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Protein

Fibrillin-1

Gene

Fbn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (By similarity). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (PubMed:20855508). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca2+ signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1. Binds heparin and this interaction plays an important role in the assembly of microfibrils (By similarity).By similarity2 Publications
Asprosin: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHormone
LigandCalcium

Enzyme and pathway databases

ReactomeiR-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1566948 Elastic fibre formation
R-MMU-2129379 Molecules associated with elastic fibres
R-MMU-216083 Integrin cell surface interactions
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-8957275 Post-translational protein phosphorylation

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillin-1
Cleaved into the following chain:
AsprosinBy similarity
Gene namesi
Name:Fbn1
Synonyms:Fbn-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:95489 Fbn1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

Neonatal lethality due to ruptured aortic aneurysm, impaired pulmonary function and/or diaphragmatic collapse. Neonatal aorta show a disorganized and poorly developed medial layer but normal levels of elastin cross-links.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24By similarityAdd BLAST24
PropeptideiPRO_000043688325 – 44By similarityAdd BLAST20
ChainiPRO_000000758245 – 2733Fibrillin-1By similarityAdd BLAST2689
ChainiPRO_00004368842734 – 2873AsprosinBy similarityAdd BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi59 ↔ 68By similarity
Disulfide bondi67 ↔ 80By similarity
Disulfide bondi85 ↔ 94PROSITE-ProRule annotation
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Disulfide bondi102 ↔ 111PROSITE-ProRule annotation
Disulfide bondi119 ↔ 129PROSITE-ProRule annotation
Disulfide bondi123 ↔ 134PROSITE-ProRule annotation
Disulfide bondi136 ↔ 145PROSITE-ProRule annotation
Disulfide bondi150 ↔ 160PROSITE-ProRule annotation
Disulfide bondi154 ↔ 166PROSITE-ProRule annotation
Disulfide bondi168 ↔ 177PROSITE-ProRule annotation
Disulfide bondi250 ↔ 262PROSITE-ProRule annotation
Disulfide bondi257 ↔ 271PROSITE-ProRule annotation
Disulfide bondi273 ↔ 286PROSITE-ProRule annotation
Disulfide bondi292 ↔ 304PROSITE-ProRule annotation
Disulfide bondi299 ↔ 313PROSITE-ProRule annotation
Disulfide bondi315 ↔ 328PROSITE-ProRule annotation
Glycosylationi450N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi455 ↔ 467PROSITE-ProRule annotation
Disulfide bondi462 ↔ 476PROSITE-ProRule annotation
Disulfide bondi478 ↔ 490PROSITE-ProRule annotation
Disulfide bondi496 ↔ 506PROSITE-ProRule annotation
Disulfide bondi501 ↔ 515PROSITE-ProRule annotation
Disulfide bondi517 ↔ 530PROSITE-ProRule annotation
Disulfide bondi536 ↔ 548PROSITE-ProRule annotation
Disulfide bondi543 ↔ 557PROSITE-ProRule annotation
Disulfide bondi559 ↔ 572PROSITE-ProRule annotation
Disulfide bondi578 ↔ 589PROSITE-ProRule annotation
Disulfide bondi584 ↔ 598PROSITE-ProRule annotation
Disulfide bondi600 ↔ 613PROSITE-ProRule annotation
Disulfide bondi619 ↔ 630PROSITE-ProRule annotation
Disulfide bondi625 ↔ 639PROSITE-ProRule annotation
Disulfide bondi641 ↔ 654PROSITE-ProRule annotation
Disulfide bondi729 ↔ 741PROSITE-ProRule annotation
Disulfide bondi736 ↔ 750PROSITE-ProRule annotation
Disulfide bondi752 ↔ 765PROSITE-ProRule annotation
Disulfide bondi771 ↔ 783PROSITE-ProRule annotation
Disulfide bondi778 ↔ 792PROSITE-ProRule annotation
Disulfide bondi794 ↔ 807PROSITE-ProRule annotation
Disulfide bondi813 ↔ 823PROSITE-ProRule annotation
Disulfide bondi818 ↔ 832PROSITE-ProRule annotation
Disulfide bondi834 ↔ 847PROSITE-ProRule annotation
Disulfide bondi855 ↔ 877PROSITE-ProRule annotation
Disulfide bondi864 ↔ 889PROSITE-ProRule annotation
Disulfide bondi878 ↔ 892PROSITE-ProRule annotation
Disulfide bondi898 ↔ 910PROSITE-ProRule annotation
Disulfide bondi916 ↔ 928PROSITE-ProRule annotation
Disulfide bondi923 ↔ 937PROSITE-ProRule annotation
Disulfide bondi939 ↔ 952PROSITE-ProRule annotation
Disulfide bondi1034 ↔ 1046PROSITE-ProRule annotation
Disulfide bondi1041 ↔ 1055PROSITE-ProRule annotation
Disulfide bondi1057 ↔ 1070PROSITE-ProRule annotation
Glycosylationi1069N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1076 ↔ 1088PROSITE-ProRule annotation
Disulfide bondi1083 ↔ 1097PROSITE-ProRule annotation
Disulfide bondi1099 ↔ 1113PROSITE-ProRule annotation
Disulfide bondi1119 ↔ 1131PROSITE-ProRule annotation
Disulfide bondi1126 ↔ 1140PROSITE-ProRule annotation
Disulfide bondi1142 ↔ 1155PROSITE-ProRule annotation
Glycosylationi1151N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1161 ↔ 1173PROSITE-ProRule annotation
Disulfide bondi1168 ↔ 1182PROSITE-ProRule annotation
Disulfide bondi1184 ↔ 1197PROSITE-ProRule annotation
Disulfide bondi1203 ↔ 1214PROSITE-ProRule annotation
Disulfide bondi1210 ↔ 1223PROSITE-ProRule annotation
Disulfide bondi1225 ↔ 1238PROSITE-ProRule annotation
Disulfide bondi1244 ↔ 1256PROSITE-ProRule annotation
Disulfide bondi1251 ↔ 1265PROSITE-ProRule annotation
Disulfide bondi1267 ↔ 1280PROSITE-ProRule annotation
Disulfide bondi1286 ↔ 1298PROSITE-ProRule annotation
Disulfide bondi1293 ↔ 1307PROSITE-ProRule annotation
Disulfide bondi1309 ↔ 1322PROSITE-ProRule annotation
Disulfide bondi1328 ↔ 1341PROSITE-ProRule annotation
Disulfide bondi1335 ↔ 1350PROSITE-ProRule annotation
Disulfide bondi1352 ↔ 1363PROSITE-ProRule annotation
Disulfide bondi1369 ↔ 1382PROSITE-ProRule annotation
Glycosylationi1371N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1376 ↔ 1391PROSITE-ProRule annotation
Disulfide bondi1393 ↔ 1404PROSITE-ProRule annotation
Disulfide bondi1410 ↔ 1422PROSITE-ProRule annotation
Disulfide bondi1417 ↔ 1431PROSITE-ProRule annotation
Disulfide bondi1433 ↔ 1446PROSITE-ProRule annotation
Disulfide bondi1452 ↔ 1463PROSITE-ProRule annotation
Disulfide bondi1458 ↔ 1472PROSITE-ProRule annotation
Disulfide bondi1474 ↔ 1487PROSITE-ProRule annotation
Glycosylationi1486N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1493 ↔ 1504PROSITE-ProRule annotation
Disulfide bondi1499 ↔ 1513PROSITE-ProRule annotation
Disulfide bondi1515 ↔ 1528PROSITE-ProRule annotation
Disulfide bondi1536 ↔ 1564PROSITE-ProRule annotation
Disulfide bondi1551 ↔ 1576PROSITE-ProRule annotation
Disulfide bondi1565 ↔ 1579PROSITE-ProRule annotation
Disulfide bondi1566 ↔ 1591PROSITE-ProRule annotation
Glycosylationi1583N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1612 ↔ 1624PROSITE-ProRule annotation
Disulfide bondi1619 ↔ 1633PROSITE-ProRule annotation
Disulfide bondi1635 ↔ 1648PROSITE-ProRule annotation
Disulfide bondi1654 ↔ 1665PROSITE-ProRule annotation
Disulfide bondi1660 ↔ 1674PROSITE-ProRule annotation
Glycosylationi1671N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1676 ↔ 1689PROSITE-ProRule annotation
Glycosylationi1705N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1715N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1772 ↔ 1784PROSITE-ProRule annotation
Disulfide bondi1779 ↔ 1793PROSITE-ProRule annotation
Disulfide bondi1795 ↔ 1808PROSITE-ProRule annotation
Disulfide bondi1814 ↔ 1826PROSITE-ProRule annotation
Disulfide bondi1820 ↔ 1835PROSITE-ProRule annotation
Disulfide bondi1837 ↔ 1849PROSITE-ProRule annotation
Disulfide bondi1855 ↔ 1867PROSITE-ProRule annotation
Disulfide bondi1862 ↔ 1876PROSITE-ProRule annotation
Disulfide bondi1878 ↔ 1891PROSITE-ProRule annotation
Disulfide bondi1897 ↔ 1907PROSITE-ProRule annotation
Disulfide bondi1902 ↔ 1916PROSITE-ProRule annotation
Glycosylationi1904N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1918 ↔ 1930PROSITE-ProRule annotation
Disulfide bondi1936 ↔ 1949PROSITE-ProRule annotation
Disulfide bondi1944 ↔ 1958PROSITE-ProRule annotation
Disulfide bondi1960 ↔ 1973PROSITE-ProRule annotation
Disulfide bondi1979 ↔ 1991PROSITE-ProRule annotation
Disulfide bondi1986 ↔ 2000PROSITE-ProRule annotation
Disulfide bondi2002 ↔ 2013PROSITE-ProRule annotation
Disulfide bondi2019 ↔ 2031PROSITE-ProRule annotation
Disulfide bondi2026 ↔ 2040PROSITE-ProRule annotation
Disulfide bondi2042 ↔ 2055PROSITE-ProRule annotation
Disulfide bondi2063 ↔ 2085PROSITE-ProRule annotationBy similarity
Disulfide bondi2072 ↔ 2098PROSITE-ProRule annotationBy similarity
Glycosylationi2079N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2086 ↔ 2101PROSITE-ProRule annotationBy similarity
Disulfide bondi2087 ↔ 2113PROSITE-ProRule annotationBy similarity
Disulfide bondi2133 ↔ 2144PROSITE-ProRule annotation
Disulfide bondi2139 ↔ 2153PROSITE-ProRule annotation
Disulfide bondi2155 ↔ 2166PROSITE-ProRule annotation
Disulfide bondi2172 ↔ 2183PROSITE-ProRule annotation
Disulfide bondi2178 ↔ 2192PROSITE-ProRule annotation
Glycosylationi2180N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2194 ↔ 2206PROSITE-ProRule annotation
Disulfide bondi2212 ↔ 2223PROSITE-ProRule annotation
Disulfide bondi2219 ↔ 2232PROSITE-ProRule annotation
Disulfide bondi2234 ↔ 2247PROSITE-ProRule annotation
Disulfide bondi2253 ↔ 2267PROSITE-ProRule annotation
Disulfide bondi2260 ↔ 2276PROSITE-ProRule annotation
Disulfide bondi2278 ↔ 2291PROSITE-ProRule annotation
Disulfide bondi2297 ↔ 2309PROSITE-ProRule annotation
Disulfide bondi2304 ↔ 2318PROSITE-ProRule annotation
Disulfide bondi2320 ↔ 2333PROSITE-ProRule annotation
Disulfide bondi2408 ↔ 2420PROSITE-ProRule annotation
Disulfide bondi2415 ↔ 2429PROSITE-ProRule annotation
Disulfide bondi2431 ↔ 2444PROSITE-ProRule annotation
Disulfide bondi2450 ↔ 2461PROSITE-ProRule annotation
Disulfide bondi2457 ↔ 2470PROSITE-ProRule annotation
Disulfide bondi2472 ↔ 2485PROSITE-ProRule annotation
Disulfide bondi2491 ↔ 2502PROSITE-ProRule annotation
Disulfide bondi2498 ↔ 2511PROSITE-ProRule annotation
Disulfide bondi2513 ↔ 2524PROSITE-ProRule annotation
Disulfide bondi2530 ↔ 2543PROSITE-ProRule annotation
Disulfide bondi2537 ↔ 2552PROSITE-ProRule annotation
Disulfide bondi2554 ↔ 2567PROSITE-ProRule annotation
Disulfide bondi2573 ↔ 2583PROSITE-ProRule annotation
Disulfide bondi2579 ↔ 2592PROSITE-ProRule annotation
Disulfide bondi2594 ↔ 2607PROSITE-ProRule annotation
Disulfide bondi2613 ↔ 2624PROSITE-ProRule annotation
Disulfide bondi2619 ↔ 2633PROSITE-ProRule annotation
Disulfide bondi2635 ↔ 2648PROSITE-ProRule annotation
Disulfide bondi2654 ↔ 2665PROSITE-ProRule annotation
Disulfide bondi2661 ↔ 2674PROSITE-ProRule annotation
Disulfide bondi2676 ↔ 2688PROSITE-ProRule annotation
Modified residuei2704PhosphoserineBy similarity1
Modified residuei2705PhosphoserineCombined sources1
Modified residuei2711PhosphoserineCombined sources1
Glycosylationi2736N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2752N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2769N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Fibrillin-1: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils. The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide. Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils.By similarity
Fibrillin-1: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei44 – 45Cleavage; by furinBy similarity2
Sitei2733 – 2734Cleavage; by furinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ61554
PaxDbiQ61554
PeptideAtlasiQ61554
PRIDEiQ61554

PTM databases

iPTMnetiQ61554
PhosphoSitePlusiQ61554

Expressioni

Tissue specificityi

Asprosin: Secreted by white adipose tissue (at protein level) (PubMed:27087445). Fibrillin-1: Strongly expressed during the first week of osteoblast differentiation (PubMed:24039232).2 Publications

Developmental stagei

Asprosin: Displays circadian oscillation with an acute decrease in levels coinciding with the onset of feeding (at protein level) (PubMed:27087445).1 Publication

Gene expression databases

BgeeiENSMUSG00000027204 Expressed in 257 organ(s), highest expression level in umbilical cord
CleanExiMM_FBN1

Interactioni

Subunit structurei

Interacts with COL16A1. Interacts with integrin alpha-V/beta-3. Interacts with ADAMTS10; this interaction promotes microfibril assembly (By similarity). Interacts with THSD4; this interaction promotes fibril formation (PubMed:19940141). Interacts (via N-terminal domain) with FBLN2, FBLN4 and FBLN5. Interacts with ELN. Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5. Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner. Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts (via N-terminal domain) with MFAP2 and MFAP5. Interacts with ADAMTSL5. Interacts with MFAP4. Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ61554, 1 interactor
STRINGi10090.ENSMUSP00000028633

Structurei

3D structure databases

ProteinModelPortaliQ61554
SMRiQ61554
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 112EGF-like 1PROSITE-ProRule annotationAdd BLAST32
Domaini115 – 146EGF-like 2PROSITE-ProRule annotationAdd BLAST32
Domaini147 – 178EGF-like 3PROSITE-ProRule annotationAdd BLAST32
Domaini184 – 236TB 1Add BLAST53
Domaini246 – 287EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini288 – 329EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini334 – 389TB 2Add BLAST56
Domaini451 – 491EGF-like 6PROSITE-ProRule annotationAdd BLAST41
Domaini492 – 531EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini532 – 573EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini574 – 614EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini615 – 655EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini661 – 713TB 3Add BLAST53
Domaini725 – 766EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini767 – 808EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini809 – 848EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini853 – 904TB 4Add BLAST52
Domaini912 – 953EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini958 – 1010TB 5Add BLAST53
Domaini1030 – 1071EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1072 – 1114EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1115 – 1156EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1157 – 1198EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1199 – 1239EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1240 – 1281EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1282 – 1323EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1324 – 1364EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1365 – 1405EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1406 – 1447EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1448 – 1488EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1489 – 1529EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1534 – 1591TB 6Add BLAST58
Domaini1608 – 1649EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1650 – 1690EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1695 – 1750TB 7Add BLAST56
Domaini1768 – 1809EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1810 – 1850EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1851 – 1892EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1893 – 1931EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini1932 – 1974EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1975 – 2014EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2015 – 2056EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2061 – 2113TB 8Add BLAST53
Domaini2129 – 2167EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini2168 – 2207EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2208 – 2248EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2249 – 2292EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini2293 – 2334EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2339 – 2392TB 9Add BLAST54
Domaini2404 – 2445EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2446 – 2486EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2487 – 2525EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini2526 – 2568EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini2569 – 2608EGF-like 45; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2609 – 2649EGF-like 46; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2650 – 2689EGF-like 47; calcium-bindingPROSITE-ProRule annotationAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 452N-terminal domainBy similarityAdd BLAST408
Regioni45 – 81Fibrillin unique N-terminal (FUN) domainBy similarityAdd BLAST37
Regioni119 – 329Interaction with MFAP4By similarityAdd BLAST211
Regioni195 – 221Hybrid domain 1By similarityAdd BLAST27
Regioni862 – 887Hybrid domain 2By similarityAdd BLAST26
Regioni1530 – 2733C-terminal domainBy similarityAdd BLAST1204

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1543 – 1545Cell attachment siteBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi402 – 448Pro-richAdd BLAST47

Sequence similaritiesi

Belongs to the fibrillin family.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217 Eukaryota
ENOG410XSTY LUCA
GeneTreeiENSGT00760000118806
HOGENOMiHOG000231768
HOVERGENiHBG005643
InParanoidiQ61554
KOiK06825
OMAiRPPVEYP
OrthoDBiEOG091G002H
PhylomeDBiQ61554
TreeFamiTF316849

Family and domain databases

Gene3Di3.90.290.10, 9 hits
InterProiView protein in InterPro
IPR026823 cEGF
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR011398 FBN
IPR009030 Growth_fac_rcpt_cys_sf
IPR017878 TB_dom
IPR036773 TB_dom_sf
PANTHERiPTHR24039 PTHR24039, 1 hit
PfamiView protein in Pfam
PF12662 cEGF, 1 hit
PF07645 EGF_CA, 41 hits
PF00683 TB, 9 hits
SMARTiView protein in SMART
SM00181 EGF, 46 hits
SM00179 EGF_CA, 44 hits
SUPFAMiSSF57184 SSF57184, 11 hits
SSF57581 SSF57581, 9 hits
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 43 hits
PS00022 EGF_1, 2 hits
PS01186 EGF_2, 38 hits
PS50026 EGF_3, 45 hits
PS01187 EGF_CA, 43 hits
PS51364 TB, 9 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61554-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRGGLLEVA LAFALLLESY TSHGADANLE AGSLKETRAN RAKRRGGGGH
60 70 80 90 100
DALKGPNVCG SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC
110 120 130 140 150
TCPSGQISPS CGSRSIQHCS IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC
160 170 180 190 200
ESGCLNGGRC VAPNRCACTY GFTGPQCERD YRTGPCFTVV SNQMCQGQLS
210 220 230 240 250
GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR TGACQDVDEC
260 270 280 290 300
QAIPGMCQGG NCINTVGSFE CKCPAGHKFN EVSQKCEDID ECSTIPGVCD
310 320 330 340 350
GGECTNTVSS YFCKCPPGFY TSPDGTRCVD VRPGYCYTAL ANGRCSNQLP
360 370 380 390 400
QSITKMQCCC DLGRCWSPGV TVAPEMCPIR STEDFNKLCS VPLVIPGRPE
410 420 430 440 450
YPPPPIGPLP PVQPVPPGYP PGPVIPAPRP PPEYPYPSPS REPPRVLPFN
460 470 480 490 500
VTDYCQLVRY LCQNGRCIPT PGSYRCECNK GFQLDIRGEC IDVDECEKNP
510 520 530 540 550
CTGGECINNQ GSYTCHCRAG YQSTLTRTEC RDIDECLQNG RICNNGRCIN
560 570 580 590 600
TDGSFHCVCN AGFHVTRDGK NCEDMDECSI RNMCLNGMCI NEDGSFKCIC
610 620 630 640 650
KPGFQLASDG RYCKDINECE TPGICMNGRC VNTDGSYRCE CFPGLAVGLD
660 670 680 690 700
GRVCVDTHMR STCYGGYRRG QCVKPLFGAV TKSECCCAST EYAFGEPCQP
710 720 730 740 750
CPAQNSAEYQ ALCSSGPGMT SAGTDINECA LDPDICPNGI CENLRGTYKC
760 770 780 790 800
ICNSGYEVDI TGKNCVDINE CVLNSLLCDN GQCRNTPGSF VCTCPKGFVY
810 820 830 840 850
KPDLKTCEDI DECESSPCIN GVCKNSPGSF ICECSPESTL DPTKTICIET
860 870 880 890 900
IKGTCWQTVI DGRCEINING ATLKSECCSS LGAAWGSPCT ICQLDPICGK
910 920 930 940 950
GFSRIKGTQC EDINECEVFP GVCKNGLCVN SRGSFKCECP NGMTLDATGR
960 970 980 990 1000
ICLDIRLETC FLKYDDEECT LPIAGRHRMD ACCCSVGAAW GTEECEECPL
1010 1020 1030 1040 1050
RNSREYEELC PRGPGFATKD ITNGKPFFKD INECKMIPSL CTHGKCRNTI
1060 1070 1080 1090 1100
GSFKCRCDSG FALDSEERNC TDIDECRISP DLCGRGQCVN TPGDFECKCD
1110 1120 1130 1140 1150
EGYESGFMMM KNCMDIDECQ RDPLLCRGGI CHNTEGSYRC ECPPGHQLSP
1160 1170 1180 1190 1200
NISACIDINE CELSANLCPH GRCVNLIGKY QCACNPGYHP THDRLFCVDI
1210 1220 1230 1240 1250
DECSIMNGGC ETFCTNSDGS YECSCQPGFA LMPDQRSCTD IDECEDNPNI
1260 1270 1280 1290 1300
CDGGQCTNIP GEYRCLCYDG FMASEDMKTC VDVNECDLNP NICLSGTCEN
1310 1320 1330 1340 1350
TKGSFICHCD MGYSGKKGKT GCTDINECEI GAHNCGRHAV CTNTAGSFKC
1360 1370 1380 1390 1400
SCSPGWIGDG IKCTDLDECS NGTHMCSQHA DCKNTMGSYR CLCKDGYTGD
1410 1420 1430 1440 1450
GFTCTDLDEC SENLNLCGNG QCLNAPGGYR CECDMGFVPS ADGKACEDID
1460 1470 1480 1490 1500
ECSLPNICVF GTCHNLPGLF RCECEIGYEL DRSGGNCTDV NECLDPTTCI
1510 1520 1530 1540 1550
SGNCVNTPGS YTCDCPPDFE LNPTRVGCVD TRSGNCYLDI RPRGDNGDTA
1560 1570 1580 1590 1600
CSNEIGVGVS KASCCCSLGK AWGTPCELCP SVNTSEYKIL CPGGEGFRPN
1610 1620 1630 1640 1650
PITVILEDID ECQELPGLCQ GGKCINTFGS FQCRCPTGYY LNEDTRVCDD
1660 1670 1680 1690 1700
VNECETPGIC GPGTCYNTVG NYTCICPPDY MQVNGGNNCM DMRRSLCYRN
1710 1720 1730 1740 1750
YYADNQTCDG ELLFNMTKKM CCCSYNIGRA WNKPCEQCPI PSTDEFATLC
1760 1770 1780 1790 1800
GSQRPGFVID IYTGLPVDID ECREIPGVCE NGVCINMVGS FRCECPVGFF
1810 1820 1830 1840 1850
YNDKLLVCED IDECQNGPVC QRNAECINTA GSYRCDCKPG YRLTSTGQCN
1860 1870 1880 1890 1900
DRNECQEIPN ICSHGQCIDT VGSFYCLCHT GFKTNVDQTM CLDINECERD
1910 1920 1930 1940 1950
ACGNGTCRNT IGSFNCRCNH GFILSHNNDC IDVDECATGN GNLCRNGQCV
1960 1970 1980 1990 2000
NTVGSFQCRC NEGYEVAPDG RTCVDINECV LDPGKCAPGT CQNLDGSYRC
2010 2020 2030 2040 2050
ICPPGYSLQN DKCEDIDECV EEPEICALGT CSNTEGSFKC LCPEGFSLSS
2060 2070 2080 2090 2100
TGRRCQDLRM SYCYAKFEGG KCSSPKSRNH SKQECCCALK GEGWGDPCEL
2110 2120 2130 2140 2150
CPTEPDEAFR QICPFGSGII VGPDDSAVDM DECKEPDVCR HGQCINTDGS
2160 2170 2180 2190 2200
YRCECPFGYI LEGNECVDTD ECSVGNPCGN GTCKNVIGGF ECTCEEGFEP
2210 2220 2230 2240 2250
GPMMTCEDIN ECAQNPLLCA FRCVNTYGSY ECKCPVGYVL REDRRMCKDE
2260 2270 2280 2290 2300
DECAEGKHDC TEKQMECKNL IGTYMCICGP GYQRRPDGEG CIDENECQTK
2310 2320 2330 2340 2350
PGICENGRCL NTLGSYTCEC NDGFTASPTQ DECLDNREGY CFSEVLQNMC
2360 2370 2380 2390 2400
QIGSSNRNPV TKSECCCDGG RGWGPHCEIC PFEGTVAYKK LCPHGRGFMT
2410 2420 2430 2440 2450
NGADIDECKV IHDVCRNGEC VNDRGSYHCI CKTGYTPDIT GTACVDLNEC
2460 2470 2480 2490 2500
NQAPKPCNFI CKNTEGSYQC SCPKGYILQE DGRSCKDLDE CATKQHNCQF
2510 2520 2530 2540 2550
LCVNTIGGFT CKCPPGFTQH HTACIDNNEC TSDINLCGSK GVCQNTPGSF
2560 2570 2580 2590 2600
TCECQRGFSL DQSGASCEDV DECEGNHRCQ HGCQNIIGGY RCSCPQGYLQ
2610 2620 2630 2640 2650
HYQWNQCVDE NECLSAHVCG GASCHNTLGS YKCMCPTGFQ YEQFSGGCQD
2660 2670 2680 2690 2700
INECGSSQAP CSYGCSNTEG GYLCGCPPGY FRIGQGHCVS GMGMGRGGPE
2710 2720 2730 2740 2750
PPASSEMDDN SLSPEACYEC KINGYPKRGR KRRSTNETDA SDIQDGSEME
2760 2770 2780 2790 2800
ANVSLASWDV EKPASFAFNI SHVNNKVRIL ELLPALTTLM NHNRYLIESG
2810 2820 2830 2840 2850
NEDGFFKINQ KEGVSYLHFT KKKPVAGTYS LQISSTPLYK KKELNQLEDR
2860 2870
YDKDYLSGEL GDNLKMKIQI LLH
Length:2,873
Mass (Da):312,298
Last modified:July 6, 2016 - v2
Checksum:i11C09D2C1ADE7292
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti120S → N in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti427A → V in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti427A → V in AAA64217 (Ref. 2) Curated1
Sequence conflicti435 – 438PYPS → LY in AAA56840 (PubMed:7829516).Curated4
Sequence conflicti449F → V in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti566 – 568TRD → SSE in AAA56840 (PubMed:7829516).Curated3
Sequence conflicti579 – 585SIRNMCL → RTPNMCP in AAA56840 (PubMed:7829516).Curated7
Sequence conflicti579S → R in AAA64217 (Ref. 2) Curated1
Sequence conflicti653V → W in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti662T → S in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1137S → T in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1243E → Q in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1427G → A in AAA64217 (Ref. 2) Curated1
Sequence conflicti1516P → S in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1539D → N in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1696L → I in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1728G → R in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1821Q → L in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti1886V → E in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2048 – 2051LSST → WSSS in AAA56840 (PubMed:7829516).Curated4
Sequence conflicti2346 – 2347LQ → FE in AAA56840 (PubMed:7829516).Curated2
Sequence conflicti2368D → V in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2375P → L in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2405I → V in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2443A → S in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2474K → N in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2542V → I in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2637T → A in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2689V → L in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2698G → A in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2774N → S in AAA56840 (PubMed:7829516).Curated1
Sequence conflicti2823 – 2824KP → NA in AAA56840 (PubMed:7829516).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29454 mRNA Translation: AAA56840.1
U22493 mRNA Translation: AAA64217.1
AL844547 Genomic DNA No translation available.
AL928930 Genomic DNA No translation available.
CCDSiCCDS16676.1
PIRiA55624
RefSeqiNP_032019.2, NM_007993.2
XP_006498810.1, XM_006498747.1
UniGeneiMm.271644

Genome annotation databases

EnsembliENSMUST00000028633; ENSMUSP00000028633; ENSMUSG00000027204
ENSMUST00000103234; ENSMUSP00000099524; ENSMUSG00000027204
GeneIDi14118
KEGGimmu:14118
UCSCiuc008mco.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29454 mRNA Translation: AAA56840.1
U22493 mRNA Translation: AAA64217.1
AL844547 Genomic DNA No translation available.
AL928930 Genomic DNA No translation available.
CCDSiCCDS16676.1
PIRiA55624
RefSeqiNP_032019.2, NM_007993.2
XP_006498810.1, XM_006498747.1
UniGeneiMm.271644

3D structure databases

ProteinModelPortaliQ61554
SMRiQ61554
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61554, 1 interactor
STRINGi10090.ENSMUSP00000028633

PTM databases

iPTMnetiQ61554
PhosphoSitePlusiQ61554

Proteomic databases

MaxQBiQ61554
PaxDbiQ61554
PeptideAtlasiQ61554
PRIDEiQ61554

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028633; ENSMUSP00000028633; ENSMUSG00000027204
ENSMUST00000103234; ENSMUSP00000099524; ENSMUSG00000027204
GeneIDi14118
KEGGimmu:14118
UCSCiuc008mco.1 mouse

Organism-specific databases

CTDi2200
MGIiMGI:95489 Fbn1

Phylogenomic databases

eggNOGiKOG1217 Eukaryota
ENOG410XSTY LUCA
GeneTreeiENSGT00760000118806
HOGENOMiHOG000231768
HOVERGENiHBG005643
InParanoidiQ61554
KOiK06825
OMAiRPPVEYP
OrthoDBiEOG091G002H
PhylomeDBiQ61554
TreeFamiTF316849

Enzyme and pathway databases

ReactomeiR-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1566948 Elastic fibre formation
R-MMU-2129379 Molecules associated with elastic fibres
R-MMU-216083 Integrin cell surface interactions
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-8957275 Post-translational protein phosphorylation

Miscellaneous databases

PROiPR:Q61554
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027204 Expressed in 257 organ(s), highest expression level in umbilical cord
CleanExiMM_FBN1

Family and domain databases

Gene3Di3.90.290.10, 9 hits
InterProiView protein in InterPro
IPR026823 cEGF
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR011398 FBN
IPR009030 Growth_fac_rcpt_cys_sf
IPR017878 TB_dom
IPR036773 TB_dom_sf
PANTHERiPTHR24039 PTHR24039, 1 hit
PfamiView protein in Pfam
PF12662 cEGF, 1 hit
PF07645 EGF_CA, 41 hits
PF00683 TB, 9 hits
SMARTiView protein in SMART
SM00181 EGF, 46 hits
SM00179 EGF_CA, 44 hits
SUPFAMiSSF57184 SSF57184, 11 hits
SSF57581 SSF57581, 9 hits
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 43 hits
PS00022 EGF_1, 2 hits
PS01186 EGF_2, 38 hits
PS50026 EGF_3, 45 hits
PS01187 EGF_CA, 43 hits
PS51364 TB, 9 hits
ProtoNetiSearch...

Entry informationi

Entry nameiFBN1_MOUSE
AccessioniPrimary (citable) accession number: Q61554
Secondary accession number(s): A2AQ53, Q60826
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 6, 2016
Last modified: November 7, 2018
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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