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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.
07-NOV-2018, entry version 123.
RecName: Full=Transforming growth factor beta-1 proprotein;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-1;
Short=TGF-beta-1;
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 AT ASN-82; ASN-136 AND ASN-176.
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]
PROTEOLYTIC CLEAVAGE.
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: Transforming growth factor beta-1 proprotein: Precursor
of the Latency-associated peptide (LAP) and Transforming growth
factor beta-1 (TGF-beta-1) chains, which constitute the regulatory
and active subunit of TGF-beta-1, respectively.
{ECO:0000250|UniProtKB:P01137}.
-!- FUNCTION: Latency-associated peptide: Required to maintain the
Transforming growth factor beta-1 (TGF-beta-1) chain in a latent
state during storage in extracellular matrix. Associates non-
covalently with TGF-beta-1 and regulates its activation via
interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP
and LRRC33/NRROS, that control activation of TGF-beta-1.
Interaction with LRRC33/NRROS regulates activation of TGF-beta-1
in macrophages and microglia. Interaction with LRRC32/GARP
controls activation of TGF-beta-1 on the surface of activated
regulatory T-cells (Tregs). Interaction with integrins
(ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-
associated peptide chain and subsequent release of the active TGF-
beta-1. {ECO:0000250|UniProtKB:P01137}.
-!- FUNCTION: Transforming growth factor beta-1: Multifunctional
protein that regulates the growth and differentiation of various
cell types and is involved in various processes, such as normal
development, immune function, microglia function and responses to
neurodegeneration (By similarity). Activation into mature form
follows different steps: following cleavage of the proprotein in
the Golgi apparatus, Latency-associated peptide (LAP) and
Transforming growth factor beta-1 (TGF-beta-1) chains remain non-
covalently linked rendering TGF-beta-1 inactive during storage in
extracellular matrix. At the same time, LAP chain interacts with
'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS
that control activation of TGF-beta-1 and maintain it in a latent
state during storage in extracellular milieus. TGF-beta-1 is
released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8):
integrin-binding to LAP stabilizes an alternative conformation of
the LAP bowtie tail and results in distortion of the LAP chain and
subsequent release of the active TGF-beta-1. Once activated
following release of LAP, TGF-beta-1 acts by binding to TGF-beta
receptors (TGFBR1 and TGFBR2), which transduce signal (By
similarity). While expressed by many cells types, TGF-beta-1 only
has a very localized range of action within cell environment
thanks to fine regulation of its activation by Latency-associated
peptide chain (LAP) and 'milieu molecules'. Plays an important
role in bone remodeling: acts as a potent stimulator of
osteoblastic bone formation, causing chemotaxis, proliferation and
differentiation in committed osteoblasts. 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 (By similarity). Stimulates
sustained production of collagen through the activation of CREB3L1
by regulated intramembrane proteolysis (RIP). 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 (By similarity). 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. May interact with THSD4;
this interaction may lead to sequestration by FBN1 microfibril
assembly and attenuation of TGFB signaling (By similarity).
Interacts with CD109, DPT and ASPN. Latency-associated peptide:
Homodimer; disulfide-linked. Latency-associated peptide: Interacts
with Transforming growth factor beta-1 (TGF-beta-1) chain;
interaction is non-covalent and maintains (TGF-beta-1) in a latent
state; each Latency-associated peptide (LAP) monomer interacts
with TGF-beta-1 in the other monomer. Latency-associated peptide:
Interacts with LTBP1; leading to regulate activation of TGF-beta-
1. Latency-associated peptide: Interacts with LRRC32/GARP; leading
to regulate activation of TGF-beta-1 on the surface of activated
regulatory T-cells (Tregs). Interacts with LRRC33/NRROS; leading
to regulate activation of TGF-beta-1 in macrophages and microglia.
Latency-associated peptide: Interacts (via cell attachment site)
with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release
of the active TGF-beta-1 (By similarity). Latency-associated
peptide: Interacts with NREP; the interaction results in a
decrease in TGFB1 autoinduction (By similarity). Latency-
associated peptide: Interacts with HSP90AB1; inhibits latent TGFB1
activation. Transforming growth factor beta-1: Homodimer;
disulfide-linked. Transforming growth factor beta-1: Interacts
with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal
transduction (By similarity). {ECO:0000250|UniProtKB:P01137,
ECO:0000250|UniProtKB:P04202}.
-!- SUBCELLULAR LOCATION: Latency-associated peptide: Secreted,
extracellular space, extracellular matrix
{ECO:0000250|UniProtKB:P01137}.
-!- SUBCELLULAR LOCATION: Transforming growth factor beta-1: Secreted
{ECO:0000250|UniProtKB:P01137}.
-!- DOMAIN: Latency-associated peptide: The 'straitjacket' and 'arm'
domains encircle the Transforming growth factor beta-1 (TGF-beta-
1) monomers and are fastened together by strong bonding between
Lys-56 and Tyr-103/Tyr-104. {ECO:0000250|UniProtKB:P07200}.
-!- DOMAIN: Latency-associated peptide: The cell attachment site motif
mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8). The
motif locates to a long loop in the arm domain called the bowtie
tail. Integrin-binding stabilizes an alternative conformation of
the bowtie tail. Activation by integrin requires force application
by the actin cytoskeleton, which is resisted by the 'milieu
molecules' (such as LTBP1, LRRC32/GARP and/or LRRC33/NRROS),
resulting in distortion of the prodomain and release of the active
TGF-beta-1. {ECO:0000250|UniProtKB:P01137}.
-!- PTM: Transforming growth factor beta-1 proprotein: The precursor
proprotein is cleaved in the Golgi apparatus by FURIN to form
Transforming growth factor beta-1 (TGF-beta-1) and Latency-
associated peptide (LAP) chains, which remain non-covalently
linked, rendering TGF-beta-1 inactive.
{ECO:0000250|UniProtKB:P01137}.
-!- PTM: Latency-associated peptide: N-glycosylated. Deglycosylation
leads to activation of Transforming growth factor beta-1 (TGF-
beta-1); mechanisms triggering deglycosylation-driven activation
of TGF-beta-1 are however unclear. {ECO:0000250|UniProtKB:P01137}.
-!- 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: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: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: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:0014008; P:positive regulation of microglia differentiation; 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 signal transduction; ISS:AgBase.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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 signal transduction; 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: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 {ECO:0000305|PubMed:3185545}.
CHAIN 30 278 Latency-associated peptide.
{ECO:0000305|PubMed:3185545}.
/FTId=PRO_0000033760.
CHAIN 279 390 Transforming growth factor beta-1.
{ECO:0000305|PubMed:3185545}.
/FTId=PRO_0000033761.
REGION 30 74 Straightjacket domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 75 271 Arm domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 226 252 Bowtie tail.
{ECO:0000250|UniProtKB:P01137}.
MOTIF 244 246 Cell attachment site. {ECO:0000255}.
SITE 278 279 Cleavage; by FURIN.
{ECO:0000250|UniProtKB:P01137}.
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-1359 or C-1384 in
LTBP1); in inactive form.
{ECO:0000250|UniProtKB:P07200}.
DISULFID 223 223 Interchain (with C-225).
{ECO:0000250|UniProtKB:P01137}.
DISULFID 225 225 Interchain (with C-223).
{ECO:0000250|UniProtKB:P01137}.
DISULFID 285 294 {ECO:0000250|UniProtKB:P01137}.
DISULFID 293 356 {ECO:0000250|UniProtKB:P01137}.
DISULFID 322 387 {ECO:0000250|UniProtKB:P01137}.
DISULFID 326 389 {ECO:0000250|UniProtKB:P01137}.
DISULFID 355 355 Interchain.
{ECO:0000250|UniProtKB:P01137}.
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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