P27090 (TGFB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transforming growth factor beta-2
Short name=TGF-beta-2

Cleaved into the following chain:

1. Latency-associated peptide
   Short name=LAP

Gene names

Name:

Tgfb2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	414 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	TGF-beta 2 has suppressive effects on interleukin-2 dependent T-cell growth.
Subunit structure	Homodimer; disulfide-linked By similarity. Heterodimers with TGFB1 and with TGFB3 have been found in bone By similarity. Interacts with ASPN By similarity. Interacts with the serine proteases HTRA1 and HTRA3. Latency-associated peptide interacts with NREP; the interaction results in a decrease in TGFB2 autoinduction. Ref.3 Ref.4 Ref.5
Subcellular location	Secreted.
Post-translational modification	The precursor is cleaved into mature TGF-beta-2 and LAP, which remains non-covalently linked to mature TGF-beta-2 rendering it inactive By similarity.
Sequence similarities	Belongs to the TGF-beta family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SMAD protein import into nucleus Inferred from sequence or structural similarity. Source: UniProtKB activation of protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB activation-induced cell death of T cells Inferred from direct assay PubMed 8206089. Source: MGI axon guidance Inferred from mutant phenotype PubMed 15528466. Source: MGI blood vessel development Inferred from mutant phenotype PubMed 15528466. Source: MGI blood vessel remodeling Inferred from mutant phenotype PubMed 12393102. Source: MGI cardiac epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: UniProtKB cardiac left ventricle morphogenesis Traceable author statement PubMed 20299672. Source: DFLAT cardiac muscle cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB cardiac right ventricle morphogenesis Traceable author statement PubMed 20299672. Source: DFLAT cardioblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB cartilage condensation Inferred from genetic interaction PubMed 8565825. Source: MGI catagen Inferred from sequence or structural similarity. Source: UniProtKB cell cycle arrest Inferred from sequence or structural similarity. Source: UniProtKB cell growth Inferred from electronic annotation. Source: InterPro cell-cell junction organization Inferred from sequence or structural similarity. Source: UniProtKB collagen fibril organization Inferred from sequence or structural similarity. Source: UniProtKB dopamine biosynthetic process Inferred from mutant phenotype PubMed 16257223. Source: UniProtKB embryonic digestive tract development Inferred from electronic annotation. Source: Compara eye development Inferred from sequence or structural similarity. Source: UniProtKB face morphogenesis Inferred from expression pattern PubMed 18498113. Source: UniProtKB glial cell migration Inferred from sequence or structural similarity. Source: UniProtKB hair follicle morphogenesis Inferred from mutant phenotype PubMed 10433821. Source: UniProtKB hemopoiesis Inferred from mutant phenotype PubMed 14707111. Source: UniProtKB induction of apoptosis Inferred from direct assay PubMed 8206089. Source: MGI menstrual cycle phase Inferred from electronic annotation. Source: Compara negative regulation of alkaline phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from electronic annotation. Source: Compara negative regulation of epithelial cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of keratinocyte differentiation Non-traceable author statement PubMed 10433821. Source: UniProtKB negative regulation of macrophage cytokine production Inferred from sequence or structural similarity. Source: UniProtKB neuron fate commitment Inferred from direct assay PubMed 15744664. Source: MGI neutrophil chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB outflow tract morphogenesis Traceable author statement PubMed 20299672. Source: DFLAT pathway-restricted SMAD protein phosphorylation Inferred from direct assay PubMed 12773577. Source: BHF-UCL positive regulation of cardioblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of catagen Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell adhesion mediated by integrin Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell cycle Inferred from mutant phenotype PubMed 14707111. Source: UniProtKB positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of gene expression Inferred from direct assay PubMed 18498113. Source: UniProtKB positive regulation of heart contraction Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of immune response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of integrin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ossification Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein secretion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of stress-activated MAPK cascade Inferred from sequence or structural similarity. Source: UniProtKB regulation of transforming growth factor beta2 production Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from sequence or structural similarity. Source: UniProtKB response to hypoxia Inferred from sequence or structural similarity. Source: UniProtKB response to progesterone stimulus Inferred from sequence or structural similarity. Source: UniProtKB salivary gland morphogenesis Inferred from electronic annotation. Source: Compara somatic stem cell division Inferred from direct assay PubMed 14707111. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB ventricular septum morphogenesis Traceable author statement PubMed 20299672. Source: DFLAT wound healing Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	axon Inferred from direct assay PubMed 16257223. Source: UniProtKB extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from direct assay PubMed 8164195. Source: MGI neuronal cell body Inferred from direct assay PubMed 16257223. Source: UniProtKB
Molecular_function	beta-amyloid binding Inferred from sequence or structural similarity. Source: UniProtKB growth factor activity Traceable author statement PubMed 16257223. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB receptor signaling protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB type II transforming growth factor beta receptor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 302	282	Latency-associated peptide		PRO_0000033786
	Chain	303 – 414	112	Transforming growth factor beta-2		PRO_0000033787
Amino acid modifications
	Glycosylation	72	1	N-linked (GlcNAc...) Potential
	Glycosylation	140	1	N-linked (GlcNAc...) Potential
	Glycosylation	241	1	N-linked (GlcNAc...) Potential
	Disulfide bond	309 ↔ 318		By similarity
	Disulfide bond	317 ↔ 380		By similarity
	Disulfide bond	346 ↔ 411		By similarity
	Disulfide bond	350 ↔ 413		By similarity
	Disulfide bond	379		Interchain By similarity
Experimental info
	Sequence conflict	95 – 96	2	DE → EQ in CAA40672. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P27090 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: DB37A7C38881F286	FASTA	414	47,589
	10 20 30 40 50 60 MHYCVLSTFL LLHLVPVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP 70 80 90 100 110 120 DEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPS HLPSENAIPP 130 140 150 160 170 180 TFYRPYFRIV RFDVSTMEKN ASNLVKAEFR VFRLQNPKAR VAEQRIELYQ ILKSKDLTSP 190 200 210 220 230 240 TQRYIDSKVV KTRAEGEWLS FDVTDAVQEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP 250 260 270 280 290 300 NKSEELEARF AGIDGTSTYA SGDQKTIKST RKKTSGKTPH LLLMLLPSYR LESQQSSRRK 310 320 330 340 350 360 KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH 370 380 390 400 410 TKVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGNTPKI EQLSNMIVKS CKCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine transforming growth factor-beta 2 cDNA sequence and expression in adult tissues and embryos." Miller D.A., Lee A., Pelton R.W., Chen E.Y., Moses H.L., Derynck R. Mol. Endocrinol. 3:1108-1114(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[3]	"P311 binds to the latency associated protein and downregulates the expression of TGF-beta1 and TGF-beta2." Paliwal S., Shi J., Dhru U., Zhou Y., Schuger L. Biochem. Biophys. Res. Commun. 315:1104-1109(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NREP.
[4]	"Developmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-beta signaling." Tocharus J., Tsuchiya A., Kajikawa M., Ueta Y., Oka C., Kawaichi M. Dev. Growth Differ. 46:257-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTRA3.
[5]	"HtrA1 serine protease inhibits signaling mediated by Tgfbeta family proteins." Oka C., Tsujimoto R., Kajikawa M., Koshiba-Takeuchi K., Ina J., Yano M., Tsuchiya A., Ueta Y., Soma A., Kanda H., Matsumoto M., Kawaichi M. Development 131:1041-1053(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTRA1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57413 mRNA. Translation: CAA40672.1. BC011170 mRNA. Translation: AAH11170.1.
IPI	IPI00114180.
PIR	WFMSB2. A40148.
RefSeq	NP_033393.2. NM_009367.3.
UniGene	Mm.18213.
3D structure databases
ProteinModelPortal	P27090.
SMR	P27090. Positions 21-414.
ModBase	Search...
PTM databases
PhosphoSite	P27090.
Proteomic databases
PaxDb	P27090.
PRIDE	P27090.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000045288; ENSMUSP00000043849; ENSMUSG00000039239.
GeneID	21808.
KEGG	mmu:21808.
Organism-specific databases
CTD	7042.
MGI	MGI:98726. Tgfb2.
Phylogenomic databases
eggNOG	NOG269146.
GeneTree	ENSGT00620000087687.
HOGENOM	HOG000290198.
HOVERGEN	HBG074115.
InParanoid	Q91VP5.
KO	K13376.
OMA	RAATCER.
OrthoDB	EOG43TZVH.
Gene expression databases
ArrayExpress	P27090.
Bgee	P27090.
CleanEx	MM_TGFB2.
Genevestigator	P27090.
GermOnline	ENSMUSG00000039239. Mus musculus.
Family and domain databases
InterPro	IPR001839. TGF-b_C. IPR001111. TGF-b_N. IPR016319. TGF-beta. IPR015615. TGF-beta-rel. IPR003940. TGFb2. IPR017948. TGFb_CS. [Graphical view]
PANTHER	PTHR11848. PTHR11848. 1 hit.
Pfam	PF00019. TGF_beta. 1 hit. PF00688. TGFb_propeptide. 1 hit. [Graphical view]
PIRSF	PIRSF001787. TGF-beta. 1 hit.
PRINTS	PR01423. TGFBETA. PR01425. TGFBETA2.
SMART	SM00204. TGFB. 1 hit. [Graphical view]
PROSITE	PS00250. TGF_BETA_1. 1 hit. PS51362. TGF_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TGFB2. mouse.
NextBio	301190.
SOURCE	Search...

Entry information

Entry name

TGFB2_MOUSE

Accession

Primary (citable) accession number: P27090
Secondary accession number(s): Q91VP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program