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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.
05-DEC-2018, entry version 169.
RecName: Full=Transforming growth factor beta-2 proprotein;
AltName: Full=Cetermin;
AltName: Full=Glioblastoma-derived T-cell suppressor factor {ECO:0000303|PubMed:3322813};
Short=G-TSF {ECO:0000303|PubMed:3322813};
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-2;
Short=TGF-beta-2;
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]
INTERACTION WITH LRRC32.
PubMed=19651619; DOI=10.1073/pnas.0901944106;
Tran D.Q., Andersson J., Wang R., Ramsey H., Unutmaz D., Shevach E.M.;
"GARP (LRRC32) is essential for the surface expression of latent TGF-
beta on platelets and activated FOXP3+ regulatory T cells.";
Proc. Natl. Acad. Sci. U.S.A. 106:13445-13450(2009).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 303-414, DISULFIDE BOND, AND
SUBUNIT.
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).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)OF 303-414, DISULFIDE BOND, AND
SUBUNIT.
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).
[15]
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).
[16]
INVOLVEMENT IN LDS4, VARIANTS LDS4 102-GLU--SER-414 DEL AND
229-CYS--SER-414 DEL, AND FUNCTION.
PubMed=22772371; DOI=10.1038/ng.2348;
National Heart, Lung, and Blood Institute (NHLBI) Go Exome Sequencing Project;
Boileau C., Guo D.C., Hanna N., Regalado E.S., Detaint D., Gong L.,
Varret M., Prakash S.K., Li A.H., d'Indy H., Braverman A.C.,
Grandchamp B., Kwartler C.S., Gouya L., Santos-Cortez R.L.,
Abifadel M., Leal S.M., Muti C., Shendure J., Gross M.S., Rieder M.J.,
Vahanian A., Nickerson D.A., Michel J.B., Jondeau G., Milewicz D.M.;
"TGFB2 mutations cause familial thoracic aortic aneurysms and
dissections associated with mild systemic features of Marfan
syndrome.";
Nat. Genet. 44:916-921(2012).
[17]
VARIANTS LDS4 100-ALA--TYR-104 DEL; TRP-299; CYS-302 AND HIS-338, AND
FUNCTION.
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).
[18]
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: 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 (By similarity).
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 (By
similarity). {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 (PubMed:22772371, PubMed:22772368). 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:0000269|PubMed:22772368,
ECO:0000269|PubMed:22772371}.
-!- SUBUNIT: Interacts with the serine proteases, HTRA1 and HTRA3 (By
similarity). Interacts with ASPN (PubMed:17827158). 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
(PubMed:19651619). 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 (PubMed:1631557, PubMed:1641027). 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:0000269|PubMed:1631557, ECO:0000269|PubMed:1641027,
ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:19651619}.
-!- INTERACTION:
P05067:APP; NbExp=7; IntAct=EBI-779581, EBI-77613;
-!- 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=A;
IsoId=P61812-1, P08112-1;
Sequence=Displayed;
Name=B;
IsoId=P61812-2, P08112-2;
Sequence=VSP_006417;
-!- 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}.
-!- 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, ECO:0000269|PubMed:22772371}.
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}.
-!- CAUTION: In contrast to other members of the family, does not
contain a R-G-D cell attachment site motif that mediates binding
to integrins and promotes release of Latency-associated peptide
(LAP) chain from TGF-beta-2. {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.
ComplexPortal; CPX-605; TGF-beta-2 complex.
ComplexPortal; CPX-834; TGF-beta-2-TGFR complex.
DIP; DIP-5936N; -.
IntAct; P61812; 2.
ChEMBL; CHEMBL3217393; -.
GlyConnect; 1836; -.
iPTMnet; P61812; -.
PhosphoSitePlus; P61812; -.
BioMuta; TGFB2; -.
DMDM; 48429157; -.
EPD; P61812; -.
MaxQB; P61812; -.
PeptideAtlas; P61812; -.
PRIDE; P61812; -.
ProteomicsDB; 57335; -.
ProteomicsDB; 57336; -. [P61812-2]
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.
PharmGKB; PA36482; -.
GeneTree; ENSGT00940000157390; -.
HOGENOM; HOG000290198; -.
HOVERGEN; HBG074115; -.
InParanoid; P61812; -.
KO; K13376; -.
OMA; WSADTQH; -.
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; Expressed in 158 organ(s), highest expression level in lung.
CleanEx; HS_TGFB2; -.
Genevisible; P61812; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0062023; C:collagen-containing 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; IBA:GO_Central.
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:signaling receptor binding; IMP:UniProtKB.
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: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: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: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:0009792; P:embryo development ending in birth or egg hatching; 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:0016525; P:negative regulation of angiogenesis; 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:0010629; P:negative regulation of gene expression; IDA: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: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:0045747; P:positive regulation of Notch signaling pathway; IDA:BHF-UCL.
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:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; 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:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:1902256; P:regulation of apoptotic process involved in outflow tract morphogenesis; ISS:BHF-UCL.
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; IDA:UniProtKB.
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:0062009; P:secondary palate development; ISS:BHF-UCL.
GO; GO:0001501; P:skeletal system development; ISS:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:BHF-UCL.
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: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.
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; Extracellular matrix; Glycoprotein; Growth factor;
Mitogen; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 302 Latency-associated peptide.
{ECO:0000305|PubMed:3476488}.
/FTId=PRO_0000033784.
CHAIN 303 414 Transforming growth factor beta-2.
{ECO:0000305|PubMed:3476488}.
/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 {ECO:0000269|PubMed:1631557,
ECO:0000269|PubMed:1641027}.
DISULFID 317 380 {ECO:0000269|PubMed:1631557,
ECO:0000269|PubMed:1641027}.
DISULFID 346 411 {ECO:0000269|PubMed:1631557,
ECO:0000269|PubMed:1641027}.
DISULFID 350 413 {ECO:0000269|PubMed:1631557,
ECO:0000269|PubMed:1641027}.
DISULFID 379 379 Interchain. {ECO:0000269|PubMed:1631557,
ECO:0000269|PubMed:1641027}.
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 102 414 Missing (in LDS4).
{ECO:0000269|PubMed:22772371}.
/FTId=VAR_080342.
VARIANT 207 207 V -> L (in dbSNP:rs10482810).
{ECO:0000269|Ref.4}.
/FTId=VAR_018923.
VARIANT 229 414 Missing (in LDS4).
{ECO:0000269|PubMed:22772371}.
/FTId=VAR_080343.
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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