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Protein

Fibrillin-1

Gene

FBN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHormone
LigandCalcium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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
R-BTA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-BTA-8957275 Post-translational protein phosphorylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fibrillin-1
Alternative name(s):
MP340
Cleaved into the following chain:
AsprosinBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FBN1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:28885 FBN1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24By similarityAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000043687925 – 44By similarityAdd BLAST20
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000758045 – 2731Fibrillin-1By similarityAdd BLAST2687
ChainiPRO_00004368802732 – 2871AsprosinBy similarityAdd BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi448N-linked (GlcNAc...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence analysis1
Disulfide bondi1674 ↔ 1687PROSITE-ProRule annotation
Glycosylationi1703N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1713N-linked (GlcNAc...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence 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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2702PhosphoserineBy similarity1
Modified residuei2709PhosphoserineBy similarity1
Glycosylationi2734N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2750N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2767N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei44 – 45Cleavage; by furinBy similarity2
Sitei2731 – 2732Cleavage; by furinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P98133

PeptideAtlas

More...
PeptideAtlasi
P98133

PRoteomics IDEntifications database

More...
PRIDEi
P98133

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000002278 Expressed in 10 organ(s), highest expression level in colon

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000002944

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P98133

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P98133

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1541 – 1543Cell attachment siteBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi392 – 446Pro-richAdd BLAST55

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the fibrillin family.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IR7H Eukaryota
ENOG410XSTY LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155011

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231768

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005643

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P98133

KEGG Orthology (KO)

More...
KOi
K06825

Identification of Orthologs from Complete Genome Data

More...
OMAi
RPPVEYP

Database of Orthologous Groups

More...
OrthoDBi
EOG091G002H

TreeFam database of animal gene trees

More...
TreeFami
TF316849

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.290.10, 9 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

The PANTHER Classification System

More...
PANTHERi
PTHR24039 PTHR24039, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12662 cEGF, 2 hits
PF07645 EGF_CA, 39 hits
PF00683 TB, 9 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181 EGF, 47 hits
SM00179 EGF_CA, 44 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57184 SSF57184, 10 hits
SSF57581 SSF57581, 9 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD49E971A8176D3B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

Protein sequence database of the Protein Information Resource

More...
PIRi
A55567

NCBI Reference Sequences

More...
RefSeqi
NP_776478.1, NM_174053.2
XP_015328665.1, XM_015473179.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Bt.107024

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000002944; ENSBTAP00000002944; ENSBTAG00000002278

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
281154

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:281154

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
SMRiP98133
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

Comparative Toxicogenomics Database

More...
CTDi
2200
VGNCiVGNC:28885 FBN1

Phylogenomic databases

eggNOGiENOG410IR7H Eukaryota
ENOG410XSTY LUCA
GeneTreeiENSGT00940000155011
HOGENOMiHOG000231768
HOVERGENiHBG005643
InParanoidiP98133
KOiK06825
OMAiRPPVEYP
OrthoDBiEOG091G002H
TreeFamiTF316849

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
R-BTA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-BTA-8957275 Post-translational protein phosphorylation

Gene expression databases

BgeeiENSBTAG00000002278 Expressed in 10 organ(s), highest expression level in colon

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, 2 hits
PF07645 EGF_CA, 39 hits
PF00683 TB, 9 hits
SMARTiView protein in SMART
SM00181 EGF, 47 hits
SM00179 EGF_CA, 44 hits
SUPFAMiSSF57184 SSF57184, 10 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFBN1_BOVIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P98133
Secondary accession number(s): F1N4K8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 6, 2016
Last modified: December 5, 2018
This is version 146 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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