ID TGBR3_HUMAN Reviewed; 851 AA.
AC Q03167; A0AUW8; A8K5N0; B9EG88; Q5T2T4; Q5U731; Q9UGI2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 24-JAN-2024, entry version 194.
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 {ECO:0000312|HGNC:HGNC:11774};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT PHE-15.
RC TISSUE=Placenta;
RX PubMed=1333192; DOI=10.1016/0006-291x(92)91566-9;
RA Moren A., Ichijo H., Miyazono K.;
RT "Molecular cloning and characterization of the human and porcine
RT transforming growth factor-beta type III receptors.";
RL Biochem. Biophys. Res. Commun. 189:356-362(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PHE-15.
RC TISSUE=Blood;
RX PubMed=10944857; DOI=10.1007/s100380070035;
RA Zippert R., Baessler A., Holmer S.R., Hengstenberg C., Schunkert H.;
RT "Eleven single nucleotide polymorphisms and one triple nucleotide insertion
RT of the human TGF-beta III receptor gene.";
RL J. Hum. Genet. 45:250-253(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-14; PHE-15; LEU-163;
RP THR-635 AND ARG-765.
RG NIEHS SNPs program;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [7]
RP INTERACTION WITH DYNLT4.
RX PubMed=16982625; DOI=10.1074/jbc.m608614200;
RA Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T.,
RA McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.;
RT "Identification of Tctex2beta, a novel dynein light chain family member
RT that interacts with different transforming growth factor-beta receptors.";
RL J. Biol. Chem. 281:37069-37080(2006).
RN [8]
RP FUNCTION.
RX PubMed=34910520; DOI=10.1126/sciadv.abl4391;
RA Brule E., Wang Y., Li Y., Lin Y.F., Zhou X., Ongaro L., Alonso C.A.I.,
RA Buddle E.R.S., Schneyer A.L., Byeon C.H., Hinck C.S., Mendelev N.,
RA Russell J.P., Cowan M., Boehm U., Ruf-Zamojski F., Zamojski M.,
RA Andoniadou C.L., Sealfon S.C., Harrison C.A., Walton K.L., Hinck A.P.,
RA Bernard D.J.;
RT "TGFBR3L is an inhibin B co-receptor that regulates female fertility.";
RL Sci. Adv. 7:eabl4391-eabl4391(2021).
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). In gonadotrope cells, acts as an inhibin A coreceptor and
CC regulates follicle-stimulating hormone (FSH) levels and female
CC fertility (PubMed:34910520). {ECO:0000250|UniProtKB:P26342,
CC ECO:0000269|PubMed:34910520}.
CC -!- SUBUNIT: Interacts with DYNLT4. {ECO:0000269|PubMed:16982625}.
CC -!- INTERACTION:
CC Q03167; O14908: GIPC1; NbExp=3; IntAct=EBI-2852679, EBI-373132;
CC Q03167; P01137: TGFB1; NbExp=2; IntAct=EBI-2852679, EBI-779636;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26342};
CC Single-pass type I membrane protein {ECO:0000255}. Secreted
CC {ECO:0000250|UniProtKB:P26342}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:P26342}. Note=Exists both
CC as a membrane-bound form and as soluble form in serum and in the
CC extracellular matrix. {ECO:0000250|UniProtKB:P26342}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03167-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03167-2; Sequence=VSP_040018;
CC -!- PTM: Extensively modified by glycosaminoglycan groups (GAG).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67061.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/42541/TGFBR3";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tgfbr3/";
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DR EMBL; L07594; AAA67061.1; ALT_FRAME; mRNA.
DR EMBL; AJ251961; CAB64374.1; -; mRNA.
DR EMBL; AY796304; AAV50003.1; -; Genomic_DNA.
DR EMBL; AK291345; BAF84034.1; -; mRNA.
DR EMBL; AC099334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126116; AAI26117.1; -; mRNA.
DR EMBL; BC136295; AAI36296.1; -; mRNA.
DR CCDS; CCDS30770.1; -. [Q03167-1]
DR CCDS; CCDS55614.1; -. [Q03167-2]
DR PIR; JC1350; JC1350.
DR RefSeq; NP_001182612.1; NM_001195683.1. [Q03167-2]
DR RefSeq; NP_001182613.1; NM_001195684.1. [Q03167-2]
DR RefSeq; NP_003234.2; NM_003243.4. [Q03167-1]
DR RefSeq; XP_006710930.1; XM_006710867.2. [Q03167-1]
DR RefSeq; XP_006710931.1; XM_006710868.2.
DR PDB; 7LBG; EM; 2.60 A; D=1-781.
DR PDBsum; 7LBG; -.
DR AlphaFoldDB; Q03167; -.
DR EMDB; EMD-23254; -.
DR SMR; Q03167; -.
DR BioGRID; 112907; 41.
DR DIP; DIP-5940N; -.
DR IntAct; Q03167; 21.
DR MINT; Q03167; -.
DR STRING; 9606.ENSP00000212355; -.
DR GlyCosmos; Q03167; 8 sites, 1 glycan.
DR GlyGen; Q03167; 9 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q03167; -.
DR PhosphoSitePlus; Q03167; -.
DR BioMuta; TGFBR3; -.
DR DMDM; 311033535; -.
DR jPOST; Q03167; -.
DR MassIVE; Q03167; -.
DR MaxQB; Q03167; -.
DR PaxDb; 9606-ENSP00000212355; -.
DR PeptideAtlas; Q03167; -.
DR ProteomicsDB; 58197; -. [Q03167-1]
DR ProteomicsDB; 58198; -. [Q03167-2]
DR Pumba; Q03167; -.
DR Antibodypedia; 1634; 546 antibodies from 43 providers.
DR DNASU; 7049; -.
DR Ensembl; ENST00000212355.9; ENSP00000212355.4; ENSG00000069702.11. [Q03167-1]
DR Ensembl; ENST00000370399.6; ENSP00000359426.2; ENSG00000069702.11. [Q03167-2]
DR Ensembl; ENST00000465892.6; ENSP00000432638.1; ENSG00000069702.11. [Q03167-2]
DR Ensembl; ENST00000525962.5; ENSP00000436127.1; ENSG00000069702.11. [Q03167-1]
DR GeneID; 7049; -.
DR KEGG; hsa:7049; -.
DR MANE-Select; ENST00000212355.9; ENSP00000212355.4; NM_003243.5; NP_003234.2.
DR UCSC; uc001doh.4; human. [Q03167-1]
DR AGR; HGNC:11774; -.
DR CTD; 7049; -.
DR DisGeNET; 7049; -.
DR GeneCards; TGFBR3; -.
DR HGNC; HGNC:11774; TGFBR3.
DR HPA; ENSG00000069702; Low tissue specificity.
DR MalaCards; TGFBR3; -.
DR MIM; 600742; gene.
DR neXtProt; NX_Q03167; -.
DR OpenTargets; ENSG00000069702; -.
DR Orphanet; 231160; Familial cerebral saccular aneurysm.
DR PharmGKB; PA36487; -.
DR VEuPathDB; HostDB:ENSG00000069702; -.
DR eggNOG; ENOG502QWNZ; Eukaryota.
DR GeneTree; ENSGT00530000063861; -.
DR HOGENOM; CLU_018613_0_0_1; -.
DR InParanoid; Q03167; -.
DR OMA; VPQRECV; -.
DR OrthoDB; 2949260at2759; -.
DR PhylomeDB; Q03167; -.
DR TreeFam; TF337375; -.
DR PathwayCommons; Q03167; -.
DR Reactome; R-HSA-1502540; Signaling by Activin.
DR Reactome; R-HSA-190370; FGFR1b ligand binding and activation.
DR Reactome; R-HSA-190373; FGFR1c ligand binding and activation.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR SignaLink; Q03167; -.
DR SIGNOR; Q03167; -.
DR BioGRID-ORCS; 7049; 12 hits in 1156 CRISPR screens.
DR ChiTaRS; TGFBR3; human.
DR GeneWiki; TGFBR3; -.
DR GenomeRNAi; 7049; -.
DR Pharos; Q03167; Tbio.
DR PRO; PR:Q03167; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q03167; Protein.
DR Bgee; ENSG00000069702; Expressed in renal glomerulus and 205 other cell types or tissues.
DR ExpressionAtlas; Q03167; baseline and differential.
DR Genevisible; Q03167; HS.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0048185; F:activin binding; IEA:Ensembl.
DR GO; GO:0036122; F:BMP binding; IPI:BHF-UCL.
DR GO; GO:0015026; F:coreceptor activity; IDA:BHF-UCL.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISS:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; ISS:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; ISS: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:BHF-UCL.
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; ISS:BHF-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:BHF-UCL.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IDA:BHF-UCL.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0016477; P:cell migration; ISS:BHF-UCL.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; ISS:BHF-UCL.
DR GO; GO:0060216; P:definitive hemopoiesis; ISS:BHF-UCL.
DR GO; GO:0060939; P:epicardium-derived cardiac fibroblast cell development; ISS:BHF-UCL.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:BHF-UCL.
DR GO; GO:0003007; P:heart morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060347; P:heart trabecula formation; ISS:BHF-UCL.
DR GO; GO:0061384; P:heart trabecula morphogenesis; ISS:BHF-UCL.
DR GO; GO:0006955; P:immune response; IMP:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:BHF-UCL.
DR GO; GO:0001889; P:liver development; ISS:BHF-UCL.
DR GO; GO:0003150; P:muscular septum morphogenesis; ISS:BHF-UCL.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IDA:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:BHF-UCL.
DR GO; GO:1901202; P:negative regulation of extracellular matrix assembly; IMP:BHF-UCL.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; IDA:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0034699; P:response to luteinizing hormone; IDA:BHF-UCL.
DR GO; GO:0034695; P:response to prostaglandin E; IDA:BHF-UCL.
DR GO; GO:0062009; P:secondary palate development; ISS:BHF-UCL.
DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; ISS:BHF-UCL.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR048290; ZP_chr.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR14002; ENDOGLIN/TGF-BETA RECEPTOR TYPE III; 1.
DR PANTHER; PTHR14002:SF7; TRANSFORMING GROWTH FACTOR BETA RECEPTOR TYPE 3; 1.
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; Alternative splicing; Cell membrane; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Membrane; Proteoglycan; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..851
FT /note="Transforming growth factor beta receptor type 3"
FT /id="PRO_0000041663"
FT TOPO_DOM 21..787
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..851
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 455..730
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 737..751
FT /note="Interaction with TGF-beta ligand"
FT /evidence="ECO:0000250"
FT REGION 816..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 545
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 639..705
FT /evidence="ECO:0000250|UniProtKB:P26342"
FT DISULFID 660..730
FT /evidence="ECO:0000250|UniProtKB:P26342"
FT DISULFID 710..723
FT /evidence="ECO:0000250|UniProtKB:O88393"
FT VAR_SEQ 359
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1333192"
FT /id="VSP_040018"
FT VARIANT 14
FT /note="S -> N (in dbSNP:rs17884205)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020891"
FT VARIANT 15
FT /note="S -> F (in dbSNP:rs1805110)"
FT /evidence="ECO:0000269|PubMed:10944857,
FT ECO:0000269|PubMed:1333192, ECO:0000269|Ref.3"
FT /id="VAR_014920"
FT VARIANT 163
FT /note="W -> L (in dbSNP:rs17885124)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020892"
FT VARIANT 351
FT /note="F -> I (in dbSNP:rs11466592)"
FT /id="VAR_057499"
FT VARIANT 635
FT /note="A -> T (in dbSNP:rs17882578)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020893"
FT VARIANT 765
FT /note="G -> R (in dbSNP:rs17882828)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020894"
FT VARIANT 777
FT /note="P -> S (in dbSNP:rs2228363)"
FT /id="VAR_066625"
FT CONFLICT 89
FT /note="P -> S (in Ref. 4; BAF84034)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="I -> V (in Ref. 4; BAF84034)"
FT /evidence="ECO:0000305"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:7LBG"
SQ SEQUENCE 851 AA; 93499 MW; AEC56C4477C003B2 CRC64;
MTSHYVIAIF ALMSSCLATA GPEPGALCEL SPVSASHPVQ ALMESFTVLS GCASRGTTGL
PQEVHVLNLR TAGQGPGQLQ REVTLHLNPI SSVHIHHKSV VFLLNSPHPL VWHLKTERLA
TGVSRLFLVS EGSVVQFSSA NFSLTAETEE RNFPHGNEHL LNWARKEYGA VTSFTELKIA
RNIYIKVGED QVFPPKCNIG KNFLSLNYLA EYLQPKAAEG CVMSSQPQNE EVHIIELITP
NSNPYSAFQV DITIDIRPSQ EDLEVVKNLI LILKCKKSVN WVIKSFDVKG SLKIIAPNSI
GFGKESERSM TMTKSIRDDI PSTQGNLVKW ALDNGYSPIT SYTMAPVANR FHLRLENNAE
EMGDEEVHTI PPELRILLDP GALPALQNPP IRGGEGQNGG LPFPFPDISR RVWNEEGEDG
LPRPKDPVIP SIQLFPGLRE PEEVQGSVDI ALSVKCDNEK MIVAVEKDSF QASGYSGMDV
TLLDPTCKAK MNGTHFVLES PLNGCGTRPR WSALDGVVYY NSIVIQVPAL GDSSGWPDGY
EDLESGDNGF PGDMDEGDAS LFTRPEIVVF NCSLQQVRNP SSFQEQPHGN ITFNMELYNT
DLFLVPSQGV FSVPENGHVY VEVSVTKAEQ ELGFAIQTCF ISPYSNPDRM SHYTIIENIC
PKDESVKFYS PKRVHFPIPQ ADMDKKRFSF VFKPVFNTSL LFLQCELTLC TKMEKHPQKL
PKCVPPDEAC TSLDASIIWA MMQNKKTFTK PLAVIHHEAE SKEKGPSMKE PNPISPPIFH
GLDTLTVMGI AFAAFVIGAL LTGALWYIYS HTGETAGRQQ VPTSPPASEN SSAAHSIGST
QSTPCSSSST A
//
