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Reviewed, UniProtKB/Swiss-Prot Q03167 (TGBR3_HUMAN)

Last modified May 26, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    TGF-beta receptor type III
Alternative name(s):
    TGFR-3
    Transforming growth factor beta receptor III
    Betaglycan
Gene names
Name: TGFBR3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length850 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Subunit structure

Interacts with TCTEX1D4. Ref.6

Subcellular location

Secreted. Secreted › extracellular space. Cell membrane; Single-pass type I membrane protein Potential. Note: Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix.

Post-translational modification

Extensively modified by glycosaminoglycan groups (GAG).

Sequence similarities

Contains 1 ZP domain.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
   Molecular functionReceptor
   PTMGlycoprotein
Proteoglycan
Gene Ontology (GO)
   Biological processBMP signaling pathway

Inferred from direct assay. Source: UniProtKB

cardiac epithelial to mesenchymal transition

Inferred from direct assay. Source: UniProtKB

cardiac muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

cell growth Ref.1

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

definitive erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

heart trabecula formation

Inferred from sequence or structural similarity. Source: UniProtKB

immune response

Inferred from mutant phenotype. Source: UniProtKB

liver development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell motion

Inferred from direct assay. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

palate development

Inferred from sequence or structural similarity. Source: UniProtKB

pathway-restricted SMAD protein phosphorylation

Inferred from mutant phenotype. Source: UniProtKB

protein kinase cascade

Inferred from mutant phenotype. Source: UniProtKB

response to follicle-stimulating hormone stimulus

Inferred from direct assay. Source: UniProtKB

response to luteinizing hormone stimulus

Inferred from direct assay. Source: UniProtKB

response to prostaglandin E stimulus

Inferred from direct assay. Source: UniProtKB

ventricular cardiac muscle morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentexternal side of plasma membrane

Inferred from direct assay. Source: UniProtKB

extracellular space

Traceable author statement. Source: UniProtKB

inhibin-betaglycan-ActRII complex

Inferred from direct assay. Source: UniProtKB

integral to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

   Molecular functionPDZ domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

SMAD binding

Inferred from mutant phenotype. Source: UniProtKB

coreceptor activity

Inferred from direct assay. Source: UniProtKB

heparin binding Ref.1

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta binding

Inferred from direct assay. Source: UniProtKB

transforming growth factor beta receptor activity, type III

Inferred from direct assay. Source: UniProtKB

type II transforming growth factor beta receptor binding

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 850830TGF-beta receptor type III
PRO_0000041663

Regions

Topological domain21 – 786766Extracellular Potential
Transmembrane787 – 80822 Potential
Topological domain809 – 85042Cytoplasmic Potential
Domain454 – 729276ZP

Amino acid modifications

Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Glycosylation5331O-linked (Xyl...) (glycosaminoglycan) By similarity
Glycosylation5441O-linked (Xyl...) (glycosaminoglycan) By similarity
Glycosylation5701N-linked (GlcNAc...) Potential
Glycosylation5891N-linked (GlcNAc...) Potential
Glycosylation6961N-linked (GlcNAc...) Potential

Natural variations

Natural variant141S → N Ref.3
VAR_020891
Natural variant151S → F: dbSNP rs1805110. Ref.3 Ref.1 Ref.2
VAR_014920
Natural variant1631W → L Ref.3
VAR_020892
Natural variant3511F → I: dbSNP rs11466592.
VAR_057499
Natural variant3581N → NA Ref.2 Ref.5
VAR_020895
Natural variant6341A → T Ref.3
VAR_020893
Natural variant7641G → R Ref.3
VAR_020894

Experimental info

Sequence conflict70 – 734RTAG → ALR in AAA67061. Ref.1
Sequence conflict349 – 3502NR → IV in AAA67061. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q03167-1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 1469BB567BD05230

FASTA85093,428
        10         20         30         40         50         60 
MTSHYVIAIF ALMSSCLATA GPEPGALCEL SPVSASHPVQ ALMESFTVLS GCASRGTTGL 

        70         80         90        100        110        120 
PQEVHVLNLR TAGQGPGQLQ REVTLHLNPI SSVHIHHKSV VFLLNSPHPL VWHLKTERLA 

       130        140        150        160        170        180 
TGVSRLFLVS EGSVVQFSSA NFSLTAETEE RNFPHGNEHL LNWARKEYGA VTSFTELKIA 

       190        200        210        220        230        240 
RNIYIKVGED QVFPPKCNIG KNFLSLNYLA EYLQPKAAEG CVMSSQPQNE EVHIIELITP 

       250        260        270        280        290        300 
NSNPYSAFQV DITIDIRPSQ EDLEVVKNLI LILKCKKSVN WVIKSFDVKG SLKIIAPNSI 

       310        320        330        340        350        360 
GFGKESERSM TMTKSIRDDI PSTQGNLVKW ALDNGYSPIT SYTMAPVANR FHLRLENNEE 

       370        380        390        400        410        420 
MGDEEVHTIP PELRILLDPG ALPALQNPPI RGGEGQNGGL PFPFPDISRR VWNEEGEDGL 

       430        440        450        460        470        480 
PRPKDPVIPS IQLFPGLREP EEVQGSVDIA LSVKCDNEKM IVAVEKDSFQ ASGYSGMDVT 

       490        500        510        520        530        540 
LLDPTCKAKM NGTHFVLESP LNGCGTRPRW SALDGVVYYN SIVIQVPALG DSSGWPDGYE 

       550        560        570        580        590        600 
DLESGDNGFP GDMDEGDASL FTRPEIVVFN CSLQQVRNPS SFQEQPHGNI TFNMELYNTD 

       610        620        630        640        650        660 
LFLVPSQGVF SVPENGHVYV EVSVTKAEQE LGFAIQTCFI SPYSNPDRMS HYTIIENICP 

       670        680        690        700        710        720 
KDESVKFYSP KRVHFPIPQA DMDKKRFSFV FKPVFNTSLL FLQCELTLCT KMEKHPQKLP 

       730        740        750        760        770        780 
KCVPPDEACT SLDASIIWAM MQNKKTFTKP LAVIHHEAES KEKGPSMKEP NPISPPIFHG 

       790        800        810        820        830        840 
LDTLTVMGIA FAAFVIGALL TGALWYIYSH TGETAGRQQV PTSPPASENS SAAHSIGSTQ 

       850 
STPCSSSSTA

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References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the human and porcine transforming growth factor-beta type III receptors."
Moren A., Ichijo H., Miyazono K.
Biochem. Biophys. Res. Commun. 189:356-362(1992) [PubMed: 1333192] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-15.
Tissue: Placenta.
[2]"Eleven single nucleotide polymorphisms and one triple nucleotide insertion of the human TGF-beta III receptor gene."
Zippert R., Baessler A., Holmer S.R., Hengstenberg C., Schunkert H.
J. Hum. Genet. 45:250-253(2000) [PubMed: 10944857] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PHE-15 AND ALA-358 INS.
Tissue: Blood.
[3]NIEHS SNPs program
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-14; PHE-15; LEU-163; THR-634 AND ARG-764.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-358 INS.
Tissue: Brain.
[6]"Identification of Tctex2beta, a novel dynein light chain family member that interacts with different transforming growth factor-beta receptors."
Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T., McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.
J. Biol. Chem. 281:37069-37080(2006) [PubMed: 16982625] [Abstract]
Cited for: INTERACTION WITH TCTEX1D4.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L07594 mRNA. Translation: AAA67061.1.
AJ251961 mRNA. Translation: CAB64374.1.
AY796304 Genomic DNA. Translation: AAV50003.1.
AL162263, AL390780, AL445992 Genomic DNA. Translation: CAI22636.1.
AL162263 expand/collapse EMBL AC list , AC099334, AL390780, AL445992 Genomic DNA. Translation: CAI22637.1.
AL390780, AL162263, AL445992 Genomic DNA. Translation: CAI14570.1.
AL390780 expand/collapse EMBL AC list , AC099334, AL162263, AL445992 Genomic DNA. Translation: CAI14571.1.
AL445992, AL162263, AL390780 Genomic DNA. Translation: CAI13392.1.
AL445992 expand/collapse EMBL AC list , AC099334, AL162263, AL390780 Genomic DNA. Translation: CAI13393.1.
BC126116 mRNA. Translation: AAI26117.1.
IPIIPI00304865.
PIRJC1350.
RefSeqNP_003234.2.
UniGeneHs.482390

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5940N.

PTM databases

PhosphoSiteQ03167.

Genome annotation databases

EnsemblENSG00000069702. Homo sapiens. [Contig view]
GeneID7049.

Organism-specific databases

GeneCardsGC01M091860.
H-InvDBHIX0028622.
HGNCHGNC:11774. TGFBR3.
HPAHPA008257.
MIM600742. gene.
PharmGKBPA36487.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ03167.

Enzyme and pathway databases

Pathway_Interaction_DBtgfbrpathway. TGF-beta receptor signaling.

Gene expression databases

ArrayExpressQ03167.
BgeeQ03167.
CleanExHS_TGFBR3.
GermOnlineENSG00000069702. Homo sapiens.

Family and domain databases

InterProIPR001507. Endoglin/CD105.
IPR017977. Endoglin/CD105_CS.
IPR017976. Endoglin/CD105_subgr.
[Graphical view]
PfamPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSPR00023. ZPELLUCIDA.
SMARTSM00241. ZP. 1 hit.
[Graphical view]
PROSITEPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio27547.
SOURCESearch...

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Entry information

Entry nameTGBR3_HUMAN
AccessionPrimary (citable) accession number: Q03167
Secondary accession number(s): A0AUW8 expand/collapse secondary AC list , Q5T2T4, Q5U731, Q9UGI2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 4, 2005
Last modified: May 26, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents