Reviewed, UniProtKB/Swiss-Prot P07200 (TGFB1_PIG)

Names and origin

Protein names

Recommended name:
    Transforming growth factor beta-1
      Short name=TGF-beta-1
Cleaved into the following chain:
    1- Recommended name:
            Latency-associated peptide
                Short name=LAP

Gene names

Name:

TGFB1

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts By similarity.
Subunit structure	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.
Subcellular location	Secreted.
Post-translational modification	Glycosylated By similarity. 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.
Sequence similarities	Belongs to the TGF-beta family.
Caution	Ref.3 sequence which was said to originate from chicken, seems (Ref.4) to originate from pig.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell death Inferred from sequence or structural similarity. Source: UniProtKB cell growth Inferred from electronic annotation. Source: InterPro cell proliferation Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB lymph node development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB organ morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of DNA binding Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein import into nucleus Inferred from sequence or structural similarity. Source: UniProtKB regulation of striated muscle development Inferred from sequence or structural similarity. Source: UniProtKB skeletal system development Inferred from sequence or structural similarity. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW transcription activator activity Inferred from sequence or structural similarity. Source: UniProtKB transforming growth factor beta receptor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EMILIN1	Q9Y6C2	1	EBI-907660,EBI-902920	From a different organism.
Emilin1	Q99K41	2	EBI-907660,EBI-906561	From a different organism.
TGFBR2	P37173	1	EBI-907660,EBI-296151	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	By similarity
	Chain	30 – 278	249	Latency-associated peptide		PRO_0000033768
	Chain	279 – 390	112	Transforming growth factor beta-1		PRO_0000033769
Regions
	Motif	244 – 246	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	82	1	N-linked (GlcNAc...) By similarity
	Glycosylation	136	1	N-linked (GlcNAc...) By similarity
	Glycosylation	176	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	285 ↔ 294		By similarity
	Disulfide bond	293 ↔ 356		By similarity
	Disulfide bond	322 ↔ 387		By similarity
	Disulfide bond	326 ↔ 389		By similarity
	Disulfide bond	355		Interchain By similarity
Natural variations
	Natural variant	114	1	L → V Ref.2 Ref.3 Ref.5
Experimental info
	Sequence conflict	6 – 7	2	LR → PG in CAA30933. Ref.3
	Sequence conflict	180	1	R → G in CAA30933. Ref.3
	Sequence conflict	237	1	N → NA in CAA30933. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P07200-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: A6E2C3659FC384E6	FASTA	390	44,294
	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

References

[1]	"Sequence of the porcine transforming growth factor-beta precursor." Derynck R., Rhee L. Nucleic Acids Res. 15:3187-3187(1987) [PubMed: 3470708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[2]	"cDNA cloning of porcine transforming growth factor-beta 1 mRNAs. Evidence for alternate splicing and polyadenylation." Kondaiah P., van Obberghen-Schilling E., Ludwig R.L., Dhar R., Sporn M.B., Roberts A.B. J. Biol. Chem. 263:18313-18317(1988) [PubMed: 2461367] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-114. Strain: Miniature swine.
[3]	"Nucleotide sequence of chicken transforming growth factor-beta 1 (TGF-beta 1)." Jakowlew S.B., Dillard P.J., Sporn M.B., Roberts A.B. Nucleic Acids Res. 16:8730-8730(1988) [PubMed: 3166520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-114.
[4]	Jakowlew S.B. Unpublished observations (MAR-1996) Cited for: SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3166520 ORIGINATES FROM PIG.
[5]	"Polymorphism in the porcine transforming growth factor beta 1 gene." Wimmers K., Chomdej S., Ponsuksili S., Schellander K. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-114.
[6]	"The transforming growth factor-beta system, a complex pattern of cross-reactive ligands and receptors." Cheifetz S., Weatherbee J.A., Tsang M.L.S., Anderson J.K., Mole J.E., Lucas R., Massague J. Cell 48:409-415(1987) [PubMed: 2879635] [Abstract] Cited for: PROTEIN SEQUENCE OF 279-322.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y00111 mRNA. Translation: CAA68291.1. M23703 mRNA. Translation: AAA64616.1. X12373 mRNA. Translation: CAA30933.1. AF461808 mRNA. Translation: AAL57902.1.
PIR	A27512. S01413.
RefSeq	NP_999180.1.
UniGene	Ssc.76
3D structure databases
HSSP	HSSP built from PDB template 1KLA based on UniProtKB P01137.
SMR	P07200. Positions 279-390.
ModBase	Search...
Protein-protein interaction databases
IntAct	P07200. 3 interactions.
Genome annotation databases
GeneID	397078.
KEGG	ssc:397078.
Phylogenomic databases
HOVERGEN	P07200.
Family and domain databases
InterPro	IPR016319. TGF-beta. IPR003911. TGF_TGFb. IPR001839. TGFb. IPR003939. TGFb1. IPR017948. TGFb_CS. IPR001111. TGFb_N. IPR015615. TGFbeta. [Graphical view]
PANTHER	PTHR11848. TGFbeta. 1 hit.
Pfam	PF00019. TGF_beta. 1 hit. PF00688. TGFb_propeptide. 1 hit. [Graphical view]
PIRSF	PIRSF001787. TGF-beta. 1 hit.
PRINTS	PR01423. TGFBETA. PR01424. TGFBETA1.
ProDom	PD000357. TGFb. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00204. TGFB. 1 hit. [Graphical view]
PROSITE	PS00250. TGF_BETA_1. 1 hit. PS51362. TGF_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TGFB1_PIG

Accession

Primary (citable) accession number: P07200
Secondary accession number(s): P08832

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)