| IED ID | IndEnz0002018216 |
| Enzyme Type ID | protease018216 |
| Protein Name |
Collagen alpha-1 VII chain Long-chain collagen LC collagen |
| Gene Name | Col7a1 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MRLRLLVAALCAAEILMGAPEVWAQPRDRVTCTRLYAADIVFLLDGSSSIGRSNFREVRGFLEGLVLPFSGAASAQGVRFATVQYSDDPQTEFGLDTLGSGSDTIRAIRELSYKGGNTRTGAALHHVSDRVFLPRLTRPGVPKVCILITDGKSQDLVDTAAQKLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLISRRVCTTAGGVPVTLPSDDTPSGPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNIPAGETSTRLQGLRPLTDYQVTVVALYANSIGEAVSGTARTTAKEGLELSLQNITSHSLLVAWRRVPGANGYRVTWRDLSGGPTQQQDLSPGQGSVFLDHLEPGTDYEVTVSALFGHSVGPAASLTARTASSVEQTLHPIILSPTSILLSWNLVPEARGYRLEWRRESGLETPQKVELPPDVTRHQLDGLQPGTEYRLTLYTLLEGREVATPATVVPTGLEQLVSPVMNLQAIELPGQRVRVSWNPVPGATEYRFTVRTTQGVERTLLLPGSQTTFDLDDVRAGLSYTVRVSARVGAQEGDASILTIHRDPEAPLVVPGLRVVASDATRIRVAWGLVPGASGFRISWRTGSGPESSRTLTPDSTVTDILGLQPSTSYQVAVSALRGREEGPPVVIVARTDPLGPVRRVHLTQAGSSSVSITWTGVPGATGYRVSWHSGHGPEKSLLVSGDATVAEIDGLEPDTEYIVRVRTHVAGVDGAPASVVVRTAPEPVGSVSKLQILNASSDVLRVTWVGVPGATSYKLAWGRSEGGPMKHRILPGNKESAEIRDLEGGVSYSVRVTALVGDREGAPVSIVITTPPATPALLETLQVVQSGEHSLRLRWEPVPGAPGFRLHWQPEGGQEQSLTLGPESNSYNLVGLEPATKYQVWLTVLGQTGEGPPRKVTAYTEPSHIPSTELRVVDTSIDSVTLTWTPVSGASSYILSWRPLRGTGQEVPRAPQTLPGTSSSHRVTGLEPGISYVFSLTPIQSGVRGSEISVTQTPACSHGPVDVVFLLHATRDNAHNAEAVRRVLERLVSALGPLGPQAAQVGLLTYSHRPSPLFPLNSSHDLGIILRKIRDIPYVDPSGNNLGTAVTTAHRYLLASNAPGRRQQVPGVMVLLVDEPLRGDILSPIREAQTSGLKVMALSLVGADPEQLRRLAPGTDPIQNFFAVDNGPGLDRAVSDLAVALCQAAVTIEPQTGPCAVHCPKGQKGEPGVTGLQGQAGPPGPPGLPGRTGAPGPQGPPGSTQAKGERGFPGPEGPPGSPGLPGVPGSPGIKGSTGRPGPRGEQGERGPQGPKGEPGEPGQITGGGGPGFPGKKGDPGPSGPPGSRGPVGDPGPRGPPGLPGISVKGDKGDRGERGPPGPGIGASEQGDPGLPGLPGSPGPQGPAGRPGEKGEKGDCEDGGPGLPGQPGPPGEPGLRGAPGMTGPKGDRGLTGTPGEPGVKGERGHPGPVGPQGLPGAAGHPGVEGPEGPPGPTGRRGEKGEPGRPGDPAVGPGGAGAKGEKGEAGLPGPRGASGSKGEQGAPGLALPGDPGPKGDPGDRGPIGLTGRAGPTGDSGPPGEKGEPGRPGSPGPVGPRGRDGEAGEKGDEGIPGEPGLPGKAGERGLRGAPGPRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDAGIESRDKGEPGQEGPRGPKGDPGPPGVSGERGIDGLRGPPGPQGDPGVRGPAGDKGDRGPPGLDGRSGLDGKPGAPGPPGLHGASGKAGDPGRDGLPGLRGEHGPPGPPGPPGVPGKAGDDGKPGLNGKNGDPGDPGEDGRKGEKGDSGAPGREGPDGPKGERGAPGNPGLQGPPGLPGQVGPPGQGFPGVPGITGPKGDRGETGSKGEQGLPGERGLRGEPGSLPNAERLLETAGIKVSALREIVDTWDESSGSFLPVPERRPGPKGDPGDRGPPGKEGLIGFPGERGLKGERGDPGPQGPPGLALGERGPPGPPGLAGEPGKPGIPGLPGRAGGSGEAGRPGERGERGEKGERGDQGRDGLPGLPGPPGPPGPKVAIEEPGPGLAREQGPPGLKGAKGEPGSDGDPGPKGDRGVPGIKGDVGEPGKRGHDGNPGLPGERGVAGPEGKPGLQGPRGTPGPVGSHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLPGPVGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGPPGRDGSSGKDGDRGSPGVPGSPGLPGPVGPKGEPGPVGAPGQVVVGPPGAKGEKGAPGDLAGALLGEPGAKGDRGLPGPRGEKGEAGRAGGPGDPGEDGQKGAPGLKGLKGEPGIGVQGPPGPSGPPGMKGDLGPPGAPGAPGVVGFPGQTGPRGETGQPGPVGERGLAGPPGREGAPGPLGPPGPPGSAGAPGASGLKGDKGDPGAGLPGPRGERGEPGVRGEDGHPGQEGPRGLVGPPGSRGEQGEKGAAGAAGLKGDKGDSAVIEGPPGPRGAKGDMGERGPRGIDGDKGPRGESGNPGDKGSKGEPGDKGSAGSIGVRGLTGPKGEPGAAGIPGEPGAPGKDGIPGFRGDKGDIGFMGPRGLKGEKGIKGTCGRDGERGDKGEAGFPGRPGLAGKKGDMGEPGLPGQSGAPGKEGLIGPKGDRGFDGQSGPKGDQGEKGERGPPGVGGFPGPRGNDGSSGPPGPPGGVGPKGPEGLQGQKGERGPPGESVVGAPGAPGTPGERGEQGRPGPAGPRGEKGEAALTEDDIRDFVRQEMSQHCACQGQFIASGSRPLPGYAADTAGSQLHHVPVLRVSHVEEEGQVPPEDDDDFSEYSVYSVEDYQEPEVPWDGEAEIKGWDQRGSDLCSLPLDEGSCTAYTLRWYHRAVPGGTACHPFVYGGCGGNANRFGTREACERRCPPQGVHSQKTGAA |
| Enzyme Length | 2944 |
| Uniprot Accession Number | Q63870 |
| 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. {ECO:0000250|UniProtKB:Q02388, ECO:0000269|PubMed:10523500}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (7); Chain (1); Compositional bias (13); Disulfide bond (6); Domain (12); Glycosylation (3); Helix (6); Modified residue (9); Motif (5); Region (6); Sequence conflict (3); Signal peptide (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Basement membrane;Cell adhesion;Collagen;Disulfide bond;Extracellular matrix;Glycoprotein;Hydroxylation;Protease inhibitor;Reference proteome;Repeat;Secreted;Serine protease inhibitor;Signal |
| Interact With | Itself |
| Induction | INDUCTION: Transcription of COL7A1 is stimulated by TGFB1 in keratinocytes and this is possibly dependent on a putative interaction between SMADS and AP1. {ECO:0000269|PubMed:14675198}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. |
| Modified Residue | MOD_RES 2158; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 2167; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 2176; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 2179; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 2616; /note=5-hydroxylysine; /evidence=ECO:0000250; MOD_RES 2622; /note=5-hydroxylysine; /evidence=ECO:0000250; MOD_RES 2655; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 2658; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 2664; /note=4-hydroxyproline; /evidence=ECO:0000250 |
| 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:0000305}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6S4C; |
| Mapped Pubmed ID | 11953986; 12766770; 12904583; 15509587; 16537572; 16920988; 17251066; 18382769; 18676816; 18688022; 18757743; 18955559; 19651211; 19893033; 21464317; 21570975; 21677750; 21967893; 21984127; 22159717; 22613833; 22940071; 23867500; 24232570; 24385431; 25640200; 25689103; 26194911; 26203639; 26676755; 26899947; 27328306; 27856617; 27989960; 28071719; 28604778; 28892093; 29305555; 30247783; 30528862; 30802441; 32031736; 34459121; 7493021; 7774920; 7796808; 8854867; 8875894; 9151677; |
| Motif | MOTIF 1171..1173; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 2002..2004; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 2063..2065; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 2601..2603; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 2631..2633; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 295,232 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |