| IED ID | IndEnz0002016269 |
| Enzyme Type ID | protease016269 |
| Protein Name |
Fibronectin FN Cleaved into: Anastellin |
| Gene Name | Fn1 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLRGPGPGRLLLLAVLCLGTSVRCTETGKSKRQAQQIVQPPSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHVLQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGDKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFHYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYSNRNYSDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGQWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDRCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHQEVTRFDFTTSASTPVTSNTVTGETAPFSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGVPRSDDVPAPKDLQFVEVTDVKVTIMWTPPNSAVTGYRVDVLPVNLPGEHGQRLPVNRNTFAEVTGLSPGVTYLFKVFAVHQGRESKPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTVGLTRGGQPKQYNVGPMASKYPLRNLQPGSEYTVTLMAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTALEEVVHADQSSCTFENRNPGLEYNVSVYTVKDDKESAPISDTVIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDVTANSFTVHWVAPRAPITGYIIRHHAEHSAGRPRQDRVPPSRNSITLTNLNPGTEYIVTIIAVNGREESPPLIGQQSTVSDVPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYQTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTAPKNGLGPTKSQTVSPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGDEDTAELHGLRPGSEYTVSVVALHGGMESQPLIGVQSTAIPAPTNLKFTQVSPTTLTAQWTAPSVKLTGYRVRVTPKEKTGPMKEINLSPDSTSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRTISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVVIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTNPGYDTENGIQLPGTSHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALHNQRRHKVREEVVTVGNTVNEGLNQPTDDSCFDPYTVSHYAVGEEWERLSDSGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYHQRTNTNVNCPIECFMPLDVQADRDDSRE |
| Enzyme Length | 2477 |
| Uniprot Accession Number | P04937 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 906..1171 |
| EC Number | |
| Enzyme Function | FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). {ECO:0000250|UniProtKB:P02751, ECO:0000250|UniProtKB:P11276}.; FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. {ECO:0000250|UniProtKB:P02751}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (3); Chain (2); Cross-link (3); DNA binding (1); Disulfide bond (30); Domain (31); Glycosylation (9); Modified residue (6); Motif (2); Region (7); Sequence conflict (3); Signal peptide (1) |
| Keywords | Acute phase;Alternative splicing;Angiogenesis;Cell adhesion;Cell shape;Direct protein sequencing;Disulfide bond;Extracellular matrix;Glycoprotein;Heparin-binding;Isopeptide bond;Oxidation;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Sulfation |
| Interact With | P34901 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. |
| Modified Residue | MOD_RES 285; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 875; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 880; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 2392; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 2454; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P02751; MOD_RES 2475; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000250|UniProtKB:P11276}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02751}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000250|UniProtKB:P02751}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000250|UniProtKB:P11276}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia. {ECO:0000250|UniProtKB:P07589}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:26479776 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10082755; 10634931; 10640397; 11025758; 11352844; 11456126; 11682445; 11698153; 11768240; 11819312; 11907153; 11914376; 11928811; 12065530; 12127979; 12160302; 12218318; 12372417; 12388756; 12482021; 12619935; 12651615; 12679595; 12716757; 12884040; 14587027; 14656002; 14986037; 15068706; 15502483; 15539768; 15604136; 15627306; 15677310; 15677465; 15833739; 15980055; 16159961; 16316526; 16534777; 16572112; 16669970; 17021600; 17065553; 17252537; 17324142; 17609505; 17715430; 17953369; 18039280; 18379124; 18723004; 19097859; 19172391; 19366727; 19546347; 19607919; 19695229; 19804410; 19914391; 20049771; 20380796; 20810141; 20942814; 21098642; 21099277; 21141136; 21586275; 21613793; 21940672; 22228707; 22732364; 22736507; 22759963; 22812390; 22897220; 22900368; 22904348; 22937115; 23211306; 23269647; 23383330; 23940049; 24691542; 24752318; 25028133; 25192797; 25375034; 25674202; 26093969; 26728369; 27053343; 27530924; 27572112; 28712960; 30926678; 31760535; 32910242; 34729793; 7806580; 9700094; |
| Motif | MOTIF 1614..1616; /note=Cell attachment site; MOTIF 2181..2183; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 272,511 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |