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Transforming growth factor beta-2 (TGF-beta-2) (BSC-1 cell growth inhibitor) (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) (Polyergin) [Cleaved into: Latency-associated peptide (LAP)]

 TGFB2_HUMAN             Reviewed;         414 AA.
P61812; B4DKC5; P08112; Q15579; Q15581; Q4VAV9;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
27-SEP-2017, entry version 158.
RecName: Full=Transforming growth factor beta-2;
Short=TGF-beta-2;
AltName: Full=BSC-1 cell growth inhibitor;
AltName: Full=Cetermin;
AltName: Full=Glioblastoma-derived T-cell suppressor factor;
Short=G-TSF;
AltName: Full=Polyergin;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Flags: Precursor;
Name=TGFB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=3322813;
de Martin R., Haendler B., Hofer-Warbinek R., Gaugitsch H., Wrann M.,
Schluesener H., Seifert J.M., Bodmer S., Fontana A., Hofer E.;
"Complementary DNA for human glioblastoma-derived T cell suppressor
factor, a novel member of the transforming growth factor-beta gene
family.";
EMBO J. 6:3673-3677(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
PubMed=3162414; DOI=10.1089/dna.1988.7.1;
Madisen L., Webb N.R., Rose T.M., Marquardt H., Ikeda T.,
Twardzik D.R., Seyedin S., Purchio A.F.;
"Transforming growth factor-beta 2: cDNA cloning and sequence
analysis.";
DNA 7:1-8(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
PubMed=2850146; DOI=10.1089/dna.1.1988.7.493;
Webb N.R., Madisen L., Rose T.M., Purchio A.F.;
"Structural and sequence analysis of TGF-beta 2 cDNA clones predicts
two different precursor proteins produced by alternative mRNA
splicing.";
DNA 7:493-497(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-91 AND LEU-207.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
TISSUE=Lung;
PubMed=1764261; DOI=10.3109/08977199109043910;
Noma T., Glick A.B., Geiser A.G., O'Reilly M.A., Miller J.,
Roberts A.B., Sporn M.B.;
"Molecular cloning and structure of the human transforming growth
factor-beta 2 gene promoter.";
Growth Factors 4:247-255(1991).
[9]
PROTEIN SEQUENCE OF 303-414.
PubMed=3476488;
Marquardt H., Lioubin M.N., Ikeda T.;
"Complete amino acid sequence of human transforming growth factor type
beta 2.";
J. Biol. Chem. 262:12127-12131(1987).
[10]
CHROMOSOMAL TRANSLOCATION WITH HDAC9.
PubMed=12706107; DOI=10.1016/S0888-7543(03)00046-6;
David D., Cardoso J., Marques B., Marques R., Silva E.D., Santos H.,
Boavida M.G.;
"Molecular characterization of a familial translocation implicates
disruption of HDAC9 and possible position effect on TGFbeta2 in the
pathogenesis of Peters' anomaly.";
Genomics 81:489-503(2003).
[11]
INTERACTION WITH ASPN.
PubMed=17827158; DOI=10.1074/jbc.M700522200;
Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.;
"Mechanisms for asporin function and regulation in articular
cartilage.";
J. Biol. Chem. 282:32185-32192(2007).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=1631557; DOI=10.1126/science.1631557;
Daopin S., Piez K.A., Ogawa Y., Davies D.R.;
"Crystal structure of transforming growth factor-beta 2: an unusual
fold for the superfamily.";
Science 257:369-373(1992).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=1641027; DOI=10.1038/358430a0;
Schlunegger M.P., Gruetter M.G.;
"An unusual feature revealed by the crystal structure at 2.2-A
resolution of human transforming growth factor-beta 2.";
Nature 358:430-434(1992).
[14]
VARIANT HIS-91.
PubMed=11528528; DOI=10.1038/sj.gene.6363780;
Alansari A., Hajeer A.H., Bayat A., Eyre S., Carthy D., Ollier W.E.;
"Two novel polymorphisms in the human transforming growth factor beta
2 gene.";
Genes Immun. 2:295-296(2001).
[15]
VARIANTS LDS4 100-ALA--TYR-104 DEL; TRP-299; CYS-302 AND HIS-338.
PubMed=22772368; DOI=10.1038/ng.2349;
Lindsay M.E., Schepers D., Bolar N.A., Doyle J.J., Gallo E.,
Fert-Bober J., Kempers M.J., Fishman E.K., Chen Y., Myers L.,
Bjeda D., Oswald G., Elias A.F., Levy H.P., Anderlid B.M., Yang M.H.,
Bongers E.M., Timmermans J., Braverman A.C., Canham N., Mortier G.R.,
Brunner H.G., Byers P.H., Van Eyk J., Van Laer L., Dietz H.C.,
Loeys B.L.;
"Loss-of-function mutations in TGFB2 cause a syndromic presentation of
thoracic aortic aneurysm.";
Nat. Genet. 44:922-927(2012).
[16]
INVOLVEMENT IN NON-SYNDROMIC AORTIC DISEASE, AND VARIANT CYS-320.
PubMed=25046559; DOI=10.1016/j.cca.2014.07.016;
Gago-Diaz M., Blanco-Verea A., Teixido-Tura G., Valenzuela I.,
Del Campo M., Borregan M., Sobrino B., Amigo J., Garcia-Dorado D.,
Evangelista A., Carracedo A., Brion M.;
"Whole exome sequencing for the identification of a new mutation in
TGFB2 involved in a familial case of non-syndromic aortic disease.";
Clin. Chim. Acta 437:88-92(2014).
-!- FUNCTION: TGF-beta 2 has suppressive effects on interleukin-2
dependent T-cell growth.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimers
with TGFB1 and with TGFB3 have been found in bone (By similarity).
Interacts with the serine proteases, HTRA1 and HTRA3 (By
similarity). Latency-associated peptide interacts with NREP; the
interaction results in a decrease in TGFB2 autoinduction (By
similarity). Interacts with ASPN. Interacts with MFAP5 (By
similarity). {ECO:0000250|UniProtKB:Q9QZJ6,
ECO:0000269|PubMed:17827158}.
-!- INTERACTION:
P05067:APP; NbExp=7; IntAct=EBI-779581, EBI-77613;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=P61812-1, P08112-1;
Sequence=Displayed;
Name=B;
IsoId=P61812-2, P08112-2;
Sequence=VSP_006417;
-!- PTM: The precursor is cleaved into mature TGF-beta-2 and LAP,
which remains non-covalently linked to mature TGF-beta-2 rendering
it inactive. {ECO:0000250}.
-!- DISEASE: Note=A chromosomal aberration involving TGFB2 is found in
a family with Peters anomaly. Translocation t(1;7)(q41;p21) with
HDAC9. {ECO:0000269|PubMed:12706107}.
-!- DISEASE: Loeys-Dietz syndrome 4 (LDS4) [MIM:614816]: An aortic
aneurysm syndrome with widespread systemic involvement. LDS4 is
characterized by arterial tortuosity, aortic dissection,
intracranial aneurysm and subarachnoid hemorrhage, hypertelorism,
bifid uvula, pectus deformity, bicuspid aortic valve,
arachnodactyly, scoliosis, foot deformities, dural ectasia, joint
hyperflexibility, and thin skin with easy bruising and striae.
{ECO:0000269|PubMed:22772368}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Defects in TGFB2 may be a cause of non-syndromic
aortic disease (NSAD). NSAD is a frequently asymptomatic but
potentially lethal disease characterized by thoracic aortic
aneurysms and dissections without additional syndromic features.
{ECO:0000269|PubMed:25046559}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tgfb2/";
-!- WEB RESOURCE: Name=Wikipedia; Note=TGF beta-2 entry;
URL="https://en.wikipedia.org/wiki/TGF_beta_2";
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EMBL; Y00083; CAA68279.1; -; mRNA.
EMBL; M19154; AAA50404.1; -; mRNA.
EMBL; M19154; AAA50405.1; -; mRNA.
EMBL; AY438979; AAR05442.1; -; Genomic_DNA.
EMBL; AK296504; BAG59137.1; -; mRNA.
EMBL; CH471100; EAW93326.1; -; Genomic_DNA.
EMBL; BC096235; AAH96235.1; -; mRNA.
EMBL; BC099635; AAH99635.1; -; mRNA.
EMBL; M87843; AAA61162.1; -; Genomic_DNA.
CCDS; CCDS1521.1; -.
CCDS; CCDS44318.1; -. [P61812-2]
PIR; A29478; B31249.
PIR; S06216; A31249.
RefSeq; NP_001129071.1; NM_001135599.3. [P61812-2]
RefSeq; NP_003229.1; NM_003238.4. [P61812-1]
UniGene; Hs.133379; -.
PDB; 1TFG; X-ray; 1.95 A; A=303-414.
PDB; 2TGI; X-ray; 1.80 A; A=303-414.
PDB; 4KXZ; X-ray; 2.83 A; A/B/D/E=303-414.
PDB; 5TX4; X-ray; 1.88 A; B=303-414.
PDB; 5TY4; EM; 2.90 A; B=317-413.
PDBsum; 1TFG; -.
PDBsum; 2TGI; -.
PDBsum; 4KXZ; -.
PDBsum; 5TX4; -.
PDBsum; 5TY4; -.
ProteinModelPortal; P61812; -.
SMR; P61812; -.
BioGrid; 112900; 8.
DIP; DIP-5936N; -.
IntAct; P61812; 2.
ChEMBL; CHEMBL3217393; -.
iPTMnet; P61812; -.
PhosphoSitePlus; P61812; -.
BioMuta; TGFB2; -.
DMDM; 48429157; -.
EPD; P61812; -.
MaxQB; P61812; -.
PeptideAtlas; P61812; -.
PRIDE; P61812; -.
Ensembl; ENST00000366929; ENSP00000355896; ENSG00000092969. [P61812-2]
Ensembl; ENST00000366930; ENSP00000355897; ENSG00000092969. [P61812-1]
GeneID; 7042; -.
KEGG; hsa:7042; -.
UCSC; uc001hlm.4; human.
CTD; 7042; -.
DisGeNET; 7042; -.
EuPathDB; HostDB:ENSG00000092969.11; -.
GeneCards; TGFB2; -.
GeneReviews; TGFB2; -.
HGNC; HGNC:11768; TGFB2.
MalaCards; TGFB2; -.
MIM; 190220; gene.
MIM; 614816; phenotype.
neXtProt; NX_P61812; -.
OpenTargets; ENSG00000092969; -.
Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
Orphanet; 708; Peters anomaly.
PharmGKB; PA36482; -.
GeneTree; ENSGT00760000119112; -.
HOGENOM; HOG000290198; -.
HOVERGEN; HBG074115; -.
InParanoid; P61812; -.
KO; K13376; -.
OMA; NERAATC; -.
OrthoDB; EOG091G0BMM; -.
PhylomeDB; P61812; -.
TreeFam; TF318514; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-3000178; ECM proteoglycans.
SignaLink; P61812; -.
SIGNOR; P61812; -.
ChiTaRS; TGFB2; human.
EvolutionaryTrace; P61812; -.
GeneWiki; TGF_beta_2; -.
GenomeRNAi; 7042; -.
PMAP-CutDB; P61812; -.
PRO; PR:P61812; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000092969; -.
CleanEx; HS_TGFB2; -.
Genevisible; P61812; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB.
GO; GO:0005125; F:cytokine activity; TAS:UniProtKB.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; TAS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IMP:UniProtKB.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IDA:UniProtKB.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; IMP:AgBase.
GO; GO:0032147; P:activation of protein kinase activity; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; TAS:UniProtKB.
GO; GO:0035910; P:ascending aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0060413; P:atrial septum morphogenesis; ISS:BHF-UCL.
GO; GO:0003289; P:atrial septum primum morphogenesis; ISS:BHF-UCL.
GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0060038; P:cardiac muscle cell proliferation; IDA:UniProtKB.
GO; GO:0003215; P:cardiac right ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0010002; P:cardioblast differentiation; IDA:UniProtKB.
GO; GO:0042637; P:catagen; IDA:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0008219; P:cell death; IDA:UniProtKB.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0016049; P:cell growth; IEA:InterPro.
GO; GO:0016477; P:cell migration; IDA:BHF-UCL.
GO; GO:0000902; P:cell morphogenesis; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0045216; P:cell-cell junction organization; IDA:BHF-UCL.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0030199; P:collagen fibril organization; IDA:BHF-UCL.
GO; GO:1904888; P:cranial skeletal system development; ISS:BHF-UCL.
GO; GO:0042416; P:dopamine biosynthetic process; ISS:UniProtKB.
GO; GO:0009790; P:embryo development; TAS:UniProtKB.
GO; GO:0048566; P:embryonic digestive tract development; IEP:DFLAT.
GO; GO:0030326; P:embryonic limb morphogenesis; ISS:BHF-UCL.
GO; GO:0003274; P:endocardial cushion fusion; ISS:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0001654; P:eye development; IDA:UniProtKB.
GO; GO:0048699; P:generation of neurons; TAS:UniProtKB.
GO; GO:0008347; P:glial cell migration; IDA:BHF-UCL.
GO; GO:0001942; P:hair follicle development; IDA:UniProtKB.
GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IDA:UniProtKB.
GO; GO:0003007; P:heart morphogenesis; IDA:BHF-UCL.
GO; GO:0003179; P:heart valve morphogenesis; ISS:BHF-UCL.
GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; ISS:BHF-UCL.
GO; GO:0001822; P:kidney development; ISS:BHF-UCL.
GO; GO:0008584; P:male gonad development; ISS:BHF-UCL.
GO; GO:0003149; P:membranous septum morphogenesis; ISS:BHF-UCL.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IDA:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:BHF-UCL.
GO; GO:1905006; P:negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0050777; P:negative regulation of immune response; TAS:UniProtKB.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; IDA:DFLAT.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:BHF-UCL.
GO; GO:0003407; P:neural retina development; ISS:BHF-UCL.
GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0042476; P:odontogenesis; NAS:BHF-UCL.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
GO; GO:0060021; P:palate development; ISS:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISS:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0051891; P:positive regulation of cardioblast differentiation; IDA:UniProtKB.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:BHF-UCL.
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; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0045823; P:positive regulation of heart contraction; IDA:UniProtKB.
GO; GO:0050778; P:positive regulation of immune response; ISS:UniProtKB.
GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IDA:BHF-UCL.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:UniProtKB.
GO; GO:0045778; P:positive regulation of ossification; IEP:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:BHF-UCL.
GO; GO:0051795; P:positive regulation of timing of catagen; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0003184; P:pulmonary valve morphogenesis; ISS:BHF-UCL.
GO; GO:1902256; P:regulation of apoptotic process involved in outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; IMP:BHF-UCL.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IMP:BHF-UCL.
GO; GO:0032570; P:response to progesterone; IDA:BHF-UCL.
GO; GO:0009611; P:response to wounding; IEP:BHF-UCL.
GO; GO:0007435; P:salivary gland morphogenesis; IEP:BHF-UCL.
GO; GO:0001501; P:skeletal system development; ISS:BHF-UCL.
GO; GO:0007184; P:SMAD protein import into nucleus; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
GO; GO:1903701; P:substantia propria of cornea development; ISS:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0042704; P:uterine wall breakdown; TAS:BHF-UCL.
GO; GO:0060065; P:uterus development; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
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.
PANTHER; PTHR11848:SF208; PTHR11848:SF208; 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;
3D-structure; Alternative splicing; Aortic aneurysm;
Chromosomal rearrangement; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Growth factor; Mitogen; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 302 Latency-associated peptide.
/FTId=PRO_0000033784.
CHAIN 303 414 Transforming growth factor beta-2.
/FTId=PRO_0000033785.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 309 318
DISULFID 317 380
DISULFID 346 411
DISULFID 350 413
DISULFID 379 379 Interchain.
VAR_SEQ 116 116 N -> TVCPVVTTPSGSVGSLCSRQSQVLCGYLD (in
isoform B). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:2850146,
ECO:0000303|PubMed:3162414}.
/FTId=VSP_006417.
VARIANT 91 91 R -> H (in dbSNP:rs10482721).
{ECO:0000269|PubMed:11528528,
ECO:0000269|Ref.4}.
/FTId=VAR_012708.
VARIANT 100 104 Missing (in LDS4).
{ECO:0000269|PubMed:22772368}.
/FTId=VAR_068931.
VARIANT 207 207 V -> L (in dbSNP:rs10482810).
{ECO:0000269|Ref.4}.
/FTId=VAR_018923.
VARIANT 299 299 R -> W (in LDS4; dbSNP:rs863223792).
{ECO:0000269|PubMed:22772368}.
/FTId=VAR_068932.
VARIANT 302 302 R -> C (in LDS4; dbSNP:rs869312903).
{ECO:0000269|PubMed:22772368}.
/FTId=VAR_068933.
VARIANT 320 320 R -> C (probable disease-associated
mutation found in a family with non-
syndromic aortic disease).
{ECO:0000269|PubMed:25046559}.
/FTId=VAR_072740.
VARIANT 338 338 P -> H (in LDS4; dbSNP:rs387907278).
{ECO:0000269|PubMed:22772368}.
/FTId=VAR_068934.
CONFLICT 32 32 F -> L (in Ref. 8; AAA61162).
{ECO:0000305}.
CONFLICT 116 116 Missing (in Ref. 3; AAA50405).
{ECO:0000305}.
HELIX 306 309 {ECO:0000244|PDB:2TGI}.
STRAND 315 320 {ECO:0000244|PDB:2TGI}.
STRAND 323 325 {ECO:0000244|PDB:2TGI}.
HELIX 326 330 {ECO:0000244|PDB:2TGI}.
STRAND 335 337 {ECO:0000244|PDB:2TGI}.
STRAND 339 342 {ECO:0000244|PDB:2TGI}.
STRAND 345 347 {ECO:0000244|PDB:2TGI}.
STRAND 354 356 {ECO:0000244|PDB:2TGI}.
HELIX 359 370 {ECO:0000244|PDB:2TGI}.
HELIX 372 374 {ECO:0000244|PDB:2TGI}.
STRAND 379 382 {ECO:0000244|PDB:2TGI}.
STRAND 384 394 {ECO:0000244|PDB:2TGI}.
STRAND 397 408 {ECO:0000244|PDB:2TGI}.
STRAND 411 414 {ECO:0000244|PDB:2TGI}.
SEQUENCE 414 AA; 47748 MW; 7D9D569E0F4A07D0 CRC64;
MHYCVLSAFL ILHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP
EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPP FFPSENAIPP
TFYRPYFRIV RFDVSAMEKN ASNLVKAEFR VFRLQNPKAR VPEQRIELYQ ILKSKDLTSP
TQRYIDSKVV KTRAEGEWLS FDVTDAVHEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP
NKSEELEARF AGIDGTSTYT SGDQKTIKST RKKNSGKTPH LLLMLLPSYR LESQQTNRRK
KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH
SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI EQLSNMIVKS CKCS


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