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O88393

- TGBR3_MOUSE

UniProt

O88393 - TGBR3_MOUSE

Protein

Transforming growth factor beta receptor type 3

Gene

Tgfbr3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors By similarity.By similarity

    GO - Molecular functioni

    1. coreceptor activity Source: Ensembl
    2. glycosaminoglycan binding Source: BHF-UCL
    3. heparin binding Source: Ensembl
    4. PDZ domain binding Source: BHF-UCL
    5. protein binding Source: BHF-UCL
    6. SMAD binding Source: BHF-UCL
    7. transforming growth factor beta-activated receptor activity Source: MGI
    8. transforming growth factor beta binding Source: BHF-UCL
    9. transforming growth factor beta receptor activity, type III Source: Ensembl

    GO - Biological processi

    1. blastocyst development Source: MGI
    2. blood vessel development Source: MGI
    3. BMP signaling pathway Source: Ensembl
    4. cardiac epithelial to mesenchymal transition Source: Ensembl
    5. cardiac muscle cell proliferation Source: BHF-UCL
    6. cell growth Source: Ensembl
    7. coronary vasculature development Source: DFLAT
    8. coronary vasculature morphogenesis Source: DFLAT
    9. definitive erythrocyte differentiation Source: BHF-UCL
    10. definitive hemopoiesis Source: BHF-UCL
    11. embryo development Source: DFLAT
    12. epicardial cell to mesenchymal cell transition Source: DFLAT
    13. heart trabecula formation Source: BHF-UCL
    14. immune response Source: Ensembl
    15. intracellular signal transduction Source: Ensembl
    16. in utero embryonic development Source: MGI
    17. liver development Source: BHF-UCL
    18. negative regulation of epithelial cell migration Source: MGI
    19. negative regulation of epithelial cell proliferation Source: BHF-UCL
    20. negative regulation of epithelial to mesenchymal transition Source: MGI
    21. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    22. organ regeneration Source: Ensembl
    23. palate development Source: BHF-UCL
    24. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    25. positive regulation of NF-kappaB transcription factor activity Source: MGI
    26. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    27. regulation of blood vessel size Source: DFLAT
    28. regulation of protein binding Source: Ensembl
    29. response to follicle-stimulating hormone Source: Ensembl
    30. response to hypoxia Source: Ensembl
    31. response to luteinizing hormone Source: Ensembl
    32. response to prostaglandin E Source: Ensembl
    33. transforming growth factor beta receptor complex assembly Source: Ensembl
    34. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    35. vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
    36. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
    37. visceral serous pericardium development Source: DFLAT

    Keywords - Molecular functioni

    Receptor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transforming growth factor beta receptor type 3
    Short name:
    TGF-beta receptor type 3
    Short name:
    TGFR-3
    Alternative name(s):
    Betaglycan
    Transforming growth factor beta receptor III
    Short name:
    TGF-beta receptor type III
    Gene namesi
    Name:Tgfbr3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:104637. Tgfbr3.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Secreted By similarity. Secretedextracellular spaceextracellular matrix By similarity
    Note: Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix.By similarity

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytoplasm Source: MGI
    3. endoplasmic reticulum Source: MGI
    4. external side of plasma membrane Source: Ensembl
    5. extracellular space Source: Ensembl
    6. inhibin-betaglycan-ActRII complex Source: Ensembl
    7. integral component of plasma membrane Source: DFLAT
    8. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi533 – 5331S → A: Loss of glycosaminoglycan chains; when associated with A-544. 1 Publication
    Mutagenesisi544 – 5441S → A: Loss of glycosaminoglycan chains; when associated with A-533. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 850828Transforming growth factor beta receptor type 3PRO_0000041664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi533 – 5331O-linked (Xyl...) (glycosaminoglycan)1 Publication
    Glycosylationi544 – 5441O-linked (Xyl...) (glycosaminoglycan)1 Publication
    Glycosylationi570 – 5701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi589 – 5891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi638 ↔ 7041 Publication
    Disulfide bondi659 ↔ 7281 Publication
    Glycosylationi696 – 6961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi709 ↔ 7211 Publication

    Post-translational modificationi

    Extensively modified by glycosaminoglycan (GAG), either chondroitin sulfate or heparan sulfate depending upon the tissue of origin.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan

    Proteomic databases

    PRIDEiO88393.

    PTM databases

    PhosphoSiteiO88393.

    Expressioni

    Gene expression databases

    BgeeiO88393.
    CleanExiMM_TGFBR3.
    GenevestigatoriO88393.

    Interactioni

    Subunit structurei

    Interacts with TCTEX1D4.By similarity

    Protein-protein interaction databases

    BioGridi204165. 1 interaction.

    Structurei

    Secondary structure

    1
    850
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi592 – 5998
    Beta strandi607 – 6126
    Beta strandi617 – 62711
    Beta strandi629 – 64416
    Beta strandi646 – 6483
    Beta strandi653 – 6564
    Beta strandi666 – 67510
    Turni676 – 6794
    Beta strandi680 – 69011
    Beta strandi695 – 71420
    Turni724 – 7285
    Beta strandi747 – 75610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AJVX-ray2.70A591-757[»]
    ProteinModelPortaliO88393.
    SMRiO88393. Positions 587-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 785763ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini809 – 85042CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei786 – 80823HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini454 – 728275ZPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni735 – 74915Interaction with TGF-beta ligandAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ZP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG40778.
    GeneTreeiENSGT00530000063861.
    HOGENOMiHOG000090193.
    HOVERGENiHBG057515.
    InParanoidiO88393.
    KOiK05843.
    OrthoDBiEOG72ZCDK.
    PhylomeDBiO88393.
    TreeFamiTF337375.

    Family and domain databases

    InterProiIPR001507. ZP_dom.
    IPR017977. ZP_dom_CS.
    [Graphical view]
    PfamiPF00100. Zona_pellucida. 1 hit.
    [Graphical view]
    PRINTSiPR00023. ZPELLUCIDA.
    SMARTiSM00241. ZP. 1 hit.
    [Graphical view]
    PROSITEiPS00682. ZP_1. 1 hit.
    PS51034. ZP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O88393-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVTSHHMVP VFVLMSACLA TAGPEPSTRC ELSPISASHP VQALMESFTV    50
    LSGCASRGTT GLPREVHILN LRSTDQGLGQ PQREVTLHLN PIASVHTHHK 100
    PVVFLLNSPQ PLVWHVKTER LAAGVPRLFL VSEGSVVQFS SGNFSLTAET 150
    EERSFPQENE HLLHWAQKEY GAVTSFTELK IARNIYIKVG EDQVFPPTCN 200
    IGKNFLSLNY LAEYLQPKAA EGCVLASQPH EKEVHIIELI SPNSNPYSTF 250
    QVDIIIDIRP AREDPEVVKN LVLILKCKKS VNWVIKSFDV KGNLKVIAPD 300
    SIGFGKESER SMTVTKLVRN DYPSTQENLM KWALDNGYSP VTSYTIAPVA 350
    NRFHLRLENN EEMRDEEVHT IPPELRILLG PDHLPALDSP PFQGEIPNGG 400
    FPFPFPDIPR RGWKEGEDRI PRPKEPIIPR VQLLPDHREP EEVQGGVNIA 450
    LSVKCDNEKM VVAVDKDSFQ TNGYSGMELT LLDPSCKAKM NGTHFVLESP 500
    LNGCGTRHRR SAPDGVVYYN SIVVQAPSPG DSSGWPDGYE DLESGDNGFP 550
    GDTDEGETAP LSRAGVVVFN CSLRQLRSPS GFQDQLDGNA TFNMELYNTD 600
    LFLVPSPGVF SVAENEHVYV EVSVTKADQD LGFAIQTCFI SPYSNPDRMS 650
    DYTIIENICP KDDSVKFYSS KRVHFPIPHA EVDKKRFSFV FKSVFNTSLL 700
    FLHCELTLCS RNKGSQKLPK CVTPDDACTS LDATMIWTMM QNKKTFTKPL 750
    AVVLQVDYKE NVPNMKESSP VPPPPQIFHG LDTLTVMGIA FAAFVIGALL 800
    TGALWYIYSH TGETARRQQV PTSPPASENS SAAHSIGSTQ STPCSSSSTA 850
    Length:850
    Mass (Da):93,829
    Last modified:November 1, 1998 - v1
    Checksum:i4154D034C7307C86
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti322 – 3221Y → I in AAH70428. (PubMed:15489334)Curated
    Sequence conflicti391 – 3911P → S in AAH70428. (PubMed:15489334)Curated
    Sequence conflicti712 – 7121N → K in AAH70428. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039601 mRNA. Translation: AAC28564.1.
    BC070428 mRNA. Translation: AAH70428.1.
    CCDSiCCDS19499.1.
    RefSeqiNP_035708.2. NM_011578.3.
    UniGeneiMm.200775.

    Genome annotation databases

    EnsembliENSMUST00000031224; ENSMUSP00000031224; ENSMUSG00000029287.
    GeneIDi21814.
    KEGGimmu:21814.
    UCSCiuc008ylz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039601 mRNA. Translation: AAC28564.1 .
    BC070428 mRNA. Translation: AAH70428.1 .
    CCDSi CCDS19499.1.
    RefSeqi NP_035708.2. NM_011578.3.
    UniGenei Mm.200775.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AJV X-ray 2.70 A 591-757 [» ]
    ProteinModelPortali O88393.
    SMRi O88393. Positions 587-755.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204165. 1 interaction.

    PTM databases

    PhosphoSitei O88393.

    Proteomic databases

    PRIDEi O88393.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031224 ; ENSMUSP00000031224 ; ENSMUSG00000029287 .
    GeneIDi 21814.
    KEGGi mmu:21814.
    UCSCi uc008ylz.2. mouse.

    Organism-specific databases

    CTDi 7049.
    MGIi MGI:104637. Tgfbr3.

    Phylogenomic databases

    eggNOGi NOG40778.
    GeneTreei ENSGT00530000063861.
    HOGENOMi HOG000090193.
    HOVERGENi HBG057515.
    InParanoidi O88393.
    KOi K05843.
    OrthoDBi EOG72ZCDK.
    PhylomeDBi O88393.
    TreeFami TF337375.

    Miscellaneous databases

    NextBioi 301212.
    PROi O88393.
    SOURCEi Search...

    Gene expression databases

    Bgeei O88393.
    CleanExi MM_TGFBR3.
    Genevestigatori O88393.

    Family and domain databases

    InterProi IPR001507. ZP_dom.
    IPR017977. ZP_dom_CS.
    [Graphical view ]
    Pfami PF00100. Zona_pellucida. 1 hit.
    [Graphical view ]
    PRINTSi PR00023. ZPELLUCIDA.
    SMARTi SM00241. ZP. 1 hit.
    [Graphical view ]
    PROSITEi PS00682. ZP_1. 1 hit.
    PS51034. ZP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites."
      Ponce-Castaneda M.V., Esparza-Lopez J., Vilchis-Landeros M.M., Mendoza V., Lopez-Casillas F.
      Biochim. Biophys. Acta 1384:189-196(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION AT SER-533 AND SER-544, MUTAGENESIS OF SER-533 AND SER-544.
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Identification of a novel TGF-beta-binding site in the zona pellucida C-terminal (ZP-C) domain of TGF-beta-receptor-3 (TGFR-3)."
      Diestel U., Resch M., Meinhardt K., Weiler S., Hellmann T.V., Mueller T.D., Nickel J., Eichler J., Muller Y.A.
      PLoS ONE 8:E67214-E67214(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 591-757, DISULFIDE BONDS, INTERACTION WITH TGF-BETA.

    Entry informationi

    Entry nameiTGBR3_MOUSE
    AccessioniPrimary (citable) accession number: O88393
    Secondary accession number(s): Q6NS72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 98 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3