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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
DOI=10.1093/nar/15.7.3187; PubMed=3470708 [NCBI, ExPASy, EBI, Israel, Japan]
Derynck R.,
Rhee L.;
"Sequence of the porcine transforming growth factor-beta precursor.";
Nucleic Acids Res. 15:3187-3187(1987).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-114.
STRAIN=Miniature swine;
PubMed=2461367 [NCBI, ExPASy, EBI, Israel, Japan]
Kondaiah P.,
van Obberghen-Schilling E.,
Ludwig R.L.,
Dhar R.,
Sporn M.B.,
Roberts A.B.;
"cDNA cloning of porcine transforming growth factor-beta 1 mRNAs. Evidence for alternate splicing and polyadenylation.";
J. Biol. Chem. 263:18313-18317(1988).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-114.
DOI=10.1093/nar/16.17.8730; PubMed=3166520 [NCBI, ExPASy, EBI, Israel, Japan]
Jakowlew S.B.,
Dillard P.J.,
Sporn M.B.,
Roberts A.B.;
"Nucleotide sequence of chicken transforming growth factor-beta 1 (TGF-beta 1).";
Nucleic Acids Res. 16:8730-8730(1988).
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[4]
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SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3166520 ORIGINATES FROM PIG.
Jakowlew S.B.;
Unpublished observations (MAR-1996).
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[5]
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NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-114.
Wimmers K.,
Chomdej S.,
Ponsuksili S.,
Schellander K.;
"Polymorphism in the porcine transforming growth factor beta 1 gene.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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[6]
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PROTEIN SEQUENCE OF 279-322.
DOI=10.1016/0092-8674(87)90192-9; PubMed=2879635 [NCBI, ExPASy, EBI, Israel, Japan]
Cheifetz S.,
Weatherbee J.A.,
Tsang M.L.S.,
Anderson J.K.,
Mole J.E.,
Lucas R.,
Massague J.;
"The transforming growth factor-beta system, a complex pattern of cross-reactive ligands and receptors.";
Cell 48:409-415(1987).
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- FUNCTION: Multifunctional protein that control proliferation, differentiation, and other functions in many cell types. Many cells synthesize TGFB1 and essentially all of them have specific receptors for this protein. It regulates the actions of many other growth factors and determines a positive or negative direction of their effects. It plays an important role in bone remodeling. It is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity).
- SUBUNIT: The inactive form consists of a TGFB1 homodimer non-covalently linked to a latency-associated peptide (LAP) homodimer. The inactive complex can contain a latent TGFB1-binding protein. The active form is a homodimer of mature TGFB1; disulfide-linked. Heterodimers of TGFB1/TGFB2 have been found in bone. Interacts with CD109 and DPT (By similarity).
- INTERACTION:
Q9Y6C2:EMILIN1 (xeno); NbExp=1; IntAct=EBI-907660, EBI-902920;
Q99K41:Emilin1 (xeno); NbExp=2; IntAct=EBI-907660, EBI-906561;
P37173:TGFBR2 (xeno); NbExp=1; IntAct=EBI-907660, EBI-296151;
- SUBCELLULAR LOCATION: Secreted.
- PTM: Glycosylated (By similarity).
- PTM: The precursor is cleaved into mature TGF-beta-1 and LAP, which remains non-covalently linked to mature TGF-beta-1 rendering it inactive (By similarity).
- SIMILARITY: Belongs to the TGF-beta family.
- CAUTION: PubMed:3166520 sequence which was said to originate from chicken, seems (Ref.4) to originate from pig.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 390 AA [This is the length of the unprocessed precursor] |
Molecular weight: 44294 Da [This is the MW of the unprocessed precursor] |
CRC64: A6E2C3659FC384E6 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MPPSGLRLLP LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
70 80 90 100 110 120
SPPSQGDVPP GPLPEAVLAL YNSTRDRVAG ESVEPEPEPE ADYYAKEVTR VLMLESGNQI
130 140 150 160 170 180
YDKFKGTPHS LYMLFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNDSWR
190 200 210 220 230 240
YLSNRLLAPS DSPEWLSFDV TGVVRQWLTR REAIEGFRLS AHCSCDSKDN TLHVEINGFN
250 260 270 280 290 300
SGRRGDLATI HGMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
310 320 330 340 350 360
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA
370 380 390
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS
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P07200 in FASTA format |
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