NiceProt View of SWISS-PROT: P01137

[General] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

General information about the entry
Entry name	TGF1_HUMAN
Primary accession number	P01137
Secondary accession number(s)	None
Entered in SWISS-PROT in	Release 01, July 1986
Sequence was last modified in	Release 17, February 1991
Annotations were last modified in	Release 38, July 1999
Name and orig in of the protein
Protein name	TRANSFORMING GROWTH FACTOR BETA 1 [Precursor]
Synonym(s)	TGF-BETA 1
Gene name(s)	TGFB1 OR TGFB
From	Homo sapiens (Human)
Taxonomy	Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
References
[1] SEQUENCE FROM N.A. MEDLINE; 87174845. [NCBI, ExPASy, Israel, Japan] Derynck R., Rhee L., Chen E.Y., van Tilburg A.; "Intron-exon structure of the human transforming growth factor-beta precursor gene."; Nucleic Acids Res. 15:3188-3189(1987).
[2] SEQUENCE FROM N.A. MEDLINE; 85296301. [NCBI, ExPASy, Israel, Japan] Derynck R., Jarrett J.A., Chen E.Y., Eaton D.H., Bell J.R., Assoian R.K., Roberts A.B., Sporn M.B., Goeddel D.V.; "Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells."; Nature 316:701-705(1985).
[3] SEQUENCE OF 279-301. MEDLINE; 85131019. [NCBI, ExPASy, Israel, Japan] Massague J., Like B.; "Cellular receptors for type beta transforming growth factor. Ligand binding and affinity labeling in human and rodent cell lines."; J. Biol. Chem. 260:2636-2645(1985).
[4] STRUCTURE BY NMR OF 279-390. MEDLINE; 93144319. [NCBI, ExPASy, Israel, Japan] Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A., Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J., Torchia D.A.; "Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells."; Biochemistry 32:1152-1163(1993).
[5] STRUCTURE BY NMR OF 279-390. MEDLINE; 93144320. [NCBI, ExPASy, Israel, Japan] Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A., Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J., Torchia D.A.; "Transforming growth factor beta 1: secondary structure as determined by heteronuclear magnetic resonance spectroscopy."; Biochemistry 32:1164-1171(1993).
[6] STRUCTURE BY NMR OF 279-390. MEDLINE; 96266150. [NCBI, ExPASy, Israel, Japan] Hinck A.P., Archer S.J., Qian S.W., Roberts A.B., Sporn M.B., Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J., Torchia D.A.; "Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2."; Biochemistry 35:8517-8534(1996).
Comments
FUNCTION: TGF-BETA IS A MULTIFUNCTIONAL PEPTIDE THAT CONTROL PROLIFERATION, DIFFERENTIATION, AND OTHER FUNCTIONS IN MANY CELL TYPES. MANY CELLS SYNTHESIZE TGF-BETA AND ESSENTIALLY ALL OF THEM HAVE SPECIFIC RECEPTORS FOR THIS PEPTIDE. TGF-BETA REGULATES THE ACTIONS OF MANY OTHER PEPTIDE GROWTH FACTORS AND DETERMINES A POSITIVE OR NEGATIVE DIRECTION OF THEIR EFFECTS. SUBUNIT: HOMODIMER, DISULFIDE-LINKED. SIMILARITY: BELONGS TO THE TGF-BETA FAMILY.
Copyright
This SWISS-PROT entry is copyright. It is produced through a collaboration between the Swiss Institute of Bioinformatics and the EMBL outstation - the European Bioinformatics Institute. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://www.isb-sib.ch/announce/ or send an email to license@isb-sib.ch).
Cross-references
EMBL X05839; CAA29283.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence] X05840; CAA29283.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence] X05843; CAA29283.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence] X05844; CAA29283.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence] X05849; CAA29283.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence] X05850; CAA29283.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence] X02812; CAA26580.1; ALT_SEQ. [EMBL / GenBank / DDBJ] [CoDingSequence] PIR A01395; WFHU2. A22290; A22290. A27513; A27513. PDB 1KLA; 17-AUG-96. [ExPASy / RCSB] 1KLC; 17-AUG-96. [ExPASy / RCSB] 1KLD; 17-AUG-96. [ExPASy / RCSB] SWISS-3DIMAGE TGF1_HUMAN. MIM 190180; -. GeneCards TGFB1. PRINTS PR00438; GFCYSKNOT. PROSITE PS00250; TGF_BETA; 1. PFAM PF00019; TGF-beta; 1. PF00688; TGFb_propeptide; 1. PRODOM [Domain structure / List of seq. sharing at least 1 domain] BLOCKS P01137. DOMO P01137. PROTOMAP P01137. PRESAGE P01137. SWISS-2DPAGE GET REGION ON 2D PAGE.
Keywords
Growth factor; Mitogen; Glycoprotein; Signal; 3D-structure.
Features
SIGNAL 1 23 POTENTIAL. PROPEP 24 278 CHAIN 279 390 TRANSFORMING GROWTH FACTOR BETA 1. DISULFID 285 294 DISULFID 293 356 DISULFID 322 387 BY SIMILARITY. DISULFID 326 389 BY SIMILARITY. DISULFID 355 355 INTERCHAIN. CARBOHYD 82 82 POTENTIAL. CARBOHYD 136 136 POTENTIAL. CARBOHYD 176 176 POTENTIAL. SITE 244 246 CELL ATTACHMENT SITE (POTENTIAL). CONFLICT 10 10 L -> P (IN REF. 2). CONFLICT 159 159 R -> RR (IN REF. 2). FT table viewer
Sequence information
Length: 390 AA [This is the length of the unprocessed precursor] Molecular weight: 44341 Da [This is the Mw of the unprocessed precursor] CRC64: 75391614250288FE [This is a checksum on the sequence]
10 20 30 40 50 60 | | | | | | MPPSGLRLLL LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA 70 80 90 100 110 120 | | | | | | SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE ADYYAKEVTR VLMVETHNEI 130 140 150 160 170 180 | | | | | | YDKFKQSTHS IYMFFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNNSWR 190 200 210 220 230 240 | | | | | | YLSNRLLAPS DSPEWLSFDV TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT 250 260 270 280 290 300 | | | | | | TGRRGDLATI HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI 310 320 330 340 350 360 | | | | | | DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA 370 380 390 | | | LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS P01137 in FASTA format