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0TGFB1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTGFB1
DescriptionTransforming growth factor beta 1 precursor (tgf-beta 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0006916 anti-apoptosis (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The transforming growth factor beta.-terminus (TGFb) domain is present in avariety of proteins which include the transforming growth factor beta.ecapentaplegic proteins and bone morphogenetic proteins. Transforming growthfactor beta is a multifunctional peptide that controls proliferation.ifferentiation and other functions in many cell types. The decapentaplegicprotein acts as an extracellular morphogen responsible for the properdevelopment of the embryonic dorsal hypoderm.or viability of larvae andfor cell viability of the epithelial cells in the imaginal disks. Bonemorphogenetic protein induces cartilage and bone formation and may be responsiblefor epithelial osteogenesis in some organisms.
  IPR001111:Transforming growth factor beta (TGFb), N-terminal
Transforming growth factor-beta (TGF-beta) is a multifunctional peptide that controls proliferation.ifferentiation and other functions in many cell types. TGF-beta-1 is a peptide of 112 amino acid residues derived by proteolytic cleavage from the C-terminal of a precursor protein.A number of proteins are known to be related to TGF-beta-1 . Proteins from the TGF-beta family are only active as homo- or heterodimer; the two chains being linked by a single disulphide bond. From X-ray studies of TGF-beta-2 .t is known that all the other cysteines are involved in intrachain disulphide bonds. As shown in the following schematic representation.here are four disulphide bonds in the TGF-betas and in inhibin beta chains.hile the other members of this family lack the first bond.
  IPR001839:Transforming growth factor beta
The crystal structures of several proteins have been reported as having unusual folds.nvolving intramolecular disulphide bridges. In transforming growth factor-beta 2 (TGF-beta2) .latelet-derived growth factor (PDGF).erve growth factor (NGF) and human chorionic gonadotropin (hCG) .ix conserved cysteines (I to VI in sequence order) form three disulphide links arranged in a knot-like topology. Cystines [II-V] and [III-VI] form a ring of eight amino acids through which the remaining disulphide bond (Cys[I-IV]) penetrates.A similar knotted arrangement of disulphide bonds has been noted in the structures of some enzyme inhibitors and neurotoxins that bind to voltage- gated Ca2+ channels . In those sequences.owever.he cystine topology differs. Cys[III-VI] penetrates a macrocyclic ring formed by Cys[I-IV] and Cys[II-V]. Thus.ystine knots fall into two structural classes: growth factor type and inhibitor-like cystine knots .All growth factor cystine knots structures have similar topology.ith two distorted beta-hairpin loops "above" the knot and a single loop "below". The sizes of the hairpin loop vary significantly.
  IPR002400:Growth factor, cystine knot
The transforming growth factors-beta (TGF-beta 1-5) constitute a family ofmulti-functional cytokines that regulate cell growth and differentiation . Many cells synthesise TGF-beta.nd essentially all have specific receptors for this peptide . TGF-beta regulates the actions of many other peptide growth factors and determines a positive or negative direction of their effects. The protein functions as a disulphide-linked homodimer. Its sequence is characterised by the presence of several C-terminal cysteine residues.hich form interlocking disulphide links arranged in a knot-like topology. A similar "cystine-knot" arrangement has been noted in thestructures of some enzyme inhibitors and neurotoxins that bind to voltage-gated Ca2+ channels.lthough the precise topology differs.The three-dimensional structures of several members of the TGF-beta super-family have been deduced . The solution structure of human TGF-beta 1 was determined using multinuclear magnetic resonance spectroscopy with hybrid distance geometry/simulated annealing . The structure shows a high degree of similarity to that of TGF-beta 2.ut with notable differences in structure and flexibility. The crystal structure of the TGF-beta 2 monomer lacks a well-defined hydrophobic core and displays an unusual elongated non-globular fold . Eight cysteine residues form 4 intra-chain disulphide bonds.reating the characteristic knotted arrangement. The dimer is stabilised by a ninth cysteine.hich forms an inter-chain disulphide bond.nd by 2 identical hydrophobic interfaces. Other members of the TGF-beta superfamily.ncluding activins.nhibins and various developmental factors.re also likely to adopt the TGF-beta fold. The crystal structure of TGF-beta 3 reveals a near identical central core to that of TGF-beta 2 . The principal differences are witnessed in the conformations of the N-terminal alpha-helix and in the beta-sheet loops.hich could account for the individual cellular responses.f these differences are recognised by the TGF-beta receptors.
  IPR003911:Transforming growth factor beta TGFb
The transforming growth factors-beta (TGF-beta 1-5) constitute a family ofmulti-functional cytokines that regulate cell growth and differentiation . Many cells synthesise TGF-beta.nd essentially all have specific receptors for this peptide . TGF-beta regulates the actions of many other peptide growth factors and determines a positive or negative direction of their effects. The protein functions as a disulphide-linked homodimer. Its sequence is characterised by the presence of several C-terminal cysteine residues.hich form interlocking disulphide links arranged in a knot-like topology. A similar "cystine-knot" arrangement has been noted in thestructures of some enzyme inhibitors and neurotoxins that bind to voltage-gated Ca2+ channels.lthough the precise topology differs.The three-dimensional structures of several members of the TGF-beta super-family have been deduced . The solution structure of human TGF-beta 1 was determined using multinuclear magnetic resonance spectroscopy with hybrid distance geometry/simulated annealing . The structure shows a high degree of similarity to that of TGF-beta 2.ut with notable differences in structure and flexibility. TGF-beta genes are expressed differentially.uggesting that the various TGF-beta species may have distinct physiological roles in vivo. Examination ofTGF-beta 1 mRNA levels in adult murine tissues indicates that expression ispredominant in spleen.ung and placenta . TGF-beta 1 is believed to play important roles in pathologic processes.
  IPR003939:Transforming growth factor, beta 1
IPR001111:TGFb_propeptide 
Evalue:-71.958610534668 
Location:33-252IPR001839:TGF_beta 
Evalue:-50.2924308776856 
Location:290-390IPR003939:TGFBETA1 
Evalue:0 
Location:12-31IPR003939:TGFBETA1 
Evalue:0 
Location:264-275
SequencesProtein: TGFB1_HUMAN (390 aa)
mRNA: NM_000660
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentK04384
  Level 3 annotation:
    transforming growth factor, beta
  Level 2 annotation:
    MAPK signaling pathway
    TGF-beta signaling pathway
    Cytokines
    Cytokine-cytokine receptor interaction
    CAM ligands
    Cell cycle
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 156 residues, 46528490-46528955Exon2: 53 residues, 46529872-46530026Exon3: 51 residues, 46539627-46539775Exon4: 28 residues, 46539914-46539992Exon5: 41 residues, 46542491-46542609Exon6: 55 residues, 46546039-46546200Exon7: 409 residues, 46550434-46551656Exon8: 2 residues, -Jump to TGFB1_HUMAN  
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