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Protein

Transforming growth factor beta-3

Gene

Tgfb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in embryogenesis and cell differentiation.

GO - Molecular functioni

GO - Biological processi

  • cell-cell junction organization Source: AgBase
  • cell development Source: GO_Central
  • cell growth Source: InterPro
  • cellular response to growth factor stimulus Source: MGI
  • detection of hypoxia Source: AgBase
  • face morphogenesis Source: UniProtKB
  • in utero embryonic development Source: MGI
  • lung alveolus development Source: BHF-UCL
  • mammary gland development Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of DNA replication Source: AgBase
  • negative regulation of macrophage cytokine production Source: AgBase
  • negative regulation of neuron apoptotic process Source: MGI
  • organ morphogenesis Source: MGI
  • ossification involved in bone remodeling Source: AgBase
  • palate development Source: BHF-UCL
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of bone mineralization Source: AgBase
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of collagen biosynthetic process Source: AgBase
  • positive regulation of DNA replication Source: AgBase
  • positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • positive regulation of filopodium assembly Source: MGI
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • positive regulation of protein secretion Source: MGI
  • positive regulation of SMAD protein import into nucleus Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of MAPK cascade Source: GO_Central
  • response to hypoxia Source: AgBase
  • response to progesterone Source: AgBase
  • salivary gland morphogenesis Source: AgBase
  • SMAD protein signal transduction Source: GO_Central
  • transforming growth factor beta receptor signaling pathway Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiREACT_307071. Platelet degranulation.
REACT_332220. Molecules associated with elastic fibres.
REACT_354321. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming growth factor beta-3
Short name:
TGF-beta-3
Cleaved into the following chain:
Gene namesi
Name:Tgfb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:98727. Tgfb3.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: MGI
  • extracellular space Source: GO_Central
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 298275Latency-associated peptideBy similarityPRO_0000033798Add
BLAST
Chaini299 – 410112Transforming growth factor beta-3PRO_0000033799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi305 ↔ 314By similarity
Disulfide bondi313 ↔ 376By similarity
Disulfide bondi342 ↔ 407By similarity
Disulfide bondi346 ↔ 409By similarity
Disulfide bondi375 – 375InterchainBy similarity

Post-translational modificationi

The precursor is cleaved into mature TGF-beta-3 and LAP, which remains non-covalently linked to mature TGF-beta-3 rendering it inactive.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP17125.

PTM databases

PhosphoSiteiP17125.

Expressioni

Tissue specificityi

Expressed in both testis and ovary.

Gene expression databases

BgeeiP17125.
CleanExiMM_TGFB3.
ExpressionAtlasiP17125. baseline and differential.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interacts with ASPN (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003687.

Structurei

3D structure databases

ProteinModelPortaliP17125.
SMRiP17125. Positions 22-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi259 – 2613Cell attachment siteSequence Analysis

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG269146.
HOVERGENiHBG074115.
InParanoidiP17125.
PhylomeDBiP17125.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR015618. TGFB3.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PIRSFiPIRSF001787. TGF-beta. 1 hit.
PRINTSiPR01423. TGFBETA.
PR01426. TGFBETA3.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17125-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLQRALVVL ALLNLATISL SLSTCTTLDF GHIKKKRVEA IRGQILSKLR
60 70 80 90 100
LTSPPEPSVM THVPYQVLAL YNSTRELLEE MHGEREEGCT QETSESEYYA
110 120 130 140 150
KEIHKFDMIQ GLAEHNELAV CPKGITSKVF RFNVSSVEKN GTNLFRAEFR
160 170 180 190 200
VLRVPNPSSK RTEQRIELFQ ILRPDEHIAK QRYIGGKNLP TRGTAEWLSF
210 220 230 240 250
DVTDTVREWL LRRESNLGLE ISIHCPCHTF QPNGDILENV HEVMEIKFKG
260 270 280 290 300
VDNEDDHGRG DLGRLKKQKD HHNPHLILMM IPPHRLDSPG QGSQRKKRAL
310 320 330 340 350
DTNYCFRNLE ENCCVRPLYI DFRQDLGWKW VHEPKGYYAN FCSGPCPYLR
360 370 380 390 400
SADTTHSTVL GLYNTLNPEA SASPCCVPQD LEPLTILYYV GRTPKVEQLS
410
NMVVKSCKCS
Length:410
Mass (Da):46,885
Last modified:August 1, 1990 - v1
Checksum:i250F7048CA432BD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32745 mRNA. Translation: AAA40422.1.
PIRiA41397.
UniGeneiMm.3992.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32745 mRNA. Translation: AAA40422.1.
PIRiA41397.
UniGeneiMm.3992.

3D structure databases

ProteinModelPortaliP17125.
SMRiP17125. Positions 22-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003687.

PTM databases

PhosphoSiteiP17125.

Proteomic databases

PRIDEiP17125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:98727. Tgfb3.

Phylogenomic databases

eggNOGiNOG269146.
HOVERGENiHBG074115.
InParanoidiP17125.
PhylomeDBiP17125.

Enzyme and pathway databases

ReactomeiREACT_307071. Platelet degranulation.
REACT_332220. Molecules associated with elastic fibres.
REACT_354321. ECM proteoglycans.

Miscellaneous databases

PROiP17125.
SOURCEiSearch...

Gene expression databases

BgeeiP17125.
CleanExiMM_TGFB3.
ExpressionAtlasiP17125. baseline and differential.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR015618. TGFB3.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PIRSFiPIRSF001787. TGF-beta. 1 hit.
PRINTSiPR01423. TGFBETA.
PR01426. TGFBETA3.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complementary DNA cloning of the murine transforming growth factor-beta 3 (TGF beta 3) precursor and the comparative expression of TGF beta 3 and TGF beta 1 messenger RNA in murine embryos and adult tissues."
    Miller D.A., Lee A., Matsui Y., Chen E.Y., Moses H.L., Derynck R.
    Mol. Endocrinol. 3:1926-1934(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning by polymerase chain reaction of a new mouse TGF-beta, mTGF-beta 3."
    Denhez F., Lafyatis R., Kondaiah P., Roberts A.B., Sporn M.B.
    Growth Factors 3:139-146(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cell lineage specificity of expression of the murine transforming growth factor beta 3 and transforming growth factor beta 1 genes."
    Watrin F., Scotto L., Assoian R.K., Wolgemuth D.J.
    Cell Growth Differ. 2:77-83(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 285-410.
    Tissue: Testis.

Entry informationi

Entry nameiTGFB3_MOUSE
AccessioniPrimary (citable) accession number: P17125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 22, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.