TGFB2_MOUSE
ID TGFB2_MOUSE Reviewed; 414 AA.
AC P27090; Q91VP5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Transforming growth factor beta-2 proprotein;
DE Contains:
DE RecName: Full=Latency-associated peptide;
DE Short=LAP;
DE Contains:
DE RecName: Full=Transforming growth factor beta-2;
DE Short=TGF-beta-2;
DE Flags: Precursor;
GN Name=Tgfb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2797004; DOI=10.1210/mend-3-7-1108;
RA Miller D.A., Lee A., Pelton R.W., Chen E.Y., Moses H.L., Derynck R.;
RT "Murine transforming growth factor-beta 2 cDNA sequence and expression in
RT adult tissues and embryos.";
RL Mol. Endocrinol. 3:1108-1114(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH NREP.
RX PubMed=14985127; DOI=10.1016/j.bbrc.2004.01.171;
RA Paliwal S., Shi J., Dhru U., Zhou Y., Schuger L.;
RT "P311 binds to the latency associated protein and downregulates the
RT expression of TGF-beta1 and TGF-beta2.";
RL Biochem. Biophys. Res. Commun. 315:1104-1109(2004).
RN [4]
RP INTERACTION WITH HTRA3.
RX PubMed=15206957; DOI=10.1111/j.1440-169x.2004.00743.x;
RA Tocharus J., Tsuchiya A., Kajikawa M., Ueta Y., Oka C., Kawaichi M.;
RT "Developmentally regulated expression of mouse HtrA3 and its role as an
RT inhibitor of TGF-beta signaling.";
RL Dev. Growth Differ. 46:257-274(2004).
RN [5]
RP INTERACTION WITH HTRA1.
RX PubMed=14973287; DOI=10.1242/dev.00999;
RA Oka C., Tsujimoto R., Kajikawa M., Koshiba-Takeuchi K., Ina J., Yano M.,
RA Tsuchiya A., Ueta Y., Soma A., Kanda H., Matsumoto M., Kawaichi M.;
RT "HtrA1 serine protease inhibits signaling mediated by Tgfbeta family
RT proteins.";
RL Development 131:1041-1053(2004).
RN [6]
RP INTERACTION WITH MFAP5.
RX PubMed=23963447; DOI=10.1074/jbc.m113.497727;
RA Combs M.D., Knutsen R.H., Broekelmann T.J., Toennies H.M., Brett T.J.,
RA Miller C.A., Kober D.L., Craft C.S., Atkinson J.J., Shipley J.M.,
RA Trask B.C., Mecham R.P.;
RT "Microfibril-associated glycoprotein 2 (MAGP2) loss of function has
RT pleiotropic effects in vivo.";
RL J. Biol. Chem. 288:28869-28880(2013).
CC -!- FUNCTION: [Transforming growth factor beta-2 proprotein]: Precursor of
CC the Latency-associated peptide (LAP) and Transforming growth factor
CC beta-2 (TGF-beta-2) chains, which constitute the regulatory and active
CC subunit of TGF-beta-2, respectively. {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P04202}.
CC -!- FUNCTION: [Latency-associated peptide]: Required to maintain the
CC Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state
CC during storage in extracellular matrix. Associates non-covalently with
CC TGF-beta-2 and regulates its activation via interaction with 'milieu
CC molecules', such as LTBP1 and LRRC32/GARP, that control activation of
CC TGF-beta-2. {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P04202}.
CC -!- FUNCTION: [Transforming growth factor beta-2]: Multifunctional protein
CC that regulates various processes such as angiogenesis and heart
CC development (By similarity). Activation into mature form follows
CC different steps: following cleavage of the proprotein in the Golgi
CC apparatus, Latency-associated peptide (LAP) and Transforming growth
CC factor beta-2 (TGF-beta-2) chains remain non-covalently linked
CC rendering TGF-beta-2 inactive during storage in extracellular matrix
CC (By similarity). At the same time, LAP chain interacts with 'milieu
CC molecules', such as LTBP1 and LRRC32/GARP, that control activation of
CC TGF-beta-2 and maintain it in a latent state during storage in
CC extracellular milieus (By similarity). Once activated following release
CC of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (TGFBR1 and
CC TGFBR2), which transduce signal (By similarity).
CC {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202,
CC ECO:0000250|UniProtKB:P61812}.
CC -!- SUBUNIT: Interacts with the serine proteases, HTRA1 and HTRA3
CC (PubMed:15206957, PubMed:14973287). Interacts with ASPN (By
CC similarity). Interacts with MFAP5 (PubMed:23963447).
CC {ECO:0000250|UniProtKB:P61812, ECO:0000269|PubMed:14973287,
CC ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:23963447}.
CC -!- SUBUNIT: [Latency-associated peptide]: Interacts with Transforming
CC growth factor beta-2 (TGF-beta-2) chain; interaction is non-covalent
CC and maintains (TGF-beta-2) in a latent state (By similarity). Interacts
CC with LRRC32/GARP; leading to regulate activation of TGF-beta-2 (By
CC similarity). Interacts with NREP; the interaction results in a decrease
CC in TGFB2 autoinduction (PubMed:14985127).
CC {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P61812,
CC ECO:0000269|PubMed:14985127}.
CC -!- SUBUNIT: [Transforming growth factor beta-2]: Transforming growth
CC factor beta-2: Homodimer; disulfide-linked (By similarity).
CC Transforming growth factor beta-2: Interacts with TGF-beta receptors
CC (TGFBR1 and TGFBR2), leading to signal transduction (By similarity).
CC {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P61812}.
CC -!- SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:P01137}.
CC -!- SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted
CC {ECO:0000250|UniProtKB:P01137}.
CC -!- PTM: [Transforming growth factor beta-2]: The precursor proprotein is
CC cleaved in the Golgi apparatus to form Transforming growth factor beta-
CC 2 (TGF-beta-2) and Latency-associated peptide (LAP) chains, which
CC remain non-covalently linked, rendering TGF-beta-2 inactive.
CC {ECO:0000250|UniProtKB:P01137}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X57413; CAA40672.1; -; mRNA.
DR EMBL; BC011170; AAH11170.1; -; mRNA.
DR CCDS; CCDS15601.1; -.
DR PIR; A40148; WFMSB2.
DR RefSeq; NP_033393.2; NM_009367.4.
DR PDB; 5TX2; X-ray; 1.82 A; A/B=303-414.
DR PDB; 5TX6; X-ray; 2.75 A; A/B/C=303-414.
DR PDBsum; 5TX2; -.
DR PDBsum; 5TX6; -.
DR AlphaFoldDB; P27090; -.
DR SMR; P27090; -.
DR BioGRID; 204160; 2.
DR ComplexPortal; CPX-827; TGF-beta-2 complex.
DR ComplexPortal; CPX-836; TGF-beta-2-TGFR complex.
DR STRING; 10090.ENSMUSP00000043849; -.
DR GlyConnect; 2777; 1 N-Linked glycan (1 site).
DR GlyGen; P27090; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P27090; -.
DR PhosphoSitePlus; P27090; -.
DR MaxQB; P27090; -.
DR PaxDb; P27090; -.
DR PeptideAtlas; P27090; -.
DR PRIDE; P27090; -.
DR ProteomicsDB; 263040; -.
DR Antibodypedia; 20732; 599 antibodies from 37 providers.
DR DNASU; 21808; -.
DR Ensembl; ENSMUST00000045288; ENSMUSP00000043849; ENSMUSG00000039239.
DR GeneID; 21808; -.
DR KEGG; mmu:21808; -.
DR UCSC; uc007dzo.2; mouse.
DR CTD; 7042; -.
DR MGI; MGI:98726; Tgfb2.
DR VEuPathDB; HostDB:ENSMUSG00000039239; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000157390; -.
DR HOGENOM; CLU_039840_0_0_1; -.
DR InParanoid; P27090; -.
DR OMA; IDSKVIR; -.
DR PhylomeDB; P27090; -.
DR TreeFam; TF318514; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR BioGRID-ORCS; 21808; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Tgfb2; mouse.
DR PRO; PR:P27090; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P27090; protein.
DR Bgee; ENSMUSG00000039239; Expressed in epithelium of cochlear duct and 337 other tissues.
DR ExpressionAtlas; P27090; baseline and differential.
DR Genevisible; P27090; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0099126; C:transforming growth factor beta complex; ISO:MGI.
DR GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; IC:ComplexPortal.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; TAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:UniProtKB.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:UniProtKB.
DR GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IDA:MGI.
DR GO; GO:0035910; P:ascending aorta morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060413; P:atrial septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003289; P:atrial septum primum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; TAS:DFLAT.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; IMP:BHF-UCL.
DR GO; GO:0010002; P:cardioblast differentiation; ISS:UniProtKB.
DR GO; GO:0001502; P:cartilage condensation; IGI:MGI.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:BHF-UCL.
DR GO; GO:0042416; P:dopamine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0048566; P:embryonic digestive tract development; ISS:AgBase.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:BHF-UCL.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; ISO:MGI.
DR GO; GO:0003274; P:endocardial cushion fusion; IMP:BHF-UCL.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0060325; P:face morphogenesis; IEP:UniProtKB.
DR GO; GO:0008347; P:glial cell migration; ISS:UniProtKB.
DR GO; GO:0001942; P:hair follicle development; IMP:UniProtKB.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0003179; P:heart valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IMP:BHF-UCL.
DR GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
DR GO; GO:0008584; P:male gonad development; IMP:BHF-UCL.
DR GO; GO:0003149; P:membranous septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0061037; P:negative regulation of cartilage development; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:AgBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:1905006; P:negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0050777; P:negative regulation of immune response; ISO:MGI.
DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; NAS:UniProtKB.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0003407; P:neural retina development; IMP:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; IMP:BHF-UCL.
DR GO; GO:0048666; P:neuron development; IMP:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; IDA:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:UniProtKB.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:1904238; P:pericyte cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:BHF-UCL.
DR GO; GO:0070237; P:positive regulation of activation-induced cell death of T cells; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IDA:UniProtKB.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:1904426; P:positive regulation of GTP binding; IDA:UniProtKB.
DR GO; GO:0045823; P:positive regulation of heart contraction; ISS:UniProtKB.
DR GO; GO:0050778; P:positive regulation of immune response; ISS:UniProtKB.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0045778; P:positive regulation of ossification; ISS:AgBase.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0051795; P:positive regulation of timing of catagen; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR GO; GO:1902256; P:regulation of apoptotic process involved in outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IMP:MGI.
DR GO; GO:0051794; P:regulation of timing of catagen; ISS:UniProtKB.
DR GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
DR GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
DR GO; GO:0001501; P:skeletal system development; IMP:BHF-UCL.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0048103; P:somatic stem cell division; IDA:UniProtKB.
DR GO; GO:1903701; P:substantia propria of cornea development; IMP:BHF-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060065; P:uterus development; IMP:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR016319; TGF-beta.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR003940; TGFb2.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR PIRSF; PIRSF001787; TGF-beta; 1.
DR PRINTS; PR01423; TGFBETA.
DR PRINTS; PR01425; TGFBETA2.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..414
FT /note="Transforming growth factor beta-2 proprotein"
FT /id="PRO_0000456181"
FT CHAIN 21..302
FT /note="Latency-associated peptide"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000033786"
FT CHAIN 303..414
FT /note="Transforming growth factor beta-2"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000033787"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 309..318
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 317..380
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 346..411
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 350..413
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 379
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT CONFLICT 95..96
FT /note="DE -> EQ (in Ref. 1; CAA40672)"
FT /evidence="ECO:0000305"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5TX2"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 385..394
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 397..408
FT /evidence="ECO:0007829|PDB:5TX2"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:5TX2"
SQ SEQUENCE 414 AA; 47589 MW; DB37A7C38881F286 CRC64;
MHYCVLSTFL LLHLVPVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP
DEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPS HLPSENAIPP
TFYRPYFRIV RFDVSTMEKN ASNLVKAEFR VFRLQNPKAR VAEQRIELYQ ILKSKDLTSP
TQRYIDSKVV KTRAEGEWLS FDVTDAVQEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP
NKSEELEARF AGIDGTSTYA SGDQKTIKST RKKTSGKTPH LLLMLLPSYR LESQQSSRRK
KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH
TKVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGNTPKI EQLSNMIVKS CKCS
