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Transforming growth factor beta-1 (TGF-beta-1) [Cleaved into: Latency-associated peptide (LAP)]

 TGFB1_CHLAE             Reviewed;         390 AA.
P09533;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 116.
RecName: Full=Transforming growth factor beta-1;
Short=TGF-beta-1;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Flags: Precursor;
Name=TGFB1;
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
NCBI_TaxID=9534;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3474130; DOI=10.1089/dna.1987.6.239;
Sharples K., Plowman G.D., Rose T.M., Twardzik D.R., Purchio A.F.;
"Cloning and sequence analysis of simian transforming growth factor-
beta cDNA.";
DNA 6:239-244(1987).
[2]
GLYCOSYLATION.
PubMed=2971654;
Purchio A.F., Cooper J.A., Brunner A.M., Lioubin M.N., Gentry L.E.,
Kovacina K.S., Roth R.A., Marquardt H.;
"Identification of mannose 6-phosphate in two asparagine-linked sugar
chains of recombinant transforming growth factor-beta 1 precursor.";
J. Biol. Chem. 263:14211-14215(1988).
[3]
CHARACTERIZATION.
PubMed=3185545; DOI=10.1128/MCB.8.10.4162;
Gentry L.E., Lioubin M.N., Purchio A.F., Marquardt H.;
"Molecular events in the processing of recombinant type 1 pre-pro-
transforming growth factor beta to the mature polypeptide.";
Mol. Cell. Biol. 8:4162-4168(1988).
-!- FUNCTION: Multifunctional protein that controls proliferation,
differentiation and other functions in many cell types. Many cells
synthesize TGFB1 and have specific receptors for it. It positively
and negatively regulates many other growth factors. It plays an
important role in bone remodeling as it is a potent stimulator of
osteoblastic bone formation, causing chemotaxis, proliferation and
differentiation in committed osteoblasts (By similarity).
Stimulates sustained production of collagen through the activation
of CREB3L1 by regulated intramembrane proteolysis (RIP) (By
similarity). Can promote either T-helper 17 cells (Th17) or
regulatory T-cells (Treg) lineage differentiation in a
concentration-dependent manner. At high concentrations, leads to
FOXP3-mediated suppression of RORC and down-regulation of IL-17
expression, favoring Treg cell development. At low concentrations
in concert with IL-6 and IL-21, leads to expression of the IL-17
and IL-23 receptors, favoring differentiation to Th17 cells.
Mediates SMAD2/3 activation by inducing its phosphorylation and
subsequent translocation to the nucleus. Can induce epithelial-to-
mesenchymal transition (EMT) and cell migration in various cell
types (By similarity). {ECO:0000250|UniProtKB:P01137,
ECO:0000250|UniProtKB:P04202}.
-!- SUBUNIT: Homodimer; disulfide-linked, or heterodimer with TGFB2
(By similarity). Secreted and stored as a biologically inactive
form in the extracellular matrix in a 290 kDa complex (large
latent TGF-beta1 complex) containing the TGFB1 homodimer, the
latency-associated peptide (LAP), and the latent TGFB1 binding
protein-1 (LTBP1). The complex without LTBP1 is known as the'small
latent TGF-beta1 complex'. Dissociation of the TGFB1 from LAP is
required for growth factor activation and biological activity.
Release of the large latent TGF-beta1 complex from the
extracellular matrix is carried out by the matrix
metalloproteinase MMP3 (By similarity). Interacts with CD109 and
DPT. Interacts with ASPN. May interact with THSD4; this
interaction may lead to sequestration by FBN1 microfibril assembly
and attenuation of TGFB signaling. Interacts with the serine
proteases, HTRA1 and HTRA3: the interaction with either inhibits
TGFB1-mediated signaling. The HTRA protease activity is required
for this inhibition (By similarity). Latency-associated peptide
interacts with NREP; the interaction results in a decrease in
TGFB1 autoinduction (By similarity). Interacts (via processed form
(LAP)) with HSP90AB1; inhibits latent TGFB1 activation (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P01137}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- DOMAIN: The 'straitjacket' and 'arm' domains encircle the growth
factor monomers and are fastened together by strong bonding
between Lys-56 and Tyr-103/Tyr-104. Activation of TGF-beta1
requires the binding of integrin alpha-V to an RGD sequence in the
prodomain and exertion of force on this domain, which is held in
the extracellular matrix by latent TGF-beta binding proteins. The
sheer physical force unfastens the straitjacket and releases the
active growth factor dimer (By similarity). {ECO:0000250}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:2971654}.
-!- PTM: The precursor is cleaved into mature TGF-beta-1 and LAP,
which remains non-covalently linked to mature TGF-beta-1 rendering
it inactive.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M16658; AAA35369.1; -; mRNA.
PIR; A26960; A26960.
ProteinModelPortal; P09533; -.
SMR; P09533; -.
iPTMnet; P09533; -.
PRIDE; P09533; -.
HOVERGEN; HBG074115; -.
PRO; PR:P09533; -.
GO; GO:0072562; C:blood microparticle; ISS:AgBase.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0003823; F:antigen binding; ISS:AgBase.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:UniProtKB.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0006754; P:ATP biosynthetic process; ISS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0016049; P:cell growth; IEA:InterPro.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:AgBase.
GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0019049; P:evasion or tolerance of host defenses by virus; ISS:UniProtKB.
GO; GO:0085029; P:extracellular matrix assembly; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:UniProtKB.
GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:AgBase.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISS:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; ISS:BHF-UCL.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS:UniProtKB.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043932; P:ossification involved in bone remodeling; ISS:AgBase.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISS:UniProtKB.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; ISS:AgBase.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISS:UniProtKB.
GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; ISS:AgBase.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISS:UniProtKB.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:AgBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; ISS:AgBase.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:AgBase.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
GO; GO:0060390; P:regulation of SMAD protein import into nucleus; ISS:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0070723; P:response to cholesterol; ISS:UniProtKB.
GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; ISS:AgBase.
GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
GO; GO:0007183; P:SMAD protein complex assembly; ISS:UniProtKB.
GO; GO:0007184; P:SMAD protein import into nucleus; ISS:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR016319; TGF-beta.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR003939; TGFb1.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF001787; TGF-beta; 1.
PRINTS; PR01423; TGFBETA.
PRINTS; PR01424; TGFBETA1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Disulfide bond;
Extracellular matrix; Glycoprotein; Growth factor; Mitogen; Secreted;
Signal.
SIGNAL 1 29
CHAIN 30 278 Latency-associated peptide.
/FTId=PRO_0000033760.
CHAIN 279 390 Transforming growth factor beta-1.
/FTId=PRO_0000033761.
REGION 30 74 Straightjacket domain. {ECO:0000250}.
REGION 75 271 Arm domain. {ECO:0000250}.
MOTIF 244 246 Cell attachment site. {ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2971654}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2971654}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2971654}.
DISULFID 33 33 Interchain (with C-? in LTBP1 TB3
domain); in inactive form. {ECO:0000250}.
DISULFID 223 223 Interchain (with C-225). {ECO:0000250}.
DISULFID 225 225 Interchain (with C-223). {ECO:0000250}.
DISULFID 285 294 {ECO:0000250}.
DISULFID 293 356 {ECO:0000250}.
DISULFID 322 387 {ECO:0000250}.
DISULFID 326 389 {ECO:0000250}.
DISULFID 355 355 Interchain. {ECO:0000250}.
SEQUENCE 390 AA; 44356 MW; DFF63E2BAB44320E CRC64;
MPPSGLRLLP LLLPLLWLLV LTPSRPAAGL STCKTIDMEL VKRKRIETIR GQILSKLRLA
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE ADYYAKEVTR VLMVETHNEI
YDKFKQSTHS IYMFFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNNSWR
YLSNRLLAPS NSPEWLSFDV TGVVRQWLSR GGEIEGFRLS AHCSCDSKDN TLQVDINGFT
TGRRGDLATI HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


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