P04937
uniprot
P04937
canonical
amino_acid_sequence
MLRGPGPGRLLLLAVLCLGTSVRCTETGKSKRQAQQIVQPPSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHVLQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGDKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFHYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYSNRNYSDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGQWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDRCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHQEVTRFDFTTSASTPVTSNTVTGETAPFSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGVPRSDDVPAPKDLQFVEVTDVKVTIMWTPPNSAVTGYRVDVLPVNLPGEHGQRLPVNRNTFAEVTGLSPGVTYLFKVFAVHQGRESKPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTVGLTRGGQPKQYNVGPMASKYPLRNLQPGSEYTVTLMAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTALEEVVHADQSSCTFENRNPGLEYNVSVYTVKDDKESAPISDTVIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDVTANSFTVHWVAPRAPITGYIIRHHAEHSAGRPRQDRVPPSRNSITLTNLNPGTEYIVTIIAVNGREESPPLIGQQSTVSDVPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYQTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTAPKNGLGPTKSQTVSPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGDEDTAELHGLRPGSEYTVSVVALHGGMESQPLIGVQSTAIPAPTNLKFTQVSPTTLTAQWTAPSVKLTGYRVRVTPKEKTGPMKEINLSPDSTSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRTISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVVIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTNPGYDTENGIQLPGTSHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALHNQRRHKVREEVVTVGNTVNEGLNQPTDDSCFDPYTVSHYAVGEEWERLSDSGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYHQRTNTNVNCPIECFMPLDVQADRDDSRE
uniprot
proteins
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}.; FUNCTION: Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling. {ECO:0000250|UniProtKB:P11276}.
uniprot
proteins
mass_dalton
272511
uniprot
proteins
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}.
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2445560
uniprot
proteins
pubmed
26479776
uniprot
proteins
pubmed
3119323
uniprot
proteins
pubmed
3863113
uniprot
proteins
pubmed
6089177
uniprot
proteins
pubmed
6317187
uniprot
proteins
pubmed
7519849
uniprot
proteins
sequence_length
2477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11276}. Secreted {ECO:0000250|UniProtKB:P11276}.
uniprot
proteins