UniProt:P98133 FBN1

chain
  • signal peptide:1-24
  • propeptide:25-44
  • chain:45-2731
  • chain:2732-2871
checksum D49E971A8176D3B8
comment
  • FUNCTION 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 Ca(2+) 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.FUNCTION 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.SUBUNIT 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 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. Interacts (via N-terminal domain) with EFEMP2; this interaction inhibits EFEMP2 binding to LOX and ELN (By similarity).SUBCELLULAR LOCATION Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin.SUBCELLULAR LOCATION Secreted into the plasma.SUBCELLULAR LOCATION 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.PTM Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils.PTM O-glycosylated on serine residues by POGLUT2 and POGLUT3 which is necessary for efficient protein secretion.SIMILARITY Belongs to the fibrillin family.
crossReference
databaseName UniProt
dbId 90292
description
  • recommendedName: fullName evidence="1"Fibrillin-1 alternativeName: MP340 component recommendedName: fullName evidence="1"Asprosin /component
displayName UniProt:P98133 FBN1
geneName
  • FBN1
identifier P98133
isSequenceChanged false
keyword
  • Calcium
  • Direct protein sequencing
  • Disulfide bond
  • EGF-like domain
  • Extracellular matrix
  • Glycoprotein
  • Hormone
  • Phosphoprotein
  • Reference proteome
  • Repeat
  • Secreted
  • Signal
modified [InstanceEdit:9852000] Weiser, Joel, 2023-11-03
moleculeType Protein
name
  • FBN1
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • FBN1_BOVIN
  • F1N4K8
sequenceLength 2871
species [Species:48898] Bos taurus
stId uniprot:P98133
url http://purl.uniprot.org/uniprot/P98133
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