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Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]

 TGFB2_PIG               Reviewed;         435 AA.
P09858;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
07-APR-2021, entry version 130.
RecName: Full=Transforming growth factor beta-2 proprotein;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-2;
Short=TGF-beta-2;
Flags: Precursor;
Name=TGFB2;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-435.
TISSUE=Lung;
Zhou Y.;
Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 303-345.
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).
-!- FUNCTION: Transforming growth factor beta-2 proprotein: Precursor of
the Latency-associated peptide (LAP) and Transforming growth factor
beta-2 (TGF-beta-2) chains, which constitute the regulatory and active
subunit of TGF-beta-2, respectively. {ECO:0000250|UniProtKB:P01137,
ECO:0000250|UniProtKB:P04202}.
-!- FUNCTION: [Latency-associated peptide]: Required to maintain the
Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state
during storage in extracellular matrix. Associates non-covalently with
TGF-beta-2 and regulates its activation via interaction with 'milieu
molecules', such as LTBP1 and LRRC32/GARP, that control activation of
TGF-beta-2. {ECO:0000250|UniProtKB:P01137,
ECO:0000250|UniProtKB:P04202}.
-!- FUNCTION: Transforming growth factor beta-2: Multifunctional protein
that regulates various processes such as angiogenesis and heart
development (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-2 (TGF-beta-2) chains remain non-covalently linked
rendering TGF-beta-2 inactive during storage in extracellular matrix
(By similarity). At the same time, LAP chain interacts with 'milieu
molecules', such as LTBP1 and LRRC32/GARP, that control activation of
TGF-beta-2 and maintain it in a latent state during storage in
extracellular milieus (By similarity). Once activated following release
of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (TGFBR1 and
TGFBR2), which transduce signal (By similarity).
{ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202,
ECO:0000250|UniProtKB:P61812}.
-!- SUBUNIT: Interacts with the serine proteases, HTRA1 and HTRA3 (By
similarity). Interacts with ASPN (By similarity). Interacts with MFAP5
(By similarity). Latency-associated peptide: Interacts with
Transforming growth factor beta-2 (TGF-beta-2) chain; interaction is
non-covalent and maintains (TGF-beta-2) in a latent state (By
similarity). Latency-associated peptide: Interacts with LRRC32/GARP;
leading to regulate activation of TGF-beta-2 (By similarity). Latency-
associated peptide: Interacts with NREP; the interaction results in a
decrease in TGFB2 autoinduction (By similarity). Transforming growth
factor beta-2: Homodimer; disulfide-linked (By similarity).
Transforming growth factor beta-2: Interacts with TGF-beta receptors
(TGFBR1 and TGFBR2), leading to signal transduction (By similarity).
{ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P27090,
ECO:0000250|UniProtKB:P61812}.
-!- SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted,
extracellular space, extracellular matrix
{ECO:0000250|UniProtKB:P01137}.
-!- SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted
{ECO:0000250|UniProtKB:P01137}.
-!- PTM: Transforming growth factor beta-2 proprotein: The precursor
proprotein is cleaved in the Golgi apparatus to form Transforming
growth factor beta-2 (TGF-beta-2) and Latency-associated peptide (LAP)
chains, which remain non-covalently linked, rendering TGF-beta-2
inactive. {ECO:0000250|UniProtKB:P01137}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; L08375; AAB03850.1; -; mRNA.
PIR; B26356; B26356.
SMR; P09858; -.
PRIDE; P09858; -.
InParanoid; P09858; -.
Proteomes; UP000008227; Unplaced.
Proteomes; UP000314985; Unplaced.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:AgBase.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; ISS:UniProtKB.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:UniProtKB.
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:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:UniProtKB.
GO; GO:0010002; P:cardioblast differentiation; ISS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0008219; P:cell death; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
GO; GO:0042416; P:dopamine biosynthetic process; ISS:UniProtKB.
GO; GO:0048566; P:embryonic digestive tract development; ISS:AgBase.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0001654; P:eye development; ISS:UniProtKB.
GO; GO:0008347; P:glial cell migration; ISS:UniProtKB.
GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
GO; GO:0001707; P:mesoderm formation; TAS:UniProtKB.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:AgBase.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:UniProtKB.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:UniProtKB.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0045823; P:positive regulation of heart contraction; ISS:UniProtKB.
GO; GO:0050778; P:positive regulation of immune response; IDA:UniProtKB.
GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0045778; P:positive regulation of ossification; ISS:AgBase.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
GO; GO:0051795; P:positive regulation of timing of catagen; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0051794; P:regulation of timing of catagen; ISS:UniProtKB.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; ISS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; 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:0060395; P:SMAD protein signal transduction; ISS:BHF-UCL.
GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; 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; IPR003940; TGFb2.
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; PR01425; TGFBETA2.
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; Direct protein sequencing;
Disulfide bond; Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1..20
/evidence="ECO:0000255"
CHAIN 21..302
/note="Latency-associated peptide"
/evidence="ECO:0000250|UniProtKB:P61812"
/id="PRO_0000033788"
CHAIN 303..435
/note="Transforming growth factor beta-2"
/evidence="ECO:0000250|UniProtKB:P61812"
/id="PRO_0000033789"
CARBOHYD 72
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 140
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 241
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 309..318
/evidence="ECO:0000250|UniProtKB:P61812"
DISULFID 317..380
/evidence="ECO:0000250|UniProtKB:P61812"
DISULFID 346..411
/evidence="ECO:0000250|UniProtKB:P61812"
DISULFID 350..413
/evidence="ECO:0000250|UniProtKB:P61812"
DISULFID 379
/note="Interchain"
/evidence="ECO:0000250|UniProtKB:P61812"
SEQUENCE 435 AA; 49922 MW; 438282E288B32322 CRC64;
MHYCVLSAFL LLHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP
EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPP FFPSENAIPP
TFYRPYFRIV RFDVSAMEKN ASNLVKAEFR VFRLQNPKAR VAEQRIELYQ ILKSKDLTSP
TQRYIDSKVV KTRAEGEWLS FDVTDAVHEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP
NKSEELEARF AGIDGTSTYT SGDQKTIKST RKKNSGKTPH LLLMLLPSYG LESQQSNRRK
KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH
SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI EQLSNMIVKS CKCSKTKLAA
FARLYHSHSN LGSET


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[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)]
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[] Latency-associated peptide (Transforming growth factor beta-2) (Transforming growth factor beta-2 proprotein)
[TGFB1] Latency-associated peptide (Transforming growth factor beta-1) (Transforming growth factor beta-1 proprotein) (Fragment)
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[CB1_001276006] Transforming growth factor beta-1 (Transforming growth factor beta-1 proprotein)
[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) (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) (ESK2) (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)
[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)

Bibliography :
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