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

 TGFB1_PIG               Reviewed;         390 AA.
P07200; K7GQZ2; P08832;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
10-OCT-2018, sequence version 2.
16-OCT-2019, entry version 159.
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;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=3470708; DOI=10.1093/nar/15.7.3187;
Derynck R., Rhee L.;
"Sequence of the porcine transforming growth factor-beta precursor.";
Nucleic Acids Res. 15:3187-3187(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-114.
STRAIN=Miniature swine;
PubMed=2461367;
Kondaiah P., van Obberghen-Schilling E., Ludwig R.L., Dhar R.,
Sporn M.B., Roberts A.B.;
"cDNA cloning of porcine transforming growth factor-beta 1 mRNAs.
Evidence for alternate splicing and polyadenylation.";
J. Biol. Chem. 263:18313-18317(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3166520; DOI=10.1093/nar/16.17.8730;
Jakowlew S.B., Dillard P.J., Sporn M.B., Roberts A.B.;
"Nucleotide sequence of chicken transforming growth factor-beta 1
(TGF-beta 1).";
Nucleic Acids Res. 16:8730-8730(1988).
[4]
SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3166520 ORIGINATES FROM PIG.
Jakowlew S.B.;
Unpublished observations (MAR-1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12030934; DOI=10.1046/j.1365-2052.2002.t01-4-00876.x;
Wimmers K., Chomdej S., Ponsuksili S., Schellander K.;
"Polymorphism in the porcine transforming growth factor-beta1 gene.";
Anim. Genet. 33:234-235(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Duroc {ECO:0000312|Ensembl:ENSSSCP00000030317};
Porcine genome sequencing project;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 279-322.
PubMed=2879635; DOI=10.1016/0092-8674(87)90192-9;
Cheifetz S., Weatherbee J.A., Tsang M.L.S., Anderson J.K., Mole J.E.,
Lucas R., Massague J.;
"The transforming growth factor-beta system, a complex pattern of
cross-reactive ligands and receptors.";
Cell 48:409-415(1987).
[8]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 30-390 OF MUTANT SER-33,
SUBUNIT, GLYCOSYLATION AT ASN-82 AND ASN-136, DISULFIDE BONDS,
MUTAGENESIS OF TYR-103 AND TYR-104, AND ACTIVATION MECHANISM.
PubMed=21677751; DOI=10.1038/nature10152;
Shi M., Zhu J., Wang R., Chen X., Mi L., Walz T., Springer T.A.;
"Latent TGF-beta structure and activation.";
Nature 474:343-349(2011).
[9] {ECO:0000244|PDB:5VQF}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 30-390, AND DISULFIDE BONDS.
PubMed=29109152; DOI=10.1074/jbc.m117.809657;
Zhao B., Xu S., Dong X., Lu C., Springer T.A.;
"Prodomain-growth factor swapping in the structure of pro-TGF-beta1.";
J. Biol. Chem. 293:1579-1589(2018).
-!- 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}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-907660, EBI-907660;
Q99K41:Emilin1 (xeno); NbExp=2; IntAct=EBI-907660, EBI-906561;
P37173:TGFBR2 (xeno); NbExp=2; IntAct=EBI-907660, EBI-296151;
-!- 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:0000269|PubMed:21677751}.
-!- 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 (PubMed:21677751). 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 (By similarity).
{ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:21677751}.
-!- 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}.
-!- CAUTION: PubMed:3166520 sequence which was said to originate from
chicken. It however seems to originate from pig.
{ECO:0000305|PubMed:3166520, ECO:0000305|Ref.4}.
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EMBL; Y00111; CAA68291.1; -; mRNA.
EMBL; M23703; AAA64616.1; -; mRNA.
EMBL; X12373; CAA30933.1; -; mRNA.
EMBL; AF461808; AAL57902.1; -; mRNA.
EMBL; AEMK02000041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A27512; A27512.
PIR; S01413; S01413.
RefSeq; NP_999180.2; NM_214015.2.
PDB; 3RJR; X-ray; 3.05 A; A/B/C/D=30-390.
PDB; 5VQF; X-ray; 2.90 A; A/B/C/D=30-390.
PDBsum; 3RJR; -.
PDBsum; 5VQF; -.
SMR; P07200; -.
DIP; DIP-35732N; -.
IntAct; P07200; 3.
STRING; 9823.ENSSSCP00000003267; -.
iPTMnet; P07200; -.
PaxDb; P07200; -.
PRIDE; P07200; -.
Ensembl; ENSSSCT00000036469; ENSSSCP00000030317; ENSSSCG00000003017.
Ensembl; ENSSSCT00070003600; ENSSSCP00070002984; ENSSSCG00070001924.
GeneID; 397078; -.
KEGG; ssc:397078; -.
CTD; 7040; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00940000160457; -.
HOGENOM; HOG000290198; -.
InParanoid; P07200; -.
KO; K13375; -.
OMA; FSAHCSC; -.
OrthoDB; 643840at2759; -.
ChiTaRS; TGFB1; pig.
Proteomes; UP000008227; Chromosome 6.
Bgee; ENSSSCG00000003017; Expressed in 6 organ(s), highest expression level in lung.
ExpressionAtlas; P07200; baseline and differential.
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:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003823; F:antigen binding; ISS:AgBase.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
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:0002460; P:adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains; IEA:Ensembl.
GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
GO; GO:0006754; P:ATP biosynthetic process; ISS:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0060751; P:branch elongation involved in mammary gland duct branching; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
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:1990402; P:embryonic liver development; IEA:Ensembl.
GO; GO:0007492; P:endoderm development; IEA:Ensembl.
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:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
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:UniProtKB.
GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
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:0032943; P:mononuclear cell proliferation; IEA:Ensembl.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0070168; P:negative regulation of biomineral tissue development; IEA:Ensembl.
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 population proliferation; ISS:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0045918; P:negative regulation of cytolysis; IEA:Ensembl.
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:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
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:0030279; P:negative regulation of ossification; IEA:Ensembl.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IEA:Ensembl.
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:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
GO; GO:0043932; P:ossification involved in bone remodeling; ISS:AgBase.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
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:2000727; P:positive regulation of cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IEA:Ensembl.
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 population 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:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
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:0042482; P:positive regulation of odontogenesis; IEA:Ensembl.
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:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
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:1903911; P:positive regulation of receptor clustering; IEA:Ensembl.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
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:0043117; P:positive regulation of vascular permeability; IEA:Ensembl.
GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0061035; P:regulation of cartilage development; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0051101; P:regulation of DNA binding; ISS:UniProtKB.
GO; GO:0032667; P:regulation of interleukin-23 production; IEA:Ensembl.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0042306; P:regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0060390; P:regulation of SMAD protein signal transduction; ISS:UniProtKB.
GO; GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl.
GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045066; P:regulatory T cell differentiation; IEA:Ensembl.
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:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0002513; P:tolerance induction to self antigen; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:1905313; P:transforming growth factor beta receptor signaling pathway involved in heart development; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
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;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Glycoprotein; Growth factor; Mitogen; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 29 {ECO:0000250|UniProtKB:P01137}.
CHAIN 30 278 Latency-associated peptide.
{ECO:0000305|PubMed:2879635}.
/FTId=PRO_0000033768.
CHAIN 279 390 Transforming growth factor beta-1.
{ECO:0000305|PubMed:2879635}.
/FTId=PRO_0000033769.
REGION 30 74 Straightjacket domain.
{ECO:0000269|PubMed:21677751}.
REGION 75 271 Arm domain.
{ECO:0000269|PubMed:21677751}.
REGION 226 252 Bowtie tail.
{ECO:0000250|UniProtKB:P01137}.
MOTIF 244 246 Cell attachment site.
{ECO:0000269|PubMed:21677751}.
SITE 278 279 Cleavage; by FURIN.
{ECO:0000250|UniProtKB:P01137}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3RJR,
ECO:0000269|PubMed:21677751}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3RJR,
ECO:0000269|PubMed:21677751}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 33 Interchain (with C-? in LTBP1 TB3
domain); in inactive form.
{ECO:0000269|PubMed:21677751}.
DISULFID 223 223 Interchain (with C-225).
{ECO:0000244|PDB:3RJR,
ECO:0000244|PDB:5VQF,
ECO:0000269|PubMed:21677751,
ECO:0000269|PubMed:29109152}.
DISULFID 225 225 Interchain (with C-223).
{ECO:0000244|PDB:3RJR,
ECO:0000244|PDB:5VQF,
ECO:0000269|PubMed:21677751,
ECO:0000269|PubMed:29109152}.
DISULFID 285 294 {ECO:0000244|PDB:3RJR,
ECO:0000244|PDB:5VQF,
ECO:0000269|PubMed:21677751,
ECO:0000269|PubMed:29109152}.
DISULFID 293 356 {ECO:0000244|PDB:3RJR,
ECO:0000244|PDB:5VQF,
ECO:0000269|PubMed:21677751,
ECO:0000269|PubMed:29109152}.
DISULFID 322 387 {ECO:0000244|PDB:3RJR,
ECO:0000244|PDB:5VQF,
ECO:0000269|PubMed:21677751,
ECO:0000269|PubMed:29109152}.
DISULFID 326 389 {ECO:0000244|PDB:3RJR,
ECO:0000244|PDB:5VQF,
ECO:0000269|PubMed:21677751,
ECO:0000269|PubMed:29109152}.
DISULFID 355 355 Interchain. {ECO:0000244|PDB:3RJR,
ECO:0000244|PDB:5VQF,
ECO:0000269|PubMed:21677751,
ECO:0000269|PubMed:29109152}.
VARIANT 114 114 V -> L. {ECO:0000269|PubMed:3470708}.
MUTAGEN 103 103 Y->A,K,T: Results in spontaneous, non
integrin-dependent activation.
{ECO:0000269|PubMed:21677751}.
MUTAGEN 104 104 Y->A,C,S,T: Results in spontaneous, non
integrin-dependent activation.
{ECO:0000269|PubMed:21677751}.
CONFLICT 6 7 LR -> PG (in Ref. 3; CAA30933).
{ECO:0000305}.
CONFLICT 180 180 R -> G (in Ref. 3; CAA30933).
{ECO:0000305}.
CONFLICT 237 237 N -> NA (in Ref. 3; CAA30933).
{ECO:0000305}.
HELIX 32 56 {ECO:0000244|PDB:5VQF}.
HELIX 75 85 {ECO:0000244|PDB:5VQF}.
STRAND 89 91 {ECO:0000244|PDB:3RJR}.
STRAND 106 112 {ECO:0000244|PDB:5VQF}.
STRAND 116 119 {ECO:0000244|PDB:5VQF}.
TURN 120 126 {ECO:0000244|PDB:5VQF}.
STRAND 130 136 {ECO:0000244|PDB:5VQF}.
HELIX 137 143 {ECO:0000244|PDB:5VQF}.
STRAND 144 146 {ECO:0000244|PDB:3RJR}.
HELIX 147 149 {ECO:0000244|PDB:5VQF}.
STRAND 150 159 {ECO:0000244|PDB:5VQF}.
STRAND 166 172 {ECO:0000244|PDB:5VQF}.
STRAND 175 177 {ECO:0000244|PDB:5VQF}.
STRAND 180 187 {ECO:0000244|PDB:5VQF}.
STRAND 194 199 {ECO:0000244|PDB:5VQF}.
HELIX 201 209 {ECO:0000244|PDB:5VQF}.
STRAND 213 221 {ECO:0000244|PDB:5VQF}.
STRAND 224 228 {ECO:0000244|PDB:5VQF}.
STRAND 231 235 {ECO:0000244|PDB:5VQF}.
STRAND 251 254 {ECO:0000244|PDB:3RJR}.
STRAND 257 262 {ECO:0000244|PDB:5VQF}.
HELIX 265 267 {ECO:0000244|PDB:5VQF}.
HELIX 282 285 {ECO:0000244|PDB:5VQF}.
STRAND 291 296 {ECO:0000244|PDB:5VQF}.
STRAND 299 301 {ECO:0000244|PDB:5VQF}.
TURN 302 306 {ECO:0000244|PDB:5VQF}.
STRAND 310 313 {ECO:0000244|PDB:5VQF}.
STRAND 315 318 {ECO:0000244|PDB:5VQF}.
STRAND 321 323 {ECO:0000244|PDB:5VQF}.
HELIX 329 331 {ECO:0000244|PDB:5VQF}.
STRAND 332 334 {ECO:0000244|PDB:5VQF}.
HELIX 337 340 {ECO:0000244|PDB:5VQF}.
HELIX 341 345 {ECO:0000244|PDB:5VQF}.
TURN 348 350 {ECO:0000244|PDB:5VQF}.
STRAND 351 353 {ECO:0000244|PDB:5VQF}.
STRAND 355 370 {ECO:0000244|PDB:5VQF}.
STRAND 373 384 {ECO:0000244|PDB:5VQF}.
STRAND 386 390 {ECO:0000244|PDB:5VQF}.
SEQUENCE 390 AA; 44280 MW; A9FC32859BA6AF06 CRC64;
MPPSGLRLLP LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
SPPSQGDVPP GPLPEAVLAL YNSTRDRVAG ESVEPEPEPE ADYYAKEVTR VLMVESGNQI
YDKFKGTPHS LYMLFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNDSWR
YLSNRLLAPS DSPEWLSFDV TGVVRQWLTR REAIEGFRLS AHCSCDSKDN TLHVEINGFN
SGRRGDLATI HGMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


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Related Genes :
[TGFB1 TGFB] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB2] Transforming growth factor beta-2 proprotein (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB3] Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)]
[TGFB2] Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFBR1 ALK5 SKR4] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr3] Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Lefty1 Ebaf Lefty Stra3 Tgfb4] Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4)
[TGFBR2] TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[LEFTY2 EBAF LEFTA LEFTYA TGFB4 PSEC0024] Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)
[Nrros Lrrc33] Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species)
[LTBP4] Latent-transforming growth factor beta-binding protein 4 (LTBP-4)
[tgfb1] Transforming growth factor beta-1 proprotein (TGF-beta-5) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGF beta TGFB1] Transforming growth factor beta

Bibliography :