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Protein

Fibrillin-1

Gene

FBN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively. 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. 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
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 hepathocytes. Promotes hepathocyte 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

Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-BTA-1474228. Degradation of the extracellular matrix.
R-BTA-1566948. Elastic fibre formation.
R-BTA-2129379. Molecules associated with elastic fibres.
R-BTA-216083. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillin-1
Alternative name(s):
MP340
Cleaved into the following chain:
AsprosinBy similarity
Gene namesi
Name:FBN1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componentsi: Chromosome 10, Unassembled WGS sequence

Subcellular locationi

  • Secreted By similarity

  • Note: Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequentely separated by furin.By similarity
Asprosin :
  • Secreted By similarity

  • Note: Secreted into the plasma.By similarity
Fibrillin-1 :

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • intracellular Source: GOC
  • microfibril Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24By similarityAdd BLAST24
PropeptideiPRO_000043687925 – 44By similarityAdd BLAST20
ChainiPRO_000000758045 – 2731Fibrillin-1By similarityAdd BLAST2687
ChainiPRO_00004368802732 – 2871AsprosinBy 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
Glycosylationi448N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi453 ↔ 465PROSITE-ProRule annotation
Disulfide bondi460 ↔ 474PROSITE-ProRule annotation
Disulfide bondi476 ↔ 488PROSITE-ProRule annotation
Disulfide bondi494 ↔ 504PROSITE-ProRule annotation
Disulfide bondi499 ↔ 513PROSITE-ProRule annotation
Disulfide bondi515 ↔ 528PROSITE-ProRule annotation
Disulfide bondi534 ↔ 546PROSITE-ProRule annotation
Disulfide bondi541 ↔ 555PROSITE-ProRule annotation
Disulfide bondi557 ↔ 570PROSITE-ProRule annotation
Disulfide bondi576 ↔ 587PROSITE-ProRule annotation
Disulfide bondi582 ↔ 596PROSITE-ProRule annotation
Disulfide bondi598 ↔ 611PROSITE-ProRule annotation
Disulfide bondi617 ↔ 628PROSITE-ProRule annotation
Disulfide bondi623 ↔ 637PROSITE-ProRule annotation
Disulfide bondi639 ↔ 652PROSITE-ProRule annotation
Disulfide bondi727 ↔ 739PROSITE-ProRule annotation
Disulfide bondi734 ↔ 748PROSITE-ProRule annotation
Disulfide bondi750 ↔ 763PROSITE-ProRule annotation
Disulfide bondi769 ↔ 781PROSITE-ProRule annotation
Disulfide bondi776 ↔ 790PROSITE-ProRule annotation
Disulfide bondi792 ↔ 805PROSITE-ProRule annotation
Disulfide bondi811 ↔ 821PROSITE-ProRule annotation
Disulfide bondi816 ↔ 830PROSITE-ProRule annotation
Disulfide bondi832 ↔ 845PROSITE-ProRule annotation
Disulfide bondi853 ↔ 875PROSITE-ProRule annotation
Disulfide bondi862 ↔ 887PROSITE-ProRule annotation
Disulfide bondi876 ↔ 890PROSITE-ProRule annotation
Disulfide bondi896 ↔ 908PROSITE-ProRule annotation
Disulfide bondi914 ↔ 926PROSITE-ProRule annotation
Disulfide bondi921 ↔ 935PROSITE-ProRule annotation
Disulfide bondi937 ↔ 950PROSITE-ProRule annotation
Disulfide bondi1032 ↔ 1044PROSITE-ProRule annotation
Disulfide bondi1039 ↔ 1053PROSITE-ProRule annotation
Disulfide bondi1055 ↔ 1068PROSITE-ProRule annotation
Glycosylationi1067N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1074 ↔ 1086PROSITE-ProRule annotation
Disulfide bondi1081 ↔ 1095PROSITE-ProRule annotation
Disulfide bondi1097 ↔ 1111PROSITE-ProRule annotation
Disulfide bondi1117 ↔ 1129PROSITE-ProRule annotation
Disulfide bondi1124 ↔ 1138PROSITE-ProRule annotation
Disulfide bondi1140 ↔ 1153PROSITE-ProRule annotation
Glycosylationi1149N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1159 ↔ 1171PROSITE-ProRule annotation
Disulfide bondi1166 ↔ 1180PROSITE-ProRule annotation
Disulfide bondi1182 ↔ 1195PROSITE-ProRule annotation
Disulfide bondi1201 ↔ 1212PROSITE-ProRule annotation
Disulfide bondi1208 ↔ 1221PROSITE-ProRule annotation
Disulfide bondi1223 ↔ 1236PROSITE-ProRule annotation
Disulfide bondi1242 ↔ 1254PROSITE-ProRule annotation
Disulfide bondi1249 ↔ 1263PROSITE-ProRule annotation
Disulfide bondi1265 ↔ 1278PROSITE-ProRule annotation
Disulfide bondi1284 ↔ 1296PROSITE-ProRule annotation
Disulfide bondi1291 ↔ 1305PROSITE-ProRule annotation
Disulfide bondi1307 ↔ 1320PROSITE-ProRule annotation
Disulfide bondi1326 ↔ 1339PROSITE-ProRule annotation
Disulfide bondi1333 ↔ 1348PROSITE-ProRule annotation
Disulfide bondi1350 ↔ 1361PROSITE-ProRule annotation
Disulfide bondi1367 ↔ 1380PROSITE-ProRule annotation
Glycosylationi1369N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1374 ↔ 1389PROSITE-ProRule annotation
Disulfide bondi1391 ↔ 1402PROSITE-ProRule annotation
Disulfide bondi1408 ↔ 1420PROSITE-ProRule annotation
Disulfide bondi1415 ↔ 1429PROSITE-ProRule annotation
Disulfide bondi1431 ↔ 1444PROSITE-ProRule annotation
Disulfide bondi1450 ↔ 1461PROSITE-ProRule annotation
Disulfide bondi1456 ↔ 1470PROSITE-ProRule annotation
Disulfide bondi1472 ↔ 1485PROSITE-ProRule annotation
Glycosylationi1484N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1491 ↔ 1502PROSITE-ProRule annotation
Disulfide bondi1497 ↔ 1511PROSITE-ProRule annotation
Disulfide bondi1513 ↔ 1526PROSITE-ProRule annotation
Disulfide bondi1534 ↔ 1562PROSITE-ProRule annotation
Disulfide bondi1549 ↔ 1574PROSITE-ProRule annotation
Disulfide bondi1563 ↔ 1577PROSITE-ProRule annotation
Disulfide bondi1564 ↔ 1589PROSITE-ProRule annotation
Glycosylationi1581N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1610 ↔ 1622PROSITE-ProRule annotation
Disulfide bondi1617 ↔ 1631PROSITE-ProRule annotation
Disulfide bondi1633 ↔ 1646PROSITE-ProRule annotation
Disulfide bondi1652 ↔ 1663PROSITE-ProRule annotation
Disulfide bondi1658 ↔ 1672PROSITE-ProRule annotation
Glycosylationi1669N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1674 ↔ 1687PROSITE-ProRule annotation
Glycosylationi1703N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1713N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1770 ↔ 1782PROSITE-ProRule annotation
Disulfide bondi1777 ↔ 1791PROSITE-ProRule annotation
Disulfide bondi1793 ↔ 1806PROSITE-ProRule annotation
Disulfide bondi1812 ↔ 1824PROSITE-ProRule annotation
Disulfide bondi1818 ↔ 1833PROSITE-ProRule annotation
Disulfide bondi1835 ↔ 1847PROSITE-ProRule annotation
Disulfide bondi1853 ↔ 1865PROSITE-ProRule annotation
Disulfide bondi1860 ↔ 1874PROSITE-ProRule annotation
Disulfide bondi1876 ↔ 1889PROSITE-ProRule annotation
Disulfide bondi1895 ↔ 1905PROSITE-ProRule annotation
Disulfide bondi1900 ↔ 1914PROSITE-ProRule annotation
Glycosylationi1902N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1916 ↔ 1928PROSITE-ProRule annotation
Disulfide bondi1934 ↔ 1947PROSITE-ProRule annotation
Disulfide bondi1942 ↔ 1956PROSITE-ProRule annotation
Disulfide bondi1958 ↔ 1971PROSITE-ProRule annotation
Disulfide bondi1977 ↔ 1989PROSITE-ProRule annotation
Disulfide bondi1984 ↔ 1998PROSITE-ProRule annotation
Disulfide bondi2000 ↔ 2011PROSITE-ProRule annotation
Disulfide bondi2017 ↔ 2029PROSITE-ProRule annotation
Disulfide bondi2024 ↔ 2038PROSITE-ProRule annotation
Disulfide bondi2040 ↔ 2053PROSITE-ProRule annotation
Disulfide bondi2061 ↔ 2083PROSITE-ProRule annotationBy similarity
Disulfide bondi2070 ↔ 2096PROSITE-ProRule annotationBy similarity
Glycosylationi2077N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2084 ↔ 2099PROSITE-ProRule annotationBy similarity
Disulfide bondi2085 ↔ 2111PROSITE-ProRule annotationBy similarity
Disulfide bondi2131 ↔ 2142PROSITE-ProRule annotation
Disulfide bondi2137 ↔ 2151PROSITE-ProRule annotation
Disulfide bondi2153 ↔ 2164PROSITE-ProRule annotation
Disulfide bondi2170 ↔ 2181PROSITE-ProRule annotation
Disulfide bondi2176 ↔ 2190PROSITE-ProRule annotation
Glycosylationi2178N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2192 ↔ 2204PROSITE-ProRule annotation
Disulfide bondi2210 ↔ 2221PROSITE-ProRule annotation
Disulfide bondi2217 ↔ 2230PROSITE-ProRule annotation
Disulfide bondi2232 ↔ 2245PROSITE-ProRule annotation
Disulfide bondi2251 ↔ 2265PROSITE-ProRule annotation
Disulfide bondi2258 ↔ 2274PROSITE-ProRule annotation
Disulfide bondi2276 ↔ 2289PROSITE-ProRule annotation
Disulfide bondi2295 ↔ 2307PROSITE-ProRule annotation
Disulfide bondi2302 ↔ 2316PROSITE-ProRule annotation
Disulfide bondi2318 ↔ 2331PROSITE-ProRule annotation
Disulfide bondi2406 ↔ 2418PROSITE-ProRule annotation
Disulfide bondi2413 ↔ 2427PROSITE-ProRule annotation
Disulfide bondi2429 ↔ 2442PROSITE-ProRule annotation
Disulfide bondi2448 ↔ 2459PROSITE-ProRule annotation
Disulfide bondi2455 ↔ 2468PROSITE-ProRule annotation
Disulfide bondi2470 ↔ 2483PROSITE-ProRule annotation
Disulfide bondi2489 ↔ 2500PROSITE-ProRule annotation
Disulfide bondi2496 ↔ 2509PROSITE-ProRule annotation
Disulfide bondi2511 ↔ 2522PROSITE-ProRule annotation
Disulfide bondi2528 ↔ 2541PROSITE-ProRule annotation
Disulfide bondi2535 ↔ 2550PROSITE-ProRule annotation
Disulfide bondi2552 ↔ 2565PROSITE-ProRule annotation
Disulfide bondi2571 ↔ 2581PROSITE-ProRule annotation
Disulfide bondi2577 ↔ 2590PROSITE-ProRule annotation
Disulfide bondi2592 ↔ 2605PROSITE-ProRule annotation
Disulfide bondi2611 ↔ 2622PROSITE-ProRule annotation
Disulfide bondi2617 ↔ 2631PROSITE-ProRule annotation
Disulfide bondi2633 ↔ 2646PROSITE-ProRule annotation
Disulfide bondi2652 ↔ 2663PROSITE-ProRule annotation
Disulfide bondi2659 ↔ 2672PROSITE-ProRule annotation
Disulfide bondi2674 ↔ 2686PROSITE-ProRule annotation
Modified residuei2702PhosphoserineBy similarity1
Modified residuei2709PhosphoserineBy similarity1
Glycosylationi2734N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2750N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2767N-linked (GlcNAc...)Sequence 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 subsequentely 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
Sitei2731 – 2732Cleavage; by furinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP98133.
PeptideAtlasiP98133.
PRIDEiP98133.

Expressioni

Gene expression databases

BgeeiENSBTAG00000002278.

Interactioni

Subunit structurei

Interacts with COL16A1. Interacts with integrin alpha-V/beta-3. Interacts with ADAMTS10; this interaction promotes microfibril assembly. Interacts with THSD4; this interaction promotes fibril formation. 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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002944.

Structurei

3D structure databases

ProteinModelPortaliP98133.
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
Domaini449 – 489EGF-like 6PROSITE-ProRule annotationAdd BLAST41
Domaini490 – 529EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini530 – 571EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini572 – 612EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini613 – 653EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini659 – 711TB 3Add BLAST53
Domaini723 – 764EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini765 – 806EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini807 – 846EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini851 – 902TB 4Add BLAST52
Domaini910 – 951EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini956 – 1008TB 5Add BLAST53
Domaini1028 – 1069EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1070 – 1112EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1113 – 1154EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1155 – 1196EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1197 – 1237EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1238 – 1279EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1280 – 1321EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1322 – 1362EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1363 – 1403EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1404 – 1445EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1446 – 1486EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1487 – 1527EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1532 – 1589TB 6Add BLAST58
Domaini1606 – 1647EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1648 – 1688EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1693 – 1748TB 7Add BLAST56
Domaini1766 – 1807EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1808 – 1848EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1849 – 1890EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1891 – 1929EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini1930 – 1972EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1973 – 2012EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2013 – 2054EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2059 – 2111TB 8Add BLAST53
Domaini2127 – 2165EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini2166 – 2205EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2206 – 2246EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2247 – 2290EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini2291 – 2332EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2337 – 2390TB 9Add BLAST54
Domaini2402 – 2443EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2444 – 2484EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2485 – 2523EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini2524 – 2566EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini2567 – 2606EGF-like 45; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2607 – 2647EGF-like 46; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2648 – 2687EGF-like 47; calcium-bindingPROSITE-ProRule annotationAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 450N-terminal domainBy similarityAdd BLAST406
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
Regioni1528 – 2731C-terminal domainBy similarityAdd BLAST1204

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1541 – 1543Cell attachment siteBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi392 – 446Pro-richAdd BLAST55

Sequence similaritiesi

Belongs to the fibrillin family.Curated
Contains 47 EGF-like domains.PROSITE-ProRule annotation
Contains 9 TB (TGF-beta binding) domains.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiP98133.
KOiK06825.
OMAiRSGNCYL.
OrthoDBiEOG091G002H.

Family and domain databases

Gene3Di3.90.290.10. 10 hits.
InterProiIPR026823. 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_.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 39 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 47 hits.
SM00179. EGF_CA. 44 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 10 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P98133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRGGLLEVA LGFTVLLASY TSHGADTNLE AGNVKETRAN RAKRRGGGGH
60 70 80 90 100
DALKGPNVCG SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC
110 120 130 140 150
TCPSGQIAPS CGSRSIQHCN IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC
160 170 180 190 200
ESGCLNGGRC VAPNRCACTY GFTGPQCERD YRTGPCFTVI SNQMCQGQLS
210 220 230 240 250
GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR TGACQDVDEC
260 270 280 290 300
QAIPGLCQGG NCINTVGSFE CKCPAGHKFN EVSQKCEDID ECSTIPGICD
310 320 330 340 350
GGECTNTVSS YFCKCPPGFY TSPDGTRCID VRPGYCYTAL ANGRCSNQLP
360 370 380 390 400
QSITKMQCCC DVGRCWSPGV TVAPEMCPIR ATEDFNKLCS VPMVIPERPG
410 420 430 440 450
YPPPPLGPVP PVQPVPPGFP PGPQIMIPRP PVEYPYPSRE PPRVLPVNVT
460 470 480 490 500
DYCQLFRYLC QNGRCIPTPG SYRCECNKGF QLDLRGECID VDECEKNPCA
510 520 530 540 550
GGECINTQGS YTCQCRPGYQ STLTRTECRD IDECLQNGRI CNNGRCINTD
560 570 580 590 600
GSFHCVCNAG FHVTRDGKNC EDMDECSIRN MCLNGMCINE DGSFKCICKP
610 620 630 640 650
GFQLASDGRY CKDINECETP GICMNGRCVN TDGSYRCECF PGLAVGLDGR
660 670 680 690 700
VCVDTHMRST CYGGYKRGQC VKPLFGAVTK SECCCASTEY AFGEPCQPCP
710 720 730 740 750
SQNSAEYQAL CSSGPGITSA GSDINECALD PDICPNGICE NLRGTYKCIC
760 770 780 790 800
NSGYEVDSTG KNCVDINECV LNSLLCDNGQ CRNTPGSFVC TCPKGFIYKP
810 820 830 840 850
ELKTCEDIDE CESSPCINGV CKNSPGSFIC ECSSESTLDP TKTICIETIK
860 870 880 890 900
GTCWQTVIDG RCEININGAT LKSQCCSSLG AAWGSPCTPC QVDPICGKGY
910 920 930 940 950
SRIKGTQCED IDECEVFPGV CKNGLCVNSK GSFKCQCPSG MTLDATGRIC
960 970 980 990 1000
LDIRLETCFL RYEDEECTLP VAGRHRMDAC CCSVGAAWGT EECEECPVRN
1010 1020 1030 1040 1050
TPEYEELCPR GPGFATKEIT NGKRFFKDIN ECKMIPNLCT HGKCRNTIGS
1060 1070 1080 1090 1100
FKCRCDSGFA LDSEERNCTD IDECRISPDL CGRGQCVNTP GDFECKCDEG
1110 1120 1130 1140 1150
YESGFMMMKN CMDIDECQRD PLLCRGGVCL NTEGSYRCEC PPGHQLAPNI
1160 1170 1180 1190 1200
SACIDINECE LSAHLCPHGR CVNLIGKYQC ACNPGYHSTP DRLFCVDIDE
1210 1220 1230 1240 1250
CSIMNGGCET FCTNSEGSYE CSCQPGFALM PDQRSCTDID ECEDNPNICD
1260 1270 1280 1290 1300
GGQCTNIPGE YRCLCYDGFM ASEDMKTCVD VNECDLNPNI CLSGTCENTK
1310 1320 1330 1340 1350
GSFICHCDMG YSGKKGKTGC TDINECEIGA HNCDRHAVCT NTAGSFKCSC
1360 1370 1380 1390 1400
SPGWIGDGIK CTDLDECSNG THMCSQHADC KNTMGSYRCL CKEGYTGDGF
1410 1420 1430 1440 1450
TCTDLDECSE NLNLCGNGQC LNAPGGYRCE CDMGFVPSAD GKACEDIDEC
1460 1470 1480 1490 1500
SLPNICVFGT CHNLPGLFRC ECEIGYELDR SGGNCTDVNE CLDPTTCISG
1510 1520 1530 1540 1550
NCVNTPGSYT CDCPPDFELN PTRVGCVDTR SGNCYLDIRP RGDNGDTACS
1560 1570 1580 1590 1600
NEIGVGVSKA SCCCSLGKAW GTPCELCPPV NTSEYKILCP GGEGFRPNPI
1610 1620 1630 1640 1650
TVILEDIDEC QELPGLCQGG KCINTFGSFQ CRCPTGYYLN EDTRVCDDVN
1660 1670 1680 1690 1700
ECETPGICGP GTCYNTVGNY TCICPPDYMQ VNGGNNCMDM RRSLCYRNYY
1710 1720 1730 1740 1750
ADNQTCDGEL LFNMTKKMCC CSYNIGRAWN KPCEQCPIPS TDEFATLCGS
1760 1770 1780 1790 1800
QRPGFVIDIY TGLPVDIDEC REIPGVCENG VCINMVGSFR CECPVGFFYN
1810 1820 1830 1840 1850
DKLLVCEDID ECQNGPVCQR NAECINTAGS YRCDCKPGYR FTSTGQCNDR
1860 1870 1880 1890 1900
NECQEIPNIC SHGQCIDTVG SFYCLCHTGF KTNADQTMCL DINECERDAC
1910 1920 1930 1940 1950
GNGTCRNTIG SFNCRCNHGF ILSHNNDCID VDECATGNGN LCRNGQCINT
1960 1970 1980 1990 2000
VGSFQCQCNE GYEVAPDGRT CVDINECLLD PRKCAPGTCQ NLDGSYRCIC
2010 2020 2030 2040 2050
PPGYSLQNDK CEDIDECVEE PEICALGTCS NTEGSFKCLC PDGFSLSSTG
2060 2070 2080 2090 2100
RRCQDLRMSY CYAKFEGGKC SSPKSRNHSK QECCCALKGE GWGDPCELCP
2110 2120 2130 2140 2150
TEPDEAFRQI CPYGSGIIVG PDDSAVDMDE CKEPDVCKHG QCINTDGSYR
2160 2170 2180 2190 2200
CECPFGYILQ GNECVDTDEC SVGNPCGNGT CKNVIGGFEC TCEEGFEPGP
2210 2220 2230 2240 2250
MMTCEDINEC AQNPLLCAFR CVNTYGSYEC KCPAGYVLRE DRRMCKDEDE
2260 2270 2280 2290 2300
CEEGKHDCAE KQMECKNLIG TYLCICGPGY QRRPDGEGCV DENECQTKPG
2310 2320 2330 2340 2350
ICENGRCLNT RGSYTCECND GFTASPNQDE CLDNREGYCF TEVLQNMCQI
2360 2370 2380 2390 2400
GSSNRNPVTK SECCCDGGRG WGPHCEICPF QGTVAFKKLC PHGRGFMTNG
2410 2420 2430 2440 2450
ADIDECKVIH DVCRNGECVN DRGSYHCICK TGYTPDITGT ACVDLNECNQ
2460 2470 2480 2490 2500
APKPCNFICK NTEGSYQCSC PKGYILQEDG RSCKDLDECA TKQHNCQFLC
2510 2520 2530 2540 2550
VNTIGSFTCK CPPGFTQHHT ACIDNNECTS DINLCGSKGI CQNTPGSFTC
2560 2570 2580 2590 2600
ECQRGFSLDP SGASCEDVDE CEGNHRCQHG CQNIIGGYRC SCPQGYLQHY
2610 2620 2630 2640 2650
QWNQCVDENE CLSAHICGGA SCHNTLGSYK CMCPAGFQYE QFSGGCQDIN
2660 2670 2680 2690 2700
ECGSAQAPCS YGCSNTEGGY LCACPPGYFR IGQGHCVSGM GMGRGNPEPP
2710 2720 2730 2740 2750
ASGEMDDNSL SPEACYECKI NGYPKRGRKR RSANETDASN IEDQPEIEAN
2760 2770 2780 2790 2800
VSLASWDVEK TAVFAFNISH ISNKVRILEL LPALTTLTNH NRYLIESGNE
2810 2820 2830 2840 2850
NGFFKINQKE GISYLHFTKK KPVAGTYSLQ ISSTPLYKKK ELNQLEDKYD
2860 2870
KDYLSGELGD NLKMKIQILL H
Length:2,871
Mass (Da):312,249
Last modified:July 6, 2016 - v2
Checksum:iD49E971A8176D3B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51D → N in AAA74122 (PubMed:7835900).Curated1
Sequence conflicti362V → A in AAA74122 (PubMed:7835900).Curated1
Sequence conflicti620P → L in AAA74122 (PubMed:7835900).Curated1
Sequence conflicti2561S → T in AAA74122 (PubMed:7835900).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28748 mRNA. Translation: AAA74122.1.
DAAA02029120 Genomic DNA. No translation available.
DAAA02029121 Genomic DNA. No translation available.
DAAA02029122 Genomic DNA. No translation available.
PIRiA55567.
RefSeqiNP_776478.1. NM_174053.2.
XP_015328665.1. XM_015473179.1.
UniGeneiBt.107024.

Genome annotation databases

EnsembliENSBTAT00000002944; ENSBTAP00000002944; ENSBTAG00000002278.
GeneIDi281154.
KEGGibta:281154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28748 mRNA. Translation: AAA74122.1.
DAAA02029120 Genomic DNA. No translation available.
DAAA02029121 Genomic DNA. No translation available.
DAAA02029122 Genomic DNA. No translation available.
PIRiA55567.
RefSeqiNP_776478.1. NM_174053.2.
XP_015328665.1. XM_015473179.1.
UniGeneiBt.107024.

3D structure databases

ProteinModelPortaliP98133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002944.

Proteomic databases

PaxDbiP98133.
PeptideAtlasiP98133.
PRIDEiP98133.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000002944; ENSBTAP00000002944; ENSBTAG00000002278.
GeneIDi281154.
KEGGibta:281154.

Organism-specific databases

CTDi2200.

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiP98133.
KOiK06825.
OMAiRSGNCYL.
OrthoDBiEOG091G002H.

Enzyme and pathway databases

ReactomeiR-BTA-1474228. Degradation of the extracellular matrix.
R-BTA-1566948. Elastic fibre formation.
R-BTA-2129379. Molecules associated with elastic fibres.
R-BTA-216083. Integrin cell surface interactions.

Gene expression databases

BgeeiENSBTAG00000002278.

Family and domain databases

Gene3Di3.90.290.10. 10 hits.
InterProiIPR026823. 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_.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 39 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 47 hits.
SM00179. EGF_CA. 44 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 10 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFBN1_BOVIN
AccessioniPrimary (citable) accession number: P98133
Secondary accession number(s): F1N4K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 6, 2016
Last modified: November 2, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.