| IED ID | IndEnz0002017132 |
| Enzyme Type ID | protease017132 |
| Protein Name |
Collagen alpha-2 I chain Alpha-2 type I collagen |
| Gene Name | Col1a2 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLSFVDTRTLLLLAVTSCLATCQSLQMGSVRKGPTGDRGPRGQRGPAGPRGRDGVDGPVGPPGPPGAPGPPGPPGPPGLTGNFAAQYSDKGVSAGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGSRGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEAGLPGLSGPVGPPGNPGANGLTGAKGATGLPGVAGAPGLPGPRGIPGPVGAAGATGPRGLVGEPGPAGSKGETGNKGEPGSAGAQGPPGPSGEEGKRGSPGEPGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPAGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGEKGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTAGEVGKPGERGLPGEFGLPGPAGPRGERGPPGESGAAGPSGPIGIRGPSGAPGPDGNKGEAGAVGAPGSAGASGPGGLPGERGAAGIPGGKGEKGETGLRGEIGNPGRDGARGAPGAIGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGSAGQPGAKGEKGTKGPKGENGIVGPTGPVGAAGPSGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGIRGPRGDQGPVGRTGEIGASGPPGFAGEKGPSGEPGTTGPPGTAGPQGLLGAPGILGLPGSRGERGQPGIAGALGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGNIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGARGLPGLKGHNGLQGLPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPIGKDGRSGHPGPVGPAGVRGSQGSQGPAGPPGPPGPPGPPGVSGGGYDFGFEGGFYRADQPRSQPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWKSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVNTPAKNAYSRAQANKHVWLGETINGGSQFEYNAEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGRLNKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWDKTVIEYKTNKPSRLPFLDIAPLDIGGTNQEFRVEVGPVCFK |
| Enzyme Length | 1372 |
| Uniprot Accession Number | P02466 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (3); Disulfide bond (3); Domain (1); Glycosylation (2); Metal binding (5); Modified residue (4); Motif (3); Propeptide (2); Region (1); Sequence conflict (6); Signal peptide (1) |
| Keywords | 3D-structure;Calcium;Collagen;Direct protein sequencing;Disulfide bond;Extracellular matrix;Glycoprotein;Hydroxylation;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. |
| Modified Residue | MOD_RES 23; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P08123; MOD_RES 86; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:5337886; MOD_RES 90; /note=Allysine; /evidence=ECO:0000269|PubMed:5337886; MOD_RES 183; /note=5-hydroxylysine; alternate; /evidence=ECO:0000250|UniProtKB:P08123 |
| Post Translational Modification | PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:26479776 |
| Structure 3D | Fiber diffraction (2) |
| Cross Reference PDB | 3HQV; 3HR2; |
| Mapped Pubmed ID | 11295527; 11786959; 1381294; 15234273; 16396496; 17916675; 1951630; 20660018; 7511187; 7512265; 8745212; |
| Motif | MOTIF 783..785; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 828..830; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 1011..1013; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 129,564 |
| Kinetics | |
| Metal Binding | METAL 1187; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1189; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1190; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1192; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1195; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692 |
| Rhea ID | |
| Cross Reference Brenda |