TGBR3_RAT
ID TGBR3_RAT Reviewed; 853 AA.
AC P26342;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1657406; DOI=10.1016/0092-8674(91)90073-8;
RA Lopez-Casillas F., Cheifetz S., Doody J., Andres J.L., Lane W.S.,
RA Massague J.;
RT "Structure and expression of the membrane proteoglycan betaglycan, a
RT component of the TGF-beta receptor system.";
RL Cell 67:785-795(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 378-388 AND 427-434.
RX PubMed=1657407; DOI=10.1016/0092-8674(91)90074-9;
RA Wang X.-F., Lin H.Y., Ng-Eaton E., Downward J., Lodish H.F., Weinberg R.A.;
RT "Expression cloning and characterization of the TGF-beta type III
RT receptor.";
RL Cell 67:797-805(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 591-763, GLYCOSYLATION AT ASN-591
RP AND ASN-698, AND DISULFIDE BONDS.
RX PubMed=21402931; DOI=10.1073/pnas.1010689108;
RA Lin S.J., Hu Y., Zhu J., Woodruff T.K., Jardetzky T.S.;
RT "Structure of betaglycan zona pellucida (ZP)-C domain provides insights
RT into ZP-mediated protein polymerization and TGF-beta binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5232-5236(2011).
CC -!- FUNCTION: Binds to TGF-beta. Could be involved in capturing and
CC retaining TGF-beta for presentation to the signaling receptors.
CC -!- SUBUNIT: Interacts with DYNLT4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Secreted. Secreted, extracellular space, extracellular matrix.
CC Note=Exists both as a membrane-bound form and as soluble form in serum
CC and in the extracellular matrix.
CC -!- PTM: Extensively modified by glycosaminoglycan groups (GAG).
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DR EMBL; M77809; AAA40813.1; -; mRNA.
DR EMBL; M80784; AAA42236.1; -; mRNA.
DR PIR; A41220; A41220.
DR RefSeq; NP_058952.1; NM_017256.1.
DR PDB; 3QW9; X-ray; 2.00 A; A/B=591-763.
DR PDBsum; 3QW9; -.
DR AlphaFoldDB; P26342; -.
DR SMR; P26342; -.
DR DIP; DIP-6248N; -.
DR STRING; 10116.ENSRNOP00000002867; -.
DR GlyGen; P26342; 8 sites.
DR iPTMnet; P26342; -.
DR PhosphoSitePlus; P26342; -.
DR PaxDb; P26342; -.
DR PRIDE; P26342; -.
DR Ensembl; ENSRNOT00000002867; ENSRNOP00000002867; ENSRNOG00000002093.
DR GeneID; 29610; -.
DR KEGG; rno:29610; -.
DR UCSC; RGD:61821; rat.
DR CTD; 7049; -.
DR RGD; 61821; Tgfbr3.
DR eggNOG; ENOG502QWNZ; Eukaryota.
DR GeneTree; ENSGT00530000063861; -.
DR HOGENOM; CLU_018613_0_0_1; -.
DR InParanoid; P26342; -.
DR OMA; QKDRKRF; -.
DR OrthoDB; 1263397at2759; -.
DR PhylomeDB; P26342; -.
DR TreeFam; TF337375; -.
DR EvolutionaryTrace; P26342; -.
DR PRO; PR:P26342; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002093; Expressed in lung and 19 other tissues.
DR Genevisible; P26342; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; TAS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0048185; F:activin binding; IDA:RGD.
DR GO; GO:0015026; F:coreceptor activity; ISO:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; IDA:RGD.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; ISO:RGD.
DR GO; GO:0070123; F:transforming growth factor beta receptor activity, type III; IDA:BHF-UCL.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; IDA:BHF-UCL.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0032963; P:collagen metabolic process; ISO:RGD.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; ISO:RGD.
DR GO; GO:0060216; P:definitive hemopoiesis; ISO:RGD.
DR GO; GO:0060939; P:epicardium-derived cardiac fibroblast cell development; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
DR GO; GO:0061384; P:heart trabecula morphogenesis; ISO:RGD.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0003150; P:muscular septum morphogenesis; ISO:RGD.
DR GO; GO:1902338; P:negative regulation of apoptotic process involved in morphogenesis; ISO:RGD.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0043393; P:regulation of protein binding; IDA:RGD.
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:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0034699; P:response to luteinizing hormone; ISO:RGD.
DR GO; GO:0034695; P:response to prostaglandin E; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0062009; P:secondary palate development; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; NAS:BHF-UCL.
DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; IMP:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISO:RGD.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
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; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Membrane; Proteoglycan; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..853
FT /note="Transforming growth factor beta receptor type 3"
FT /id="PRO_0000041666"
FT TOPO_DOM 24..789
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 812..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 456..730
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 530..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..751
FT /note="Interaction with TGF-beta ligand"
FT /evidence="ECO:0000250"
FT REGION 820..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 546
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21402931"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21402931"
FT DISULFID 640..706
FT /evidence="ECO:0000269|PubMed:21402931"
FT DISULFID 661..730
FT /evidence="ECO:0000269|PubMed:21402931"
FT DISULFID 711..723
FT /evidence="ECO:0000250"
FT CONFLICT 164
FT /note="L -> V (in Ref. 2; AAA42236)"
FT /evidence="ECO:0000305"
FT STRAND 592..601
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 619..629
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 633..644
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 668..677
FT /evidence="ECO:0007829|PDB:3QW9"
FT TURN 678..681
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 682..692
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 700..717
FT /evidence="ECO:0007829|PDB:3QW9"
FT HELIX 726..731
FT /evidence="ECO:0007829|PDB:3QW9"
FT STRAND 746..754
FT /evidence="ECO:0007829|PDB:3QW9"
SQ SEQUENCE 853 AA; 94103 MW; AF7078599560A928 CRC64;
MAVTSHHMIP VMVVLMSACL ATAGPEPSTR CELSPINASH PVQALMESFT VLSGCASRGT
TGLPREVHVL NLRSTDQGPG QRQREVTLHL NPIASVHTHH KPIVFLLNSP QPLVWHLKTE
RLAAGVPRLF LVSEGSVVQF PSGNFSLTAE TEERNFPQEN EHLLRWAQKE YGAVTSFTEL
KIARNIYIKV GEDQVFPPTC NIGKNFLSLN YLAEYLQPKA AEGCVLPSQP HEKEVHIIEL
ITPSSNPYSA FQVDIIVDIR PAQEDPEVVK NLVLILKCKK SVNWVIKSFD VKGNLKVIAP
NSIGFGKESE RSMTMTKLVR DDIPSTQENL MKWALDNGYR PVTSYTMAPV ANRFHLRLEN
NEEMRDEEVH TIPPELRILL DPDHPPALDN PLFPGEGSPN GGLPFPFPDI PRRGWKEGED
RIPRPKQPIV PSVQLLPDHR EPEEVQGGVD IALSVKCDHE KMVVAVDKDS FQTNGYSGME
LTLLDPSCKA KMNGTHFVLE SPLNGCGTRH RRSTPDGVVY YNSIVVQAPS PGDSSGWPDG
YEDLESGDNG FPGDGDEGET APLSRAGVVV FNCSLRQLRN PSGFQGQLDG NATFNMELYN
TDLFLVPSPG VFSVAENEHV YVEVSVTKAD QDLGFAIQTC FLSPYSNPDR MSDYTIIENI
CPKDDSVKFY SSKRVHFPIP HAEVDKKRFS FLFKSVFNTS LLFLHCELTL CSRKKGSLKL
PRCVTPDDAC TSLDATMIWT MMQNKKTFTK PLAVVLQVDY KENVPSTKDS SPIPPPPPQI
FHGLDTLTVM GIAFAAFVIG ALLTGALWYI YSHTGETARR QQVPTSPPAS ENSSAAHSIG
STQSTPCSSS STA
