A0A087WR50 · A0A087WR50_MOUSE
- ProteinFibronectin
- GeneFn1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2386 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | heparin binding | |
Biological Process | acute-phase response | |
Biological Process | cell adhesion | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameFibronectin
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionA0A087WR50
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MLRGPGPGRLLLLAVLCLGTSVRCTEA | ||||||
Chain | PRO_5015029550 | 28-2386 | Fibronectin | |||
Sequence: GKSKRQAQQIVQPQSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHALQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSASTPVTSNTVTGETAPYSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGTPRSDNVPPPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTSLEEVVHADQSSCTFENLNPGLEYNVSVYTVKDDKESAPISDTVVPAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSDIPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTTPKNGLGPSKTKTASPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIRELFPAPDGEDDTAELQGLRPGSEYTVSVVALHDDMESQPLIGIQSTAIPAPTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTENGIQLPGTTHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALQNQRRHKVREEVVTVGNAVSEGLNQPTDDSCFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYNQRTNTNVNCPIECFMPLDVQADRDDSRE | ||||||
Disulfide bond | 360↔386 | |||||
Sequence: CVLPFTYNGRTFYSCTTEGRQDGHLWC | ||||||
Disulfide bond | 374↔401 | |||||
Sequence: CTTEGRQDGHLWCSTTSNYEQDQKYSFC | ||||||
Disulfide bond | 420↔446 | |||||
Sequence: CHFPFLYNNRNYTDCTSEGRRDNMKWC | ||||||
Disulfide bond | 434↔461 | |||||
Sequence: CTSEGRRDNMKWCGTTQNYDADQKFGFC |
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7. Interacts with COMP. Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain); this interaction enhances fibronectin fibril assembly. TNFAIP6 may act as a bridging molecule between FN1 and THBS1. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth. Interacts with FST3 and MYOC. Interacts with SVEP1.
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-91 | Fibronectin type-I | ||||
Sequence: PGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESK | ||||||
Domain | 96-139 | Fibronectin type-I | ||||
Sequence: ETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIA | ||||||
Domain | 140-183 | Fibronectin type-I | ||||
Sequence: NRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPI | ||||||
Domain | 185-229 | Fibronectin type-I | ||||
Sequence: EKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSR | ||||||
Domain | 230-274 | Fibronectin type-I | ||||
Sequence: NRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERH | ||||||
Domain | 355-403 | Fibronectin type-II | ||||
Sequence: SNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTD | ||||||
Domain | 415-463 | Fibronectin type-II | ||||
Sequence: SNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPM | ||||||
Domain | 468-511 | Fibronectin type-I | ||||
Sequence: EICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPY | ||||||
Domain | 516-558 | Fibronectin type-I | ||||
Sequence: DQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPI | ||||||
Domain | 559-602 | Fibronectin type-I | ||||
Sequence: DQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPL | ||||||
Domain | 610-717 | Fibronectin type-III | ||||
Sequence: GPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSASTPVTSNTVTGETAPY | ||||||
Domain | 721-811 | Fibronectin type-III | ||||
Sequence: VATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPD | ||||||
Domain | 812-903 | Fibronectin type-III | ||||
Sequence: APPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGTPRS | ||||||
Domain | 908-997 | Fibronectin type-III | ||||
Sequence: PPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLD | ||||||
Domain | 998-1087 | Fibronectin type-III | ||||
Sequence: APTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPL | ||||||
Domain | 1088-1174 | Fibronectin type-III | ||||
Sequence: RSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLS | ||||||
Domain | 1175-1265 | Fibronectin type-III | ||||
Sequence: PPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTSLEEVVHADQSSCTFENLNPGLEYNVSVYTVKDDKESAPISDTVVPA | ||||||
Domain | 1268-1360 | Fibronectin type-III | ||||
Sequence: PPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSP | ||||||
Domain | 1361-1448 | Fibronectin type-III | ||||
Sequence: TGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSD | ||||||
Domain | 1449-1542 | Fibronectin type-III | ||||
Sequence: IPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKTEID | ||||||
Domain | 1543-1634 | Fibronectin type-III | ||||
Sequence: KPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTTPKNGLGPSKTKTASPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRP | ||||||
Region | 1570-1593 | Disordered | ||||
Sequence: GYRVTTTPKNGLGPSKTKTASPDQ | ||||||
Domain | 1635-1722 | Fibronectin type-III | ||||
Sequence: KGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIRELFPAPDGEDDTAELQGLRPGSEYTVSVVALHDDMESQPLIGIQSTAIP | ||||||
Domain | 1723-1816 | Fibronectin type-III | ||||
Sequence: APTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPP | ||||||
Domain | 1817-1903 | Fibronectin type-III | ||||
Sequence: RRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAID | ||||||
Domain | 1904-1994 | Fibronectin type-III | ||||
Sequence: APSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELP | ||||||
Domain | 2102-2196 | Fibronectin type-III | ||||
Sequence: PGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALQNQRRHKVREEVVTVGNAVSEG | ||||||
Domain | 2203-2247 | Fibronectin type-I | ||||
Sequence: DSCFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSS | ||||||
Domain | 2248-2290 | Fibronectin type-I | ||||
Sequence: KWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPH | ||||||
Domain | 2292-2332 | Fibronectin type-I | ||||
Sequence: ATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNC |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,386
- Mass (Da)262,842
- Last updated2014-10-29 v1
- ChecksumF1B372D123C2DD2E
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P11276 | FINC_MOUSE | Fn1 | 2477 | ||
Q4KL80 | Q4KL80_MOUSE | Fn1 | 383 | ||
Q3UHL6 | Q3UHL6_MOUSE | Fn1 | 2361 | ||
B7ZNJ1 | B7ZNJ1_MOUSE | Fn1 | 2176 | ||
A0A087WQE0 | A0A087WQE0_MOUSE | Fn1 | 71 | ||
A0A087WQW8 | A0A087WQW8_MOUSE | Fn1 | 160 | ||
A0A087WS56 | A0A087WS56_MOUSE | Fn1 | 2266 | ||
A0A087WS99 | A0A087WS99_MOUSE | Fn1 | 200 | ||
A0A087WSU6 | A0A087WSU6_MOUSE | Fn1 | 67 | ||
A0A087WSN6 | A0A087WSN6_MOUSE | Fn1 | 2296 | ||
B9EHT6 | B9EHT6_MOUSE | Fn1 | 2271 |
Keywords
- Technical term