IED Industry Enzyme Database

Detail Information for IndEnz0002005509
IED ID IndEnz0002005509
Enzyme Type ID protease005509
Protein Name Collagen alpha-2
I
chain
Alpha-2 type I collagen
Gene Name COL1A2
Organism Bos taurus (Bovine)
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MLSFVDTRTLLLLAVTSCLATCQSLQEATARKGPSGDRGPRGERGPPGPPGRDGDDGIPGPPGPPGPPGPPGLGGNFAAQFDAKGGGPGPMGLMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLPGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGAVGQPGPPGPSGEEGKRGSTGEIGPAGPPGPPGLRGNPGSRGLPGADGRAGVMGPAGSRGATGPAGVRGPNGDSGRPGEPGLMGPRGFPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPSGDPGKAGEKGHAGLAGARGAPGPDGNNGAQGPPGLQGVQGGKGEQGPAGPPGFQGLPGPAGTAGEAGKPGERGIPGEFGLPGPAGARGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAPGTAGPSGPSGLPGERGAAGIPGGKGEKGETGLRGDIGSPGRDGARGAPGAIGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTKGPKGENGPVGPTGPVGAAGPSGPNGPPGPAGSRGDGGPPGATGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRSGETGASGPPGFVGEKGPSGEPGTAGPPGTPGPQGLLGAPGFLGLPGSRGERGLPGVAGSVGEPGPLGIAGPPGARGPPGNVGNPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNAGPVGAAGAPGPQGPVGPVGKHGNRGEPGPAGAVGPAGAVGPRGPSGPQGIRGDKGEPGDKGPRGLPGLKGHNGLQGLPGLAGHHGDQGAPGAVGPAGPRGPAGPSGPAGKDGRIGQPGAVGPAGIRGSQGSQGPAGPPGPPGPPGPPGPSGGGYEFGFDGDFYRADQPRSPTSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPEDIPVKNWYRNSKAKKHVWVGETINGGTQFEYNVEGVTTKEMATQLAFMRLLANHASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWQKTIIEYKTNKPSRLPILDIAPLDIGGADQEIRLNIGPVCFK
Enzyme Length 1364
Uniprot Accession Number P02465
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 (4); Disulfide bond (3); Domain (1); Glycosylation (2); Metal binding (5); Modified residue (48); Propeptide (2); Region (1); Sequence conflict (5); Signal peptide (1)
Keywords 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 80; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:4609475; MOD_RES 84; /note=Allysine; /evidence=ECO:0000305|PubMed:4609475; MOD_RES 100; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 106; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 115; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 118; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 121; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 133; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 136; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 145; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 151; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 166; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 169; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 172; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 175; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:173531; MOD_RES 190; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 193; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 196; /note=5-hydroxylysine; /evidence=ECO:0000269|PubMed:173531; MOD_RES 199; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 202; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 208; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 217; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 226; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 253; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 256; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 259; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 262; /note=5-hydroxylysine; /evidence=ECO:0000269|PubMed:173531; MOD_RES 271; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 286; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 295; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 304; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 307; /note=5-hydroxylysine; /evidence=ECO:0000269|PubMed:173531; MOD_RES 313; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 319; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 322; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 328; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 346; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 352; /note=5-hydroxylysine; /evidence=ECO:0000269|PubMed:173531; MOD_RES 361; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 367; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 370; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 391; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 394; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 400; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 406; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:173531; MOD_RES 439; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:4412529; MOD_RES 442; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:4412529
Post Translational Modification PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000250|UniProtKB:P02466
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12878203; 15848196;
Motif
Gene Encoded By
Mass 129,064
Kinetics
Metal Binding METAL 1179; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1181; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1182; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1184; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1187; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692
Rhea ID
Cross Reference Brenda