TGBR3_MOUSE
ID TGBR3_MOUSE Reviewed; 850 AA.
AC O88393; Q6NS72;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transforming growth factor beta receptor type 3;
DE Short=TGF-beta receptor type 3;
DE Short=TGFR-3;
DE AltName: Full=Betaglycan;
DE AltName: Full=Transforming growth factor beta receptor III;
DE Short=TGF-beta receptor type III;
DE Flags: Precursor;
GN Name=Tgfbr3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION AT SER-533 AND SER-544, AND
RP MUTAGENESIS OF SER-533 AND SER-544.
RX PubMed=9659379; DOI=10.1016/s0167-4838(98)00033-8;
RA Ponce-Castaneda M.V., Esparza-Lopez J., Vilchis-Landeros M.M., Mendoza V.,
RA Lopez-Casillas F.;
RT "Murine betaglycan primary structure, expression and glycosaminoglycan
RT attachment sites.";
RL Biochim. Biophys. Acta 1384:189-196(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 591-757, DISULFIDE BONDS, AND
RP INTERACTION WITH TGF-BETA.
RX PubMed=23826237; DOI=10.1371/journal.pone.0067214;
RA Diestel U., Resch M., Meinhardt K., Weiler S., Hellmann T.V., Mueller T.D.,
RA Nickel J., Eichler J., Muller Y.A.;
RT "Identification of a novel TGF-beta-binding site in the zona pellucida C-
RT terminal (ZP-C) domain of TGF-beta-receptor-3 (TGFR-3).";
RL PLoS ONE 8:E67214-E67214(2013).
CC -!- FUNCTION: Binds to TGF-beta. Could be involved in capturing and
CC retaining TGF-beta for presentation to the signaling receptors (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DYNLT4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Secreted {ECO:0000250}. Secreted,
CC extracellular space, extracellular matrix {ECO:0000250}. Note=Exists
CC both as a membrane-bound form and as soluble form in serum and in the
CC extracellular matrix. {ECO:0000250}.
CC -!- PTM: Extensively modified by glycosaminoglycan (GAG), either
CC chondroitin sulfate or heparan sulfate depending upon the tissue of
CC origin.
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DR EMBL; AF039601; AAC28564.1; -; mRNA.
DR EMBL; BC070428; AAH70428.1; -; mRNA.
DR CCDS; CCDS19499.1; -.
DR RefSeq; NP_035708.2; NM_011578.4.
DR PDB; 4AJV; X-ray; 2.70 A; A=591-757.
DR PDBsum; 4AJV; -.
DR AlphaFoldDB; O88393; -.
DR SMR; O88393; -.
DR BioGRID; 204165; 2.
DR STRING; 10090.ENSMUSP00000031224; -.
DR GlyGen; O88393; 7 sites.
DR iPTMnet; O88393; -.
DR PhosphoSitePlus; O88393; -.
DR MaxQB; O88393; -.
DR PaxDb; O88393; -.
DR PeptideAtlas; O88393; -.
DR PRIDE; O88393; -.
DR ProteomicsDB; 263036; -.
DR DNASU; 21814; -.
DR GeneID; 21814; -.
DR KEGG; mmu:21814; -.
DR UCSC; uc008ylz.2; mouse.
DR CTD; 7049; -.
DR MGI; MGI:104637; Tgfbr3.
DR eggNOG; ENOG502QWNZ; Eukaryota.
DR InParanoid; O88393; -.
DR OrthoDB; 1263397at2759; -.
DR PhylomeDB; O88393; -.
DR TreeFam; TF337375; -.
DR BioGRID-ORCS; 21814; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Tgfbr3; mouse.
DR PRO; PR:O88393; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88393; protein.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0048185; F:activin binding; ISO:MGI.
DR GO; GO:0015026; F:coreceptor activity; ISO:MGI.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; IPI:BHF-UCL.
DR GO; GO:0046332; F:SMAD binding; IMP:BHF-UCL.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IDA:MGI.
DR GO; GO:0070123; F:transforming growth factor beta receptor activity, type III; ISO:MGI.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IMP:MGI.
DR GO; GO:0001824; P:blastocyst development; IDA:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0097746; P:blood vessel diameter maintenance; TAS:DFLAT.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0032963; P:collagen metabolic process; IGI:BHF-UCL.
DR GO; GO:0060976; P:coronary vasculature development; TAS:DFLAT.
DR GO; GO:0060977; P:coronary vasculature morphogenesis; TAS:DFLAT.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:BHF-UCL.
DR GO; GO:0003347; P:epicardial cell to mesenchymal cell transition; TAS:DFLAT.
DR GO; GO:0060939; P:epicardium-derived cardiac fibroblast cell development; IMP:BHF-UCL.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0060347; P:heart trabecula formation; IMP:BHF-UCL.
DR GO; GO:0061384; P:heart trabecula morphogenesis; IMP:BHF-UCL.
DR GO; GO:0006955; P:immune response; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0001889; P:liver development; IMP:BHF-UCL.
DR GO; GO:0003150; P:muscular septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:1902338; P:negative regulation of apoptotic process involved in morphogenesis; IMP:MGI.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0043393; P:regulation of protein binding; ISO:MGI.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; ISO:MGI.
DR GO; GO:0034699; P:response to luteinizing hormone; ISO:MGI.
DR GO; GO:0034695; P:response to prostaglandin E; ISO:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; IMP:BHF-UCL.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT.
DR DisProt; DP02636; -.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Membrane; Proteoglycan; Receptor; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..850
FT /note="Transforming growth factor beta receptor type 3"
FT /id="PRO_0000041664"
FT TOPO_DOM 23..785
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..850
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 454..728
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 528..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..749
FT /note="Interaction with TGF-beta ligand"
FT REGION 817..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:9659379"
FT CARBOHYD 544
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:9659379"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 638..704
FT /evidence="ECO:0000269|PubMed:23826237"
FT DISULFID 659..728
FT /evidence="ECO:0000269|PubMed:23826237"
FT DISULFID 709..721
FT /evidence="ECO:0000269|PubMed:23826237"
FT MUTAGEN 533
FT /note="S->A: Loss of glycosaminoglycan chains; when
FT associated with A-544."
FT /evidence="ECO:0000269|PubMed:9659379"
FT MUTAGEN 544
FT /note="S->A: Loss of glycosaminoglycan chains; when
FT associated with A-533."
FT /evidence="ECO:0000269|PubMed:9659379"
FT CONFLICT 322
FT /note="Y -> I (in Ref. 2; AAH70428)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="P -> S (in Ref. 2; AAH70428)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="N -> K (in Ref. 2; AAH70428)"
FT /evidence="ECO:0000305"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 617..627
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 629..644
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 666..675
FT /evidence="ECO:0007829|PDB:4AJV"
FT TURN 676..679
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 680..690
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 695..714
FT /evidence="ECO:0007829|PDB:4AJV"
FT TURN 724..728
FT /evidence="ECO:0007829|PDB:4AJV"
FT STRAND 747..756
FT /evidence="ECO:0007829|PDB:4AJV"
SQ SEQUENCE 850 AA; 93829 MW; 4154D034C7307C86 CRC64;
MAVTSHHMVP VFVLMSACLA TAGPEPSTRC ELSPISASHP VQALMESFTV LSGCASRGTT
GLPREVHILN LRSTDQGLGQ PQREVTLHLN PIASVHTHHK PVVFLLNSPQ PLVWHVKTER
LAAGVPRLFL VSEGSVVQFS SGNFSLTAET EERSFPQENE HLLHWAQKEY GAVTSFTELK
IARNIYIKVG EDQVFPPTCN IGKNFLSLNY LAEYLQPKAA EGCVLASQPH EKEVHIIELI
SPNSNPYSTF QVDIIIDIRP AREDPEVVKN LVLILKCKKS VNWVIKSFDV KGNLKVIAPD
SIGFGKESER SMTVTKLVRN DYPSTQENLM KWALDNGYSP VTSYTIAPVA NRFHLRLENN
EEMRDEEVHT IPPELRILLG PDHLPALDSP PFQGEIPNGG FPFPFPDIPR RGWKEGEDRI
PRPKEPIIPR VQLLPDHREP EEVQGGVNIA LSVKCDNEKM VVAVDKDSFQ TNGYSGMELT
LLDPSCKAKM NGTHFVLESP LNGCGTRHRR SAPDGVVYYN SIVVQAPSPG DSSGWPDGYE
DLESGDNGFP GDTDEGETAP LSRAGVVVFN CSLRQLRSPS GFQDQLDGNA TFNMELYNTD
LFLVPSPGVF SVAENEHVYV EVSVTKADQD LGFAIQTCFI SPYSNPDRMS DYTIIENICP
KDDSVKFYSS KRVHFPIPHA EVDKKRFSFV FKSVFNTSLL FLHCELTLCS RNKGSQKLPK
CVTPDDACTS LDATMIWTMM QNKKTFTKPL AVVLQVDYKE NVPNMKESSP VPPPPQIFHG
LDTLTVMGIA FAAFVIGALL TGALWYIYSH TGETARRQQV PTSPPASENS SAAHSIGSTQ
STPCSSSSTA
