| IED ID | IndEnz0002018209 |
| Enzyme Type ID | protease018209 |
| Protein Name |
Collagen alpha-1 VII chain Long-chain collagen LC collagen |
| Gene Name | COL7A1 |
| 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 | MTLRLLVAALCAGILAEAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAALTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD |
| Enzyme Length | 2944 |
| Uniprot Accession Number | Q02388 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Compositional bias (14); Disulfide bond (6); Domain (12); Frameshift (1); Glycosylation (5); Modified residue (14); Motif (4); Natural variant (85); Region (8); Sequence conflict (14); Signal peptide (1); Site (1) |
| Keywords | Alternative splicing;Basement membrane;Cell adhesion;Collagen;Direct protein sequencing;Disease variant;Disulfide bond;Epidermolysis bullosa;Extracellular matrix;Glycoprotein;Hydroxylation;Protease inhibitor;Reference proteome;Repeat;Secreted;Serine protease inhibitor;Signal |
| Interact With | Q5JRA6 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. |
| Modified Residue | MOD_RES 2036; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:2537292; MOD_RES 2039; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:2537292; MOD_RES 2084; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:2537292; MOD_RES 2087; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:2537292; MOD_RES 2090; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:2537292; MOD_RES 2167; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2176; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2185; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2188; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2625; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2631; /note=5-hydroxylysine; alternate; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2664; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2667; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:8051117; MOD_RES 2673; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:8051117 |
| 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:2537292}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10366422; 10551873; 10679020; 10747087; 10809722; 10825291; 10903204; 10934207; 10982397; 11035026; 11285137; 11306556; 11577169; 11927603; 11986329; 12060403; 12235121; 12353709; 12475640; 12482924; 12485454; 12787118; 1323838; 14500733; 14727126; 15044469; 15113589; 15265795; 15365990; 15774758; 1577494; 15810887; 15816848; 15888141; 16169070; 16272566; 16303754; 16470588; 16500083; 16563355; 16591531; 16624868; 16923137; 16971478; 17005010; 17038314; 1704217; 17106611; 171650; 17192411; 17229600; 17287728; 17316621; 17336503; 17425959; 17495952; 17525268; 17916216; 18331784; 18374850; 18429782; 18440202; 18450758; 18487197; 18496702; 18558993; 18599485; 18843296; 19075007; 19164740; 19197535; 19250433; 19367581; 19422682; 19435799; 19486043; 19638414; 19656848; 19665875; 19681861; 19945621; 20184583; 20195357; 20470363; 20545907; 20555349; 20679433; 20920254; 20966969; 21113014; 21448560; 21478858; 21482078; 21525241; 21532587; 21574979; 21658117; 21878990; 21879237; 21967573; 21994455; 22013193; 22070715; 22157747; 22209565; 22266148; 22515571; 22675024; 22757647; 22974128; 23106673; 23226319; 23378591; 23397949; 23479643; 23591773; 23624125; 23679163; 23688405; 23698585; 23769655; 23834951; 23947675; 24117545; 24119662; 24127822; 24213372; 24252097; 24317394; 24357722; 24732400; 24794830; 24810542; 24917561; 24927163; 25406594; 25425313; 2543975; 2551898; 25556825; 25566895; 25586378; 25619252; 25619253; 25639640; 25689103; 26066885; 26289024; 26472200; 26476432; 26568311; 26586712; 26595603; 26897595; 27117059; 27328306; 27899325; 28126522; 28164502; 2834383; 2845110; 28800953; 29182795; 29272047; 29305555; 29473190; 29490344; 29499655; 29504492; 29512192; 29512197; 29531004; 29574987; 3082888; 30930113; 31709745; 3173483; 32396230; 32484238; 32926178; 33081018; 33258232; 34543471; 34948168; 3872795; 6809411; 710450; 8463259; 8663406; 8920930; 9054364; 9092507; 9094723; 9150144; 9245798; 9307973; 9545296; 9560306; 9582318; 9647643; 9651395; 9856810; |
| Motif | MOTIF 1170..1172; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 1334..1336; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 2008..2010; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 2553..2555; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 295,220 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |