TGFB2_RAT
ID TGFB2_RAT Reviewed; 442 AA.
AC Q07257; Q63574; Q9QW26; Q9R281; Q9R298; Q9R2B8; Q9WUQ8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 170.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TGF-BETA2A AND TGF-BETA2B), TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Muscle;
RX PubMed=10899565; DOI=10.1016/s0304-419x(00)00012-3;
RA Koishi K., Dalzell K.G., McLennan I.S.;
RT "The expression and structure of TGF-beta2 transcripts in rat muscles.";
RL Biochim. Biophys. Acta 1492:311-319(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TGF-BETA2A).
RC STRAIN=Wistar;
RX PubMed=11014222; DOI=10.1210/endo.141.10.7728;
RA Konrad L., Albrecht M., Renneberg H., Aumuller G.;
RT "Transforming growth factor-beta2 mediates mesenchymal-epithelial
RT interactions of testicular somatic cells.";
RL Endocrinology 141:3679-3686(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TGF-BETA2A).
RA Plisov S.Y., Ivanov S.V., Plisova T.M., Lerman M., Perantoni A.O.;
RT "Rat transforming growth factor-beta2, complete coding sequence.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 278-348.
RX PubMed=8509457; DOI=10.1083/jcb.121.6.1397;
RA McKinnon R.D., Piras G., Ida J., Dubois-Dalq M.;
RT "A role for TGF-beta in oligodendrocyte differentiation.";
RL J. Cell Biol. 121:1397-1407(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 366-441.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=8486763; DOI=10.1172/jci116412;
RA Nishida M., Springhorn J.P., Kelly R.A., Smith T.W.;
RT "Cell-cell signaling between adult rat ventricular myocytes and cardiac
RT microvascular endothelial cells in heterotypic primary culture.";
RL J. Clin. Invest. 91:1934-1941(1993).
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 (By
CC similarity). Interacts with ASPN (By similarity). Interacts with MFAP5
CC (By similarity). {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P27090, ECO:0000250|UniProtKB:P61812}.
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 (By similarity). {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P27090, ECO:0000250|UniProtKB:P61812}.
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:P27090,
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=TGF-beta2B;
CC IsoId=Q07257-1; Sequence=Displayed;
CC Name=TGF-beta2A;
CC IsoId=Q07257-2; Sequence=VSP_006418, VSP_006419;
CC -!- TISSUE SPECIFICITY: [Isoform TGF-beta2B]: Expressed in the aorta,
CC primary bronchus, uterus, heart, skeletal muscle, sciatic nerve and
CC spinal cord but not in the intestine. {ECO:0000269|PubMed:10899565}.
CC -!- DEVELOPMENTAL STAGE: High expression at E14. Sharp decline in
CC expression between E16 and E18. Absent in adulthood.
CC {ECO:0000269|PubMed:10899565}.
CC -!- INDUCTION: Both isoforms down-regulated during muscle development. Up-
CC regulated after denervation. {ECO:0000269|PubMed:10899565}.
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}.
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DR EMBL; AF153012; AAD34159.1; -; mRNA.
DR EMBL; AF153013; AAD34160.1; -; mRNA.
DR EMBL; AJ132718; CAB42003.1; -; mRNA.
DR EMBL; AF135598; AAD24484.1; -; mRNA.
DR EMBL; X71904; CAA50723.1; -; mRNA.
DR EMBL; M96643; AAA88514.1; ALT_SEQ; mRNA.
DR PIR; A40699; A40699.
DR RefSeq; NP_112393.1; NM_031131.1. [Q07257-1]
DR RefSeq; XP_006250510.1; XM_006250448.3. [Q07257-2]
DR AlphaFoldDB; Q07257; -.
DR SMR; Q07257; -.
DR STRING; 10116.ENSRNOP00000003313; -.
DR GlyGen; Q07257; 3 sites.
DR PhosphoSitePlus; Q07257; -.
DR PaxDb; Q07257; -.
DR PRIDE; Q07257; -.
DR GeneID; 81809; -.
DR KEGG; rno:81809; -.
DR UCSC; RGD:70491; rat. [Q07257-1]
DR CTD; 7042; -.
DR RGD; 70491; Tgfb2.
DR eggNOG; KOG3900; Eukaryota.
DR InParanoid; Q07257; -.
DR OrthoDB; 643840at2759; -.
DR PhylomeDB; Q07257; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR PRO; PR:Q07257; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002418; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; Q07257; baseline and differential.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
DR GO; GO:0005576; C:extracellular region; ISS:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:AgBase.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0047485; F:protein N-terminus binding; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:AgBase.
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:AgBase.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0035910; P:ascending aorta morphogenesis; ISO:RGD.
DR GO; GO:0060413; P:atrial septum morphogenesis; ISO:RGD.
DR GO; GO:0003289; P:atrial septum primum morphogenesis; ISO:RGD.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:AgBase.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; ISO:RGD.
DR GO; GO:0010002; P:cardioblast differentiation; ISS:AgBase.
DR GO; GO:0001502; P:cartilage condensation; ISO:RGD.
DR GO; GO:0008219; P:cell death; ISS:AgBase.
DR GO; GO:0016477; P:cell migration; ISS:AgBase.
DR GO; GO:0000902; P:cell morphogenesis; ISS:AgBase.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
DR GO; GO:0030199; P:collagen fibril organization; ISS:AgBase.
DR GO; GO:1904888; P:cranial skeletal system development; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0048566; P:embryonic digestive tract development; ISS:AgBase.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IDA:RGD.
DR GO; GO:0003274; P:endocardial cushion fusion; ISO:RGD.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:AgBase.
DR GO; GO:0001654; P:eye development; ISS:AgBase.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0060364; P:frontal suture morphogenesis; IEP:RGD.
DR GO; GO:0008347; P:glial cell migration; ISS:AgBase.
DR GO; GO:0001942; P:hair follicle development; ISS:AgBase.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:AgBase.
DR GO; GO:0003007; P:heart morphogenesis; ISS:AgBase.
DR GO; GO:0003179; P:heart valve morphogenesis; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0030902; P:hindbrain development; IEP:RGD.
DR GO; GO:0048839; P:inner ear development; IEP:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0030324; P:lung development; TAS:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0003149; P:membranous septum morphogenesis; ISO:RGD.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISS:AgBase.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0061037; P:negative regulation of cartilage development; ISO:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:AgBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:AgBase.
DR GO; GO:1905006; P:negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0050777; P:negative regulation of immune response; IDA:RGD.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IDA:RGD.
DR GO; GO:0003407; P:neural retina development; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; ISO:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:RGD.
DR GO; GO:0031016; P:pancreas development; IEP:RGD.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:AgBase.
DR GO; GO:1904238; P:pericyte cell differentiation; ISO:RGD.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISO:RGD.
DR GO; GO:0070237; P:positive regulation of activation-induced cell death of T cells; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:AgBase.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:AgBase.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS: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:AgBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:AgBase.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISO:RGD.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:RGD.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1904426; P:positive regulation of GTP binding; ISO:RGD.
DR GO; GO:0045823; P:positive regulation of heart contraction; ISS:AgBase.
DR GO; GO:0050778; P:positive regulation of immune response; ISS:UniProtKB.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:AgBase.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:AgBase.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0045778; P:positive regulation of ossification; ISS:AgBase.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:AgBase.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:AgBase.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:AgBase.
DR GO; GO:0051795; P:positive regulation of timing of catagen; ISS:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:AgBase.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:1902256; P:regulation of apoptotic process involved in outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; TAS:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; ISO:RGD.
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:AgBase.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; ISS:AgBase.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; ISS:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
DR GO; GO:0062009; P:secondary palate development; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISS:AgBase.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:AgBase.
DR GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
DR GO; GO:1903701; P:substantia propria of cornea development; ISO:RGD.
DR GO; GO:0030878; P:thyroid gland development; IEP:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
DR GO; GO:0060065; P:uterus development; ISO:RGD.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IMP:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; 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..442
FT /note="Transforming growth factor beta-2 proprotein"
FT /id="PRO_0000456184"
FT CHAIN 21..330
FT /note="Latency-associated peptide"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000033790"
FT CHAIN 331..442
FT /note="Transforming growth factor beta-2"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000033791"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 337..346
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 345..408
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 374..439
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 378..441
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 407
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT VAR_SEQ 116..143
FT /note="Missing (in isoform TGF-beta2A)"
FT /evidence="ECO:0000303|PubMed:10899565,
FT ECO:0000303|PubMed:11014222, ECO:0000303|Ref.3"
FT /id="VSP_006418"
FT VAR_SEQ 144
FT /note="D -> N (in isoform TGF-beta2A)"
FT /evidence="ECO:0000303|PubMed:10899565,
FT ECO:0000303|PubMed:11014222, ECO:0000303|Ref.3"
FT /id="VSP_006419"
FT CONFLICT 99
FT /note="Y -> C (in Ref. 2; CAB42003)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="L -> P (in Ref. 3; AAD24484)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="D -> H (in Ref. 2; CAB42003 and 4; CAA50723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 50534 MW; 69C81A19CE06C253 CRC64;
MHYCVLRTFL LLHLVPVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP
DEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPS HFPSETVCPV
VTTSSGSVGS FCSIQSQVLC GYLDAIPPTF YRPYFRIVRF DVSTMEKNAS NLVKAEFRVF
RLQNPKARVA EQRIELYQIL KSKDLTSPTQ RYIDSKVVKT RAEGEWLSFD VTDAVHEWLH
HKDRNLGFKI SLHCPCCTFI PSNNYIIPNK SQELEARFAG IDGTSTYASG DQKTIKSTRK
KSSGKTPHLL LMLLPSYRLE SQQSSRRRKR ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW
KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY
YIGNTPKIEQ LSNMIVKSCK CS
