| IED ID | IndEnz0002012122 |
| Enzyme Type ID | protease012122 |
| Protein Name |
von Willebrand factor vWF |
| Gene Name | VWF F8VWF |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| 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 Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | MSPTRLVRVLLALALILPGKLCTKGTVGRSSMARCSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEHSVSLIGGFQNGKRVSLSVYLGEFFDIHLFVNGTMLQGTQSISMPYASNGLYLEAEAGYYKLSSEAYGFVARIDGNGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFRTQEGTLTSDPYDFANSWALSSGEQRCKRVSPPSSPCNVSSDEVQQVLWEQCQLLKSASVFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGIVLYGWTDHSVCRPACPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLDEGHCVGSAECSCVHAGQRYPPGASLLQDCHTCICRNSLWICSNEECPGECLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDHTFSVVIETVQCADDLDAVCTRSVTVRLPGHHNSLVKLKHGGGVSMDGQDIQIPLLQGDLRIQHTVMASVRLSYGEDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRGDDFVTPAGLAEPLVEDFGNAWKLLGACENLQKQHRDPCSLNPRQARFAEEACALLTSSKFEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHIAWREPGFCALSCPQGQVYLQCGTPCNMTCRSLSYPEEDCNEVCLEGCFCPPGLYLDERGDCVPKAQCPCYYDGEIFQPEDIFSDHHTMCYCEDGFMHCTTSGGLGSLLPNPVLSSPRSHRSKRSLSCRPPMVKLVCPADNPRAEGLECAKTCQNYDLQCMSTGCVSGCLCPQGMVRHENRCVALERCPCFHQGQEYAPGETVKIDCNTCVCRDRKWNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDYCGSNPGTFRILVGNEGCSYPSVKCKKRVTILVEGGEIELFDGEVNVKKPMKDETHFEVVESGQYVILLLGKALSVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNNDFTSSSLQIEEDPVDFGNSWKVNPQCADTKKVPLDSSPAVCHNNIMKQTMVDSSCRILTSDIFQDCNRLVDPEPFLDICIYDTCSCESIGDCTCFCDTIAAYAHVCAQHGKVVAWRTATFCPQNCEERNLHENGYECEWRYNSCAPACPITCQHPEPLACPVQCVEGCHAHCPPGKILDELLQTCIDPEDCPVCEVAGRRLAPGKKIILNPSDPEHCQICHCDGVNFTCQACREPGSLVVPPTEGPIGSTTSYVEDTPEPPLHDFHCSRLLDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVASTSEVLKYTLFQIFGKIDRPEASRIALLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPENKAFVFSGVDELEQRRDEIINYLCDLAPEAPAPTQHPPMAQVTVGSELLGVSSPGPKRNSMVLDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTNTGLALQYLSEHSFSVSQGDREQVPNLVYMVTGNPASDEIKRMPGDIQVVPIGVGPHANVQELEKIGWPNAPILIHDFEMLPREAPDLVLQRCCSGEGLQIPTLSPTPDCSQPLDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPSQIGDALSFAVRYVTSEVHGARPGASKAVVILVTDVSVDSVDAAAEAARSNRVTVFPIGIGDRYSEAQLSSLAGPKAGSNMVRLQRIEDLPTVATLGNSFFHKLCSGFDRVCVDEDGNEKRPGDVWTLPDQCHTVTCLPDGQTLLKSHRVNCDRGPRPSCPNGQPPLRVEETCGCRWTCPCVCMGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQDLEVILHNGACSPGAKETCMKSIEVKHDGLSVELHSDMQMTVNGRLVSIPYVGGDMEVNVYGTIMYEVRFNHLGHIFTFTPQNNEFQLQLSPRTFASKTYGLCGICDENGANDFILRDGTVTTDWKALIQEWTVQQLGKTCQPVPEEQCPVSSSSHCQVLLSELFAECHKVLAPATFYAMCQPDSCHPKKVCEAIALYAHLCRTKGVCVDWRRANFCAMSCPPSLVYNHCEHGCPRLCEGNTSSCGDQPSEGCFCPPNQVMLEGSCVPEEACTQCISEDGVRHQFLETWVPAHQPCQICTCLSGRKVNCTLQPCPTARAPTCGPCEVARLRQNAEQCCPEYECVCDLVSCDLPPVPPCEDGLQMTLTNPGECRPNFTCACRKDECRRESPPSCPPHRTLALRKTQCCDEYECACNCVNSTVSCPLGYLASAVTNDCGCTTTTCFPDKVCVHRGTIYPVGQFWEEACDVCTCTDLEDSVMGLRVAQCSQKPCEDNCLSGFTYVLHEGECCGRCLPSACEVVIGSPRGDAQSHWKNVGSHWASPDNPCLINECVRVKEEVFVQQRNVSCPQLNVPTCPTGFQLSCKTSECCPTCHCEPLEACLLNGTIIGPGKSLMIDVCTTCRCTVQVGVISGFKLECRKTTCEACPLGYKEEKNQGECCGRCLPIACTIQLRGGQIMTLKRDETIQDGCDSHFCKVNERGEYIWEKRVTGCPPFDEHKCLAEGGKIMKIPGTCCDTCEEPECKDIIAKLQRVKVGDCKSEEEVDIHYCEGKCASKAVYSIHMEDVQDQCSCCSPTQTEPMQVPLRCTNGSLIYHEILNAMQCRCSPRKCSK |
| Enzyme Length | 2813 |
| Uniprot Accession Number | Q28295 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex, glycoprotein Ibalpha/IX/V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (34); Domain (15); Glycosylation (15); Motif (3); Propeptide (1); Region (4); Sequence conflict (8); Signal peptide (1) |
| Keywords | Blood coagulation;Cell adhesion;Cleavage on pair of basic residues;Disulfide bond;Extracellular matrix;Glycoprotein;Hemostasis;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10961880}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10961880}. Note=Localized to storage granules. |
| Modified Residue | |
| Post Translational Modification | PTM: All cysteine residues are involved in intrachain or interchain disulfide bonds. {ECO:0000250}.; PTM: N- and O-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 531..533; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 698..700; /note=Cell attachment site; /evidence=ECO:0000255; MOTIF 2507..2509; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 309,719 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |