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

 TGFB2_RAT               Reviewed;         442 AA.
Q07257; Q63574; Q9QW26; Q9R281; Q9R298; Q9R2B8; Q9WUQ8;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
15-MAY-2002, sequence version 2.
07-NOV-2018, entry version 155.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TGF-BETA2A AND TGF-BETA2B),
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=Wistar; TISSUE=Muscle;
PubMed=10899565; DOI=10.1016/S0304-419X(00)00012-3;
Koishi K., Dalzell K.G., McLennan I.S.;
"The expression and structure of TGF-beta2 transcripts in rat
muscles.";
Biochim. Biophys. Acta 1492:311-319(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TGF-BETA2A).
STRAIN=Wistar;
PubMed=11014222; DOI=10.1210/endo.141.10.7728;
Konrad L., Albrecht M., Renneberg H., Aumuller G.;
"Transforming growth factor-beta2 mediates mesenchymal-epithelial
interactions of testicular somatic cells.";
Endocrinology 141:3679-3686(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TGF-BETA2A).
Plisov S.Y., Ivanov S.V., Plisova T.M., Lerman M., Perantoni A.O.;
"Rat transforming growth factor-beta2, complete coding sequence.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 278-348.
PubMed=8509457; DOI=10.1083/jcb.121.6.1397;
McKinnon R.D., Piras G., Ida J., Dubois-Dalq M.;
"A role for TGF-beta in oligodendrocyte differentiation.";
J. Cell Biol. 121:1397-1407(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 366-441.
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=8486763; DOI=10.1172/JCI116412;
Nishida M., Springhorn J.P., Kelly R.A., Smith T.W.;
"Cell-cell signaling between adult rat ventricular myocytes and
cardiac microvascular endothelial cells in heterotypic primary
culture.";
J. Clin. Invest. 91:1934-1941(1993).
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=TGF-beta2B;
IsoId=Q07257-1; Sequence=Displayed;
Name=TGF-beta2A;
IsoId=Q07257-2; Sequence=VSP_006418, VSP_006419;
-!- TISSUE SPECIFICITY: Isoform TGF-beta2B: Expressed in the aorta,
primary bronchus, uterus, heart, skeletal muscle, sciatic nerve
and spinal cord but not in the intestine.
{ECO:0000269|PubMed:10899565}.
-!- DEVELOPMENTAL STAGE: High expression at E14. Sharp decline in
expression between E16 and E18. Absent in adulthood.
{ECO:0000269|PubMed:10899565}.
-!- INDUCTION: Both isoforms down-regulated during muscle development.
Up-regulated after denervation. {ECO:0000269|PubMed:10899565}.
-!- 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; AF153012; AAD34159.1; -; mRNA.
EMBL; AF153013; AAD34160.1; -; mRNA.
EMBL; AJ132718; CAB42003.1; -; mRNA.
EMBL; AF135598; AAD24484.1; -; mRNA.
EMBL; X71904; CAA50723.1; -; mRNA.
EMBL; M96643; AAA88514.1; ALT_SEQ; mRNA.
PIR; A40699; A40699.
RefSeq; NP_112393.1; NM_031131.1. [Q07257-1]
RefSeq; XP_006250510.1; XM_006250448.3. [Q07257-2]
UniGene; Rn.24539; -.
ProteinModelPortal; Q07257; -.
STRING; 10116.ENSRNOP00000003313; -.
PhosphoSitePlus; Q07257; -.
PaxDb; Q07257; -.
PRIDE; Q07257; -.
Ensembl; ENSRNOT00000087023; ENSRNOP00000074059; ENSRNOG00000002418. [Q07257-2]
GeneID; 81809; -.
KEGG; rno:81809; -.
UCSC; RGD:70491; rat. [Q07257-1]
CTD; 7042; -.
RGD; 70491; Tgfb2.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00910000143982; -.
HOVERGEN; HBG074115; -.
InParanoid; Q07257; -.
KO; K13376; -.
PhylomeDB; Q07257; -.
Reactome; R-RNO-114608; Platelet degranulation.
Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
PRO; PR:Q07257; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000002418; Expressed in 10 organ(s), highest expression level in lung.
ExpressionAtlas; Q07257; baseline and differential.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005604; C:basement membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
GO; GO:0005576; C:extracellular region; ISS:AgBase.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
GO; GO:0001540; F:amyloid-beta binding; ISS:AgBase.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0047485; F:protein N-terminus binding; IMP:RGD.
GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0032147; P:activation of protein kinase activity; ISS:AgBase.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:AgBase.
GO; GO:0010002; P:cardioblast differentiation; ISS:AgBase.
GO; GO:0007050; P:cell cycle arrest; ISS:AgBase.
GO; GO:0008219; P:cell death; ISS:AgBase.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0016477; P:cell migration; ISS:AgBase.
GO; GO:0000902; P:cell morphogenesis; ISS:AgBase.
GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
GO; GO:0030199; P:collagen fibril organization; ISS:AgBase.
GO; GO:0048565; P:digestive tract development; IEP:RGD.
GO; GO:0042416; P:dopamine biosynthetic process; ISS:UniProtKB.
GO; GO:0048566; P:embryonic digestive tract development; ISS:AgBase.
GO; GO:0048702; P:embryonic neurocranium morphogenesis; IDA:RGD.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:AgBase.
GO; GO:0001654; P:eye development; ISS:AgBase.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0060364; P:frontal suture morphogenesis; IEP:RGD.
GO; GO:0008347; P:glial cell migration; ISS:AgBase.
GO; GO:0001942; P:hair follicle development; ISS:AgBase.
GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:AgBase.
GO; GO:0003007; P:heart morphogenesis; ISS:AgBase.
GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
GO; GO:0030902; P:hindbrain development; IEP:RGD.
GO; GO:0048839; P:inner ear development; IEP:RGD.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0030324; P:lung development; TAS:RGD.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISS:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:0030308; P:negative regulation of cell growth; ISS:AgBase.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:AgBase.
GO; GO:0050777; P:negative regulation of immune response; IDA:RGD.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IDA:RGD.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0031016; P:pancreas development; IEP:RGD.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:AgBase.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:AgBase.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:AgBase.
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:AgBase.
GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:AgBase.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0045823; P:positive regulation of heart contraction; ISS:AgBase.
GO; GO:0050778; P:positive regulation of immune response; ISS:UniProtKB.
GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:AgBase.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:AgBase.
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:AgBase.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:AgBase.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:AgBase.
GO; GO:0051795; P:positive regulation of timing of catagen; ISS:AgBase.
GO; GO:0006468; P:protein phosphorylation; ISS:AgBase.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0001558; P:regulation of cell growth; TAS:RGD.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; 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:AgBase.
GO; GO:0009409; P:response to cold; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0032570; P:response to progesterone; ISS:AgBase.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
GO; GO:0009611; P:response to wounding; ISS:AgBase.
GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
GO; GO:0023014; P:signal transduction by protein phosphorylation; ISS:AgBase.
GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
GO; GO:0060395; P:SMAD protein signal transduction; ISS:BHF-UCL.
GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
GO; GO:0030878; P:thyroid gland development; IEP:RGD.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
GO; GO:0042060; P:wound healing; IMP:RGD.
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.
PANTHER; PTHR11848:SF141; PTHR11848:SF141; 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.
2: Evidence at transcript level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Growth factor; Mitogen; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 330 Latency-associated peptide.
{ECO:0000250|UniProtKB:P61812}.
/FTId=PRO_0000033790.
CHAIN 331 442 Transforming growth factor beta-2.
{ECO:0000250|UniProtKB:P61812}.
/FTId=PRO_0000033791.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 337 346 {ECO:0000250|UniProtKB:P61812}.
DISULFID 345 408 {ECO:0000250|UniProtKB:P61812}.
DISULFID 374 439 {ECO:0000250|UniProtKB:P61812}.
DISULFID 378 441 {ECO:0000250|UniProtKB:P61812}.
DISULFID 407 407 Interchain.
{ECO:0000250|UniProtKB:P61812}.
VAR_SEQ 116 143 Missing (in isoform TGF-beta2A).
{ECO:0000303|PubMed:10899565,
ECO:0000303|PubMed:11014222,
ECO:0000303|Ref.3}.
/FTId=VSP_006418.
VAR_SEQ 144 144 D -> N (in isoform TGF-beta2A).
{ECO:0000303|PubMed:10899565,
ECO:0000303|PubMed:11014222,
ECO:0000303|Ref.3}.
/FTId=VSP_006419.
CONFLICT 99 99 Y -> C (in Ref. 2; CAB42003).
{ECO:0000305}.
CONFLICT 310 310 L -> P (in Ref. 3; AAD24484).
{ECO:0000305}.
CONFLICT 343 343 D -> H (in Ref. 2; CAB42003 and 4;
CAA50723). {ECO:0000305}.
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


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