procollagen. Alignment determines the composition of the trimer, brings the individual chains into the correct register and initiates formation of the triple helix at the C-terminus, which then proceeds to the N-terminus in a zipper-like fashion (Engel & Prockop 1991). Most early refolding studies were performed with collagen type III which contains a disulfide linkage at the C-terminus of its triple helix (Bächinger et al. 1978, Bruckner et al. 1978) that acts as a permanent linker even after removal of the non-collagenous domains. <br><br>Mutations within the C-propeptides further suggest that they are crucial for the correct interaction of the three polypeptide chains and for subsequent correct folding (refs. in Boudko et al. 2011). 710450Pubmed1978The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagenBächinger, HPBrückner, PeterTimpl, REngel, JEur J Biochem 90:605-13171650Pubmed1975Interchain disulfide bonds in procollagen are located in a large nontriple-helical COOH-terminal domainByers, PHClick, EMHarper, EBornstein, PProc Natl Acad Sci U S A 72:3009-131867713Pubmed1991The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipperEngel, JProckop, DJAnnu Rev Biophys Biophys Chem 20:137-52710449Pubmed1978Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transitionBrückner, PeterBächinger, HPTimpl, REngel, JEur J Biochem 90:595-60322001560Pubmed2011The crucial role of trimerization domains in collagen foldingBoudko, SPEngel, JBächinger, HPInt J Biochem Cell Biolinferred from electronic annotationEVIDENCE CODEECO:0000203