TGBR3_PIG
ID TGBR3_PIG Reviewed; 848 AA.
AC P35054;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
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).
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; L07595; AAA31126.1; -; mRNA.
DR PIR; JC1351; JC1351.
DR RefSeq; NP_999437.1; NM_214272.1.
DR AlphaFoldDB; P35054; -.
DR SMR; P35054; -.
DR STRING; 9823.ENSSSCP00000028383; -.
DR PRIDE; P35054; -.
DR GeneID; 397512; -.
DR KEGG; ssc:397512; -.
DR CTD; 7049; -.
DR eggNOG; ENOG502QWNZ; Eukaryota.
DR InParanoid; P35054; -.
DR OrthoDB; 1263397at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; TAS:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:BHF-UCL.
DR GO; GO:0015026; F:coreceptor activity; ISS:BHF-UCL.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; ISS:BHF-UCL.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; ISS:BHF-UCL.
DR GO; GO:0070123; F:transforming growth factor beta receptor activity, type III; ISS:BHF-UCL.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:BHF-UCL.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
DR GO; GO:0006955; P:immune response; ISS:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:BHF-UCL.
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; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; NAS:BHF-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Membrane; Proteoglycan; Receptor; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..848
FT /note="Transforming growth factor beta receptor type 3"
FT /id="PRO_0000041665"
FT TOPO_DOM 21..784
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 807..848
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 454..729
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 390..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..750
FT /note="Interaction with TGF-beta ligand"
FT /evidence="ECO:0000250"
FT REGION 813..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
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 529
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 544
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
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:0000250"
FT DISULFID 659..729
FT /evidence="ECO:0000250"
FT DISULFID 709..722
FT /evidence="ECO:0000250"
SQ SEQUENCE 848 AA; 93005 MW; 0DD18A78299FE5DF CRC64;
MTLHCVVALF ALISSCLATA GPEPGVQCAL SPVNASHPVQ ALMESFTVLS GCASRGTMGR
PQEVHVLNLR AADQGPGQRQ SEVTLHLNPI SSVHIHHKPV VFLLNSPQPL VWHLKTERLA
VGVSRLFLVS EGSVVHFSSG NFSLSAETEE RNFPHGNEHL LNWARKEYGA VTSFTELKIA
RNIYIKVGED QVFPPTCSIG KNFLSLNYLA EYLQPKPAEG CVVSGRPQEK EVHIIELIAP
NSNPYSAFQV DIIIDIRPSR KDPELVKNLI LILKCKKSVN WVIKSFDVKG NLKVLAPNSI
GFGRESERSM IMTKSVRDDI PSTQEKLLRW ALDNGYSPVT SYTVAPVANR FHLRLENNEE
MRDEEVHTIP PELQILLDPG ALPVLDHPPS GEGAARHGGL PFPFPYIPRR GRQDGGKDRL
PRPKDPVVPS IQLLPGPREP QEAQGSRDVA LSVRCDSEKM LVAVEKDSFQ ASGYPGLELT
LLDPTCKAKT NGTHFILESP LDGCGTRHRR SAPDGVVYYN SIVIQAPPSG DSSGWPDGYE
DLESGDNGFP GDVDEGDVAL SSRPELVVFN CSLRPARHPS RAQDPPTRNV TFSMDLYTTD
LFLAPAQGVF SVAENGHVYV EVSVTKADQE LGFAIQTCFI SPYSNPDRMS DYTIIENICP
KDESVKFYDP KRVHFPIPQA ETDKKRFSFV FKPVFNTSLL FLQCELTLCT KREKEPQKLP
KCVLPDEACT SLDASMIWAM MQNKKTFTKP LAVIHHEVQF KGPSTKESNP ISPPIFHGLD
TLTVMGIAFA AFVIGALLTG ALWYIYSHTG DSAGRQPVPT SPPASENSSA AHSLGSTQST
PCSSSSAA
