ID   TGFR2_PIG               Reviewed;         297 AA.
AC   P38551;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   22-JUL-2008, entry version 63.
DE   RecName: Full=TGF-beta receptor type-2;
DE            EC=2.7.11.30;
DE   AltName: Full=Transforming growth factor-beta receptor type II;
DE            Short=TGF-beta receptor type II;
DE   AltName: Full=TGF-beta type II receptor;
DE   AltName: Full=TbetaR-II;
DE   AltName: Full=TGFR-2;
DE   Flags: Precursor; Fragment;
GN   Name=TGFBR2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92154690; PubMed=1310899; DOI=10.1016/0092-8674(92)90152-3;
RA   Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.;
RT   "Expression cloning of the TGF-beta type II receptor, a functional
RT   transmembrane serine/threonine kinase.";
RL   Cell 68:775-785(1992).
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC       of two type II and two type I transmembrane serine/threonine
CC       kinases. Type II receptors phosphorylate and activate type I
CC       receptors which autophosphorylate, then bind and activate SMAD
CC       transcriptional regulators. Receptor for TGF-beta.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SUBUNIT: Binds to DAXX. Interacts with TCTEX1D4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic
CC       domain.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   HSSP; P37173; 1KTZ.
DR   SMR; P38551; 38-159.
DR   HOVERGEN; P38551; -.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_bd_CS.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR015769; TGF-beta_II_C.
DR   InterPro; IPR015013; TGF_beta_receptor2.
DR   InterPro; IPR001245; Tyr_pkinase.
DR   PANTHER; PTHR23255:SF11; TGF-beta_II_C; 1.
DR   Pfam; PF08917; ecTbetaR2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; PARTIAL.
PE   3: Inferred from homology;
KW   ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24   >297       TGF-beta receptor type-2.
FT                                /FTId=PRO_0000024428.
FT   TOPO_DOM     24    166       Extracellular (Potential).
FT   TRANSMEM    167    187       Potential.
FT   TOPO_DOM    188   >297       Cytoplasmic (Potential).
FT   DOMAIN      244   >297       Protein kinase.
FT   NP_BIND     250    258       ATP (By similarity).
FT   BINDING     277    277       ATP (By similarity).
FT   CARBOHYD     70     70       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     94     94       N-linked (GlcNAc...) (Potential).
FT   DISULFID     51     84       By similarity.
FT   DISULFID     54     71       By similarity.
FT   DISULFID     61     67       By similarity.
FT   DISULFID     77    101       By similarity.
FT   DISULFID    121    136       By similarity.
FT   DISULFID    138    143       By similarity.
FT   NON_TER     297    297
SQ   SEQUENCE   297 AA;  33302 MW;  F9869D3079B66A15 CRC64;
     MGRGLLGGLW PLHVVLWTRI ASTIPPHVPK SVNSDMMVTD SNGAVKLPQL CKFCDVRSST
     CDNQKSCLSN CSITAICEKP QEVCVAVWRK NDENITIETV CDDPKIAYHG FVLDDAASSK
     CIMKERKGSG ETFFMCSCSS DECNDHIIFS EEYATNNPDL LLVIFQVTGV SLLPPLGIAI
     AVIITFYCYR VHRQQKLSPS WDSGKPRKLM EFSEHLAIIL EDDRSDISST CANNINHNTE
     LLPIELDTLV GKGRFAEVYK AKLRQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDL
//