P11276 · FINC_MOUSE
- ProteinFibronectin
- GeneFn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2477 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape 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 (PubMed:21768292).
Participates in the regulation of type I collagen deposition by osteoblasts (PubMed:21768292).
Acts as a ligand for the Lilrb4a receptor, inhibiting Fcgr1/CD64-mediated monocyte activation (PubMed:34089617).
Anastellin
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 906-1171 | |||||
Sequence: VPPPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVT |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFibronectin
- Short namesFN
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP11276
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 35 | 99% decrease in cross-linking efficiency; when associated with A-36 and A-48. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 35 | 65% decrease in cross-linking efficiency; when associated with L-36. | ||||
Sequence: Q → L | ||||||
Mutagenesis | 36 | 99% decrease in cross-linking efficiency; when associated with A-35 and A-48. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 36 | 65% decrease in cross-linking efficiency; when associated with L-35. | ||||
Sequence: Q → L | ||||||
Mutagenesis | 48 | 99% decrease in cross-linking efficiency; when associated with A-35 and A-36. | ||||
Sequence: Q → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 94 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, modified residue, chain, cross-link, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MLRGPGPGRLLLLAVLCLGTSVRCTEAGKSKR | ||||||
Modified residue | 33 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000019236 | 33-2477 | Fibronectin | |||
Sequence: QAQQIVQPQSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHALQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSASTPVTSNTVTGETAPYSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGTPRSDNVPPPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTSLEEVVHADQSSCTFENLNPGLEYNVSVYTVKDDKESAPISDTVVPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSDIPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTTPKNGLGPSKTKTASPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIRELFPAPDGEDDTAELQGLRPGSEYTVSVVALHDDMESQPLIGIQSTAIPAPTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTENGIQLPGTTHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALQNQRRHKVREEVVTVGNAVSEGLNQPTDDSCFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYNQRTNTNVNCPIECFMPLDVQADRDDSRE | ||||||
Cross-link | 35 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) | ||||
Sequence: Q | ||||||
Cross-link | 36 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) | ||||
Sequence: Q | ||||||
Cross-link | 48 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) | ||||
Sequence: Q | ||||||
Disulfide bond | 53↔79 | |||||
Sequence: CFDNGKHYQINQQWERTYLGNALVCTC | ||||||
Disulfide bond | 77↔88 | |||||
Sequence: CTCYGGSRGFNC | ||||||
Disulfide bond | 98↔126 | |||||
Sequence: CFDKYTGNTYKVGDTYERPKDSMIWDCTC | ||||||
Disulfide bond | 124↔136 | |||||
Sequence: CTCIGAGRGRISC | ||||||
Disulfide bond | 142↔170 | |||||
Sequence: CHEGGQSYKIGDKWRRPHETGGYMLECLC | ||||||
Disulfide bond | 168↔180 | |||||
Sequence: CLCLGNGKGEWTC | ||||||
Disulfide bond | 187↔216 | |||||
Sequence: CFDHAAGTSYVVGETWEKPYQGWMMVDCTC | ||||||
Disulfide bond | 214↔226 | |||||
Sequence: CTCLGEGNGRITC | ||||||
Disulfide bond | 232↔261 | |||||
Sequence: CNDQDTRTSYRIGDTWSKKDNRGNLLQCVC | ||||||
Disulfide bond | 259↔271 | |||||
Sequence: CVCTGNGRGEWKC | ||||||
Modified residue | 285 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 308↔335 | |||||
Sequence: CVTDSGVVYSVGMQWLKSQGNKQMLCTC | ||||||
Disulfide bond | 333↔342 | |||||
Sequence: CTCLGNGVSC | ||||||
Disulfide bond | 360↔386 | |||||
Sequence: CVLPFTYNGRTFYSCTTEGRQDGHLWC | ||||||
Disulfide bond | 374↔401 | |||||
Sequence: CTTEGRQDGHLWCSTTSNYEQDQKYSFC | ||||||
Disulfide bond | 420↔446 | |||||
Sequence: CHFPFLYNNRNYTDCTSEGRRDNMKWC | ||||||
Glycosylation | 430 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 434↔461 | |||||
Sequence: CTSEGRRDNMKWCGTTQNYDADQKFGFC | ||||||
Disulfide bond | 470↔498 | |||||
Sequence: CTTNEGVMYRIGDQWDKQHDLGHMMRCTC | ||||||
Disulfide bond | 496↔508 | |||||
Sequence: CTCVGNGRGEWAC | ||||||
Disulfide bond | 518↔545 | |||||
Sequence: CIVDDITYNVNDTFHKRHEEGHMLNCTC | ||||||
Glycosylation | 528 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 542 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 543↔555 | |||||
Sequence: CTCFGQGRGRWKC | ||||||
Disulfide bond | 561↔589 | |||||
Sequence: CQDSETRTFYQIGDSWEKFVHGVRYQCYC | ||||||
Disulfide bond | 587↔599 | |||||
Sequence: CYCYGRGIGEWHC | ||||||
Chain | PRO_0000390480 | 627-701 | Anastellin | |||
Sequence: PIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSA | ||||||
Modified residue | 875 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 876 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 880 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 1006 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1243 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2198 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2296↔2325 | |||||
Sequence: CFDPYTVSHYAIGEEWERLSDAGFKLTCQC | ||||||
Disulfide bond | 2323↔2335 | |||||
Sequence: CQCLGFGSGHFRC | ||||||
Disulfide bond | 2341↔2368 | |||||
Sequence: CHDNGVNYKIGEKWDRQGENGQRMSCTC | ||||||
Disulfide bond | 2366↔2378 | |||||
Sequence: CTCLGNGKGEFKC | ||||||
Disulfide bond | 2385↔2411 | |||||
Sequence: CYDDGKTYHVGEQWQKEYLGAICSCTC | ||||||
Modified residue | 2392 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Disulfide bond | 2409↔2420 | |||||
Sequence: CTCFGGQRGWRC | ||||||
Modified residue | 2454 | Phosphothreonine | ||||
Sequence: T | ||||||
Disulfide bond | 2458 | Interchain (with C-2462) | ||||
Sequence: C | ||||||
Disulfide bond | 2462 | Interchain (with C-2458) | ||||
Sequence: C | ||||||
Modified residue | 2475 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix
Induction
Gene expression databases
Interaction
Subunit
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 (By similarity).
Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity).
Interacts with FST3 and MYOC (By similarity).
Interacts with SVEP1 (PubMed:36792666).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P11276 | Plcg2 Q8CIH5 | 6 | EBI-641955, EBI-617954 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-91 | Fibronectin type-I 1 | ||||
Sequence: PGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESK | ||||||
Region | 53-273 | Fibrin- and heparin-binding 1 | ||||
Sequence: CFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCER | ||||||
Domain | 96-139 | Fibronectin type-I 2 | ||||
Sequence: ETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIA | ||||||
Region | 124-143 | Required for binding to Lilrb4a | ||||
Sequence: CTCIGAGRGRISCTIANRCH | ||||||
Domain | 140-183 | Fibronectin type-I 3 | ||||
Sequence: NRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPI | ||||||
Domain | 185-229 | Fibronectin type-I 4 | ||||
Sequence: EKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSR | ||||||
Domain | 230-274 | Fibronectin type-I 5 | ||||
Sequence: NRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERH | ||||||
Domain | 306-343 | Fibronectin type-I 6 | ||||
Sequence: GHCVTDSGVVYSVGMQWLKSQGNKQMLCTCLGNGVSCQ | ||||||
Region | 308-608 | Collagen-binding | ||||
Sequence: CVTDSGVVYSVGMQWLKSQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGT | ||||||
Domain | 355-403 | Fibronectin type-II 1 | ||||
Sequence: SNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTD | ||||||
Domain | 415-463 | Fibronectin type-II 2 | ||||
Sequence: SNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPM | ||||||
Domain | 468-516 | Fibronectin type-I 7 | ||||
Sequence: EICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPYSQLRD | ||||||
Domain | 516-558 | Fibronectin type-I 8 | ||||
Sequence: DQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPI | ||||||
Domain | 559-602 | Fibronectin type-I 9 | ||||
Sequence: DQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPL | ||||||
Domain | 610-717 | Fibronectin type-III 1 | ||||
Sequence: GPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSASTPVTSNTVTGETAPY | ||||||
Domain | 721-811 | Fibronectin type-III 2 | ||||
Sequence: VATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPD | ||||||
Domain | 812-903 | Fibronectin type-III 3 | ||||
Sequence: APPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGTPRS | ||||||
Domain | 908-997 | Fibronectin type-III 4 | ||||
Sequence: PPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLD | ||||||
Domain | 998-1087 | Fibronectin type-III 5 | ||||
Sequence: APTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPL | ||||||
Domain | 1088-1174 | Fibronectin type-III 6 | ||||
Sequence: RSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLS | ||||||
Domain | 1175-1269 | Fibronectin type-III 7 | ||||
Sequence: PPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTSLEEVVHADQSSCTFENLNPGLEYNVSVYTVKDDKESAPISDTVVPEVPQL | ||||||
Domain | 1270-1358 | Fibronectin type-III 8; extra domain B | ||||
Sequence: TDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVP | ||||||
Region | 1357-1630 | Cell-attachment | ||||
Sequence: VPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSDIPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKT | ||||||
Domain | 1359-1451 | Fibronectin type-III 9 | ||||
Sequence: PPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSP | ||||||
Domain | 1452-1539 | Fibronectin type-III 10 | ||||
Sequence: TGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSD | ||||||
Domain | 1540-1633 | Fibronectin type-III 11 | ||||
Sequence: IPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKTEID | ||||||
Motif | 1614-1616 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 1634-1725 | Fibronectin type-III 12 | ||||
Sequence: KPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTTPKNGLGPSKTKTASPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRP | ||||||
Region | 1661-1684 | Disordered | ||||
Sequence: GYRVTTTPKNGLGPSKTKTASPDQ | ||||||
Domain | 1726-1813 | Fibronectin type-III 13; extra domain A | ||||
Sequence: KGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIRELFPAPDGEDDTAELQGLRPGSEYTVSVVALHDDMESQPLIGIQSTAIP | ||||||
Region | 1811-2081 | Heparin-binding 2 | ||||
Sequence: AIPAPTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKT | ||||||
Domain | 1814-1907 | Fibronectin type-III 14 | ||||
Sequence: APTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPP | ||||||
Domain | 1908-1994 | Fibronectin type-III 15 | ||||
Sequence: RRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAID | ||||||
Domain | 1995-2085 | Fibronectin type-III 16 | ||||
Sequence: APSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELP | ||||||
Region | 2082-2201 | V region (type III connecting segment, IIICS) | ||||
Sequence: DELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTENGIQLPGTTHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNAST | ||||||
Motif | 2181-2183 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 2193-2287 | Fibronectin type-III 17 | ||||
Sequence: PGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALQNQRRHKVREEVVTVGNAVSEG | ||||||
Domain | 2294-2338 | Fibronectin type-I 10 | ||||
Sequence: DSCFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSS | ||||||
Region | 2296-2427 | Fibrin-binding 2 | ||||
Sequence: CFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPG | ||||||
Domain | 2339-2381 | Fibronectin type-I 11 | ||||
Sequence: KWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPH | ||||||
Domain | 2383-2426 | Fibronectin type-I 12 | ||||
Sequence: ATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. The diversity of isoforms depends on the V region and either of the two extra domain which can be either included or excluded (partially or completely for the V region).
P11276-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length2,477
- Mass (Da)272,538
- Last updated2012-10-03 v4
- Checksum24A207BE67F85585
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q4KL80 | Q4KL80_MOUSE | Fn1 | 383 | ||
Q3UHL6 | Q3UHL6_MOUSE | Fn1 | 2361 | ||
B7ZNJ1 | B7ZNJ1_MOUSE | Fn1 | 2176 | ||
A0A087WQE0 | A0A087WQE0_MOUSE | Fn1 | 71 | ||
A0A087WR50 | A0A087WR50_MOUSE | Fn1 | 2386 | ||
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 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1063 | in Ref. 6; CAA63654 | ||||
Sequence: V → A | ||||||
Sequence conflict | 1820 | in Ref. 6; CAA63654 | ||||
Sequence: F → L | ||||||
Sequence conflict | 2440 | in Ref. 7; AAA37636 | ||||
Sequence: T → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC124821 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466548 EMBL· GenBank· DDBJ | EDL00265.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC051082 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
Z22729 EMBL· GenBank· DDBJ | CAA80422.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X82402 EMBL· GenBank· DDBJ | CAA57796.1 EMBL· GenBank· DDBJ | mRNA | ||
X93167 EMBL· GenBank· DDBJ | CAA63654.1 EMBL· GenBank· DDBJ | mRNA | ||
M18194 EMBL· GenBank· DDBJ | AAA37636.1 EMBL· GenBank· DDBJ | mRNA | ||
S45680 EMBL· GenBank· DDBJ | AAB23491.1 EMBL· GenBank· DDBJ | mRNA |