Detail Information for IndEnz0002017054
IED ID IndEnz0002017054
Enzyme Type ID protease017054
Protein Name Collagen alpha-2
I
chain
Alpha-2 type I collagen
Gene Name COL1A2
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGHPGTVGPAGIRGPQGHQGPAGPPGPPGPPGPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETINAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK
Enzyme Length 1366
Uniprot Accession Number P08123
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 (15); Natural variant (113); Propeptide (2); Region (1); Sequence conflict (11); Signal peptide (1)
Keywords 3D-structure;Calcium;Chromosomal rearrangement;Collagen;Direct protein sequencing;Disease variant;Disulfide bond;Dwarfism;Ehlers-Danlos syndrome;Extracellular matrix;Glycoprotein;Hydroxylation;Metal-binding;Osteogenesis imperfecta;Pyrrolidone carboxylic acid;Reference proteome;Repeat;Secreted;Signal
Interact With P02452; O00303; Q6PIL6; Q14696; O43765; Q96EQ0; Q96GM5; Q9UMX0; Q9UMX0-2; Q9UHD9
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:0000269|PubMed:2394758"; MOD_RES 47; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255"; MOD_RES 50; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255"; MOD_RES 62; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255"; MOD_RES 65; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255"; MOD_RES 68; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255"; MOD_RES 71; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255"; MOD_RES 80; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:5529814"; MOD_RES 84; /note="Allysine"; /evidence="ECO:0000269|PubMed:5529814"; MOD_RES 102; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:3680255"; MOD_RES 108; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:3680255"; MOD_RES 177; /note="5-hydroxylysine; alternate"; /evidence="ECO:0000269|PubMed:4319110"; MOD_RES 420; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:4412529"; MOD_RES 441; /note="4-hydroxyproline"; /evidence="ECO:0000269|PubMed:4412529"; MOD_RES 444; /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. {ECO:0000269|PubMed:4412529}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000250|UniProtKB:P02466
Structure 3D X-ray crystallography (4)
Cross Reference PDB 5CTD; 5CTI; 5CVA; 6JEC;
Mapped Pubmed ID 10479448; 10521801; 10551873; 10596943; 10627461; 10686426; 10809722; 10872800; 10887121; 10934207; 11084047; 11259413; 11310843; 11481033; 11518510; 11572855; 11577169; 11668615; 11700320; 11836364; 11986307; 12101112; 12160476; 12200454; 12211432; 12225811; 1237296; 12393755; 12424255; 12475640; 12496264; 12646579; 12702564; 12759229; 12813128; 12855811; 12879219; 12968017; 1323838; 1348714; 1400327; 14500733; 14555266; 14739420; 1484505; 15044469; 15075323; 15085313; 15149860; 15155468; 15211650; 15241796; 15257288; 15345715; 15365990; 15389632; 1544908; 15514164; 15516691; 15599596; 1567360; 15703183; 15741186; 1577494; 15788405; 15818662; 15837520; 15869882; 15917161; 15982862; 15983038; 16036621; 16091368; 16102041; 16192463; 16272566; 16278217; 16285730; 16293224; 16316921; 16463783; 16563355; 16564026; 16591531; 16702209; 16782899; 16806867; 16825197; 16849317; 16864092; 17072841; 17142024; 17146610; 171650; 17334644; 17407139; 17459242; 17485091; 17588949; 17620151; 17653508; 17875077; 17884818; 17903307; 18093617; 18209062; 18284430; 18298657; 18323784; 18434090; 18487197; 18570923; 18599485; 18644377; 18664619; 1874735; 18791848; 18818748; 19015742; 19035720; 19075007; 19180518; 19208385; 19282863; 19395477; 1939645; 19409513; 19424577; 19426706; 19491193; 19527514; 19559927; 19565505; 19578796; 19594296; 19679847; 19700402; 19705750; 19714363; 19790048; 19913121; 19929435; 19932771; 20087402; 20102701; 2010539; 20140262; 20452482; 20463013; 20466318; 20470363; 2059554; 20628086; 20673868; 20711500; 20721936; 20730098; 20736093; 20837772; 20961463; 21044367; 21252155; 21341209; 21405976; 21443102; 21530898; 21602843; 21665180; 21667357; 21690299; 21746880; 21789315; 21841309; 21874239; 21878990; 21967573; 22028813; 22049076; 22130917; 22131293; 22379029; 22674299; 22796342; 22815632; 23036172; 23079621; 23227268; 23546968; 23548243; 2364322; 23800505; 23918805; 24042342; 24058639; 24140640; 2430969; 24361166; 24434151; 24641356; 24668929; 24709079; 24804215; 24835590; 25107895; 25200162; 25290763; 25416956; 2543975; 25451260; 2551898; 25608812; 25692237; 25716998; 25858481; 25944380; 26065693; 26235824; 26260940; 26452701; 26471105; 26496610; 26564713; 26861712; 26910001; 26926600; 26927310; 27027429; 27090748; 27264419; 27454992; 27519266; 27655672; 27665867; 27691923; 27748872; 27894325; 27897211; 27997896; 28281531; 2834383; 28401451; 28424212; 2845110; 28498836; 28528406; 28612031; 28738217; 28810924; 28916840; 28930368; 28953610; 28981938; 29164999; 29543922; 29572562; 29594386; 29636545; 30172079; 30310058; 30358852; 3038863; 30583585; 30604926; 30683734; 30716784; 30825231; 30945869; 31159867; 31202624; 31371266; 3155520; 3159726; 3173483; 31794058; 31853946; 31876392; 32081708; 32091183; 32157794; 32166892; 32234057; 32335875; 32335877; 32482890; 32843132; 32989910; 33707149; 33737018; 33974636; 34290266; 34592197; 34727246; 3595596; 3872140; 3872795; 3905801; 3992061; 41816; 5246001; 5723342; 6129847; 6270089; 6313757; 641035; 6439184; 6809411; 710450; 7852349; 7890717; 8034572; 8144597; 8207089; 8440685; 8463259; 8576151; 8617742; 8631758; 8920930; 8943283; 8999957; 9028946; 9054364; 9092507; 9252349; 9295288; 9425086; 9470928; 9545296; 9560306; 9582318; 9651395; 9659899; 9659900; 9685393;
Motif
Gene Encoded By
Mass 129,314
Kinetics
Metal Binding METAL 1181; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1183; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1184; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1186; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q03692; METAL 1189; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q03692
Rhea ID
Cross Reference Brenda