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TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)

 TGFR2_CHICK             Reviewed;         557 AA.
Q90999;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 143.
RecName: Full=TGF-beta receptor type-2;
Short=TGFR-2;
EC=2.7.11.30;
AltName: Full=TGF-beta type II receptor;
AltName: Full=Transforming growth factor-beta receptor type II;
Short=TGF-beta receptor type II;
Short=TbetaR-II;
Flags: Precursor;
Name=TGFBR2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TGF-BETA, AND
TISSUE SPECIFICITY.
TISSUE=Embryonic brain;
PubMed=8167376; DOI=10.1002/aja.1001990103;
Barnett J.V., Moustakas A., Lin W., Wang X.-F., Lin H.Y., Galper J.B.,
Maas R.L.;
"Cloning and developmental expression of the chick type II and type
III TGF beta receptors.";
Dev. Dyn. 199:12-27(1994).
[2]
STRUCTURE BY NMR OF 36-142, AND DISULFIDE BONDS.
PubMed=12589747; DOI=10.1016/S0022-2836(03)00023-8;
Marlow M.S., Brown C.B., Barnett J.V., Krezel A.M.;
"Solution structure of the chick TGFbeta type II receptor ligand-
binding domain.";
J. Mol. Biol. 326:989-997(2003).
-!- FUNCTION: Transmembrane serine/threonine kinase forming with the
TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-
promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and
TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell
surface to the cytoplasm and is thus regulating a plethora of
physiological and pathological processes including cell cycle
arrest in epithelial and hematopoietic cells, control of
mesenchymal cell proliferation and differentiation, wound healing,
extracellular matrix production, immunosuppression and
carcinogenesis. The formation of the receptor complex composed of
2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the
cytokine dimer results in the phosphorylation and the activation
of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
phosphorylates SMAD2 which dissociates from the receptor and
interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently
translocated to the nucleus where it modulates the transcription
of the TGF-beta-regulated genes. This constitutes the canonical
SMAD-dependent TGF-beta signaling cascade. Also involved in non-
canonical, SMAD-independent TGF-beta signaling pathways (By
similarity). {ECO:0000250|UniProtKB:P37173,
ECO:0000269|PubMed:8167376}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands
assemble a functional receptor composed of two TGFBR1 and TGFBR2
heterodimers to form a ligand-receptor heterohexamer.
{ECO:0000250|UniProtKB:P37173}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P37173}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P37173}. Membrane raft
{ECO:0000250|UniProtKB:P37173}.
-!- TISSUE SPECIFICITY: Detected at low levels in embryonic heart,
brain and lung. Detected at high levels in hatchling heart and
lung. {ECO:0000269|PubMed:8167376}.
-!- PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic
domain. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L18784; AAA49091.1; -; mRNA.
PIR; I50429; I50429.
RefSeq; NP_990759.1; NM_205428.1.
UniGene; Gga.2645; -.
PDB; 1KS6; NMR; -; A=36-142.
PDBsum; 1KS6; -.
ProteinModelPortal; Q90999; -.
SMR; Q90999; -.
IntAct; Q90999; 1.
STRING; 9031.ENSGALP00000018634; -.
PaxDb; Q90999; -.
Ensembl; ENSGALT00000037691; ENSGALP00000036896; ENSGALG00000011442.
GeneID; 396399; -.
KEGG; gga:396399; -.
CTD; 7048; -.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000231495; -.
HOVERGEN; HBG104975; -.
InParanoid; Q90999; -.
KO; K04388; -.
OMA; NDMMVTD; -.
OrthoDB; EOG091G03YO; -.
PhylomeDB; Q90999; -.
TreeFam; TF314724; -.
Reactome; R-GGA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-GGA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-GGA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
EvolutionaryTrace; Q90999; -.
PRO; PR:Q90999; -.
Proteomes; UP000000539; Chromosome 2.
Bgee; ENSGALG00000011442; -.
GO; GO:0005901; C:caveola; ISA:AgBase.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0009897; C:external side of plasma membrane; ISA:AgBase.
GO; GO:0031012; C:extracellular matrix; ISM:AgBase.
GO; GO:0016021; C:integral component of membrane; ISA:AgBase.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0045121; C:membrane raft; ISA:AgBase.
GO; GO:0005886; C:plasma membrane; ISA:AgBase.
GO; GO:0043235; C:receptor complex; ISA:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005539; F:glycosaminoglycan binding; ISA:AgBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
GO; GO:0050431; F:transforming growth factor beta binding; IDA:AgBase.
GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:InterPro.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; ISA:AgBase.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISA:AgBase.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IDA:AgBase.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; ISA:AgBase.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0060434; P:bronchus morphogenesis; IEA:Ensembl.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IEP:AgBase.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; IEA:Ensembl.
GO; GO:0001775; P:cell activation; IMP:AgBase.
GO; GO:0016477; P:cell migration; TAS:AgBase.
GO; GO:0045216; P:cell-cell junction organization; ISM:AgBase.
GO; GO:0070483; P:detection of hypoxia; ISM:AgBase.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEP:AgBase.
GO; GO:0003274; P:endocardial cushion fusion; IEA:Ensembl.
GO; GO:0001654; P:eye development; IEP:AgBase.
GO; GO:0060325; P:face morphogenesis; ISM:AgBase.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IEA:Ensembl.
GO; GO:0007507; P:heart development; IDA:AgBase.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:1905317; P:inferior endocardial cushion morphogenesis; IEA:Ensembl.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:1990086; P:lens fiber cell apoptotic process; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEP:AgBase.
GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
GO; GO:0048762; P:mesenchymal cell differentiation; IMP:AgBase.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISM:AgBase.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0002663; P:positive regulation of B cell tolerance induction; IEA:Ensembl.
GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IMP:AgBase.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:AgBase.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; TAS:AgBase.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
GO; GO:1905075; P:positive regulation of occluding junction disassembly; ISS:AgBase.
GO; GO:0050714; P:positive regulation of protein secretion; ISM:AgBase.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISA:AgBase.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:AgBase.
GO; GO:0002666; P:positive regulation of T cell tolerance induction; IEA:Ensembl.
GO; GO:0002651; P:positive regulation of tolerance induction to self antigen; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISA:AgBase.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0070723; P:response to cholesterol; ISA:AgBase.
GO; GO:0042493; P:response to drug; ISA:AgBase.
GO; GO:0001666; P:response to hypoxia; ISM:AgBase.
GO; GO:0032570; P:response to progesterone; ISM:AgBase.
GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
GO; GO:0060440; P:trachea formation; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISA:AgBase.
GO; GO:0003186; P:tricuspid valve morphogenesis; IEA:Ensembl.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
InterPro; IPR017194; Transform_growth_fac-b_typ-2.
InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF08917; ecTbetaR2; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF037393; TGFRII; 1.
PRINTS; PR00653; ACTIVIN2R.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; ATP-binding; Cell membrane;
Complete proteome; Differentiation; Disulfide bond; Glycoprotein;
Growth regulation; Kinase; Magnesium; Manganese; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Serine/threonine-protein kinase; Signal;
Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 557 TGF-beta receptor type-2.
/FTId=PRO_5000142219.
TOPO_DOM 24 155 Extracellular. {ECO:0000255}.
TRANSMEM 156 176 Helical. {ECO:0000255}.
TOPO_DOM 177 557 Cytoplasmic. {ECO:0000255}.
DOMAIN 234 537 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 240 248 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 369 369 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 267 267 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 74 {ECO:0000269|PubMed:12589747}.
DISULFID 44 61 {ECO:0000269|PubMed:12589747}.
DISULFID 51 57 {ECO:0000269|PubMed:12589747}.
DISULFID 67 91 {ECO:0000269|PubMed:12589747}.
DISULFID 111 126 {ECO:0000269|PubMed:12589747}.
DISULFID 128 133 {ECO:0000269|PubMed:12589747}.
STRAND 44 48 {ECO:0000244|PDB:1KS6}.
STRAND 69 71 {ECO:0000244|PDB:1KS6}.
STRAND 74 81 {ECO:0000244|PDB:1KS6}.
STRAND 84 90 {ECO:0000244|PDB:1KS6}.
STRAND 106 110 {ECO:0000244|PDB:1KS6}.
STRAND 114 116 {ECO:0000244|PDB:1KS6}.
STRAND 119 132 {ECO:0000244|PDB:1KS6}.
TURN 133 135 {ECO:0000244|PDB:1KS6}.
SEQUENCE 557 AA; 63308 MW; 0C578ABFAB357DF1 CRC64;
MPPRLRPLLL RVSLWVLVGS SSPALLHDRS KENGLQLPRL CKFCDVKATT CSNQDQCKSN
CNITSICEKN NEVCAAVWRR NDENVTLETI CHDPQKRLYG HMLDDSSSEQ CVMKEKKDDG
GLMFMCSCTG EECNDVLIFS AIDPHKPEEK DEISKVTIIS LVPLLVISVA VIVIFYAYRT
HKKRKLNKAW EKNVKPKKHK DCSDVCAIML DDDHSDISST CANNINHNTE LLPIELDIVV
GKGRFAEVYK AKLKQNTSEQ YETVAVKIFP YEEYASWKTE KDIFSDVNLK HENILQFLTA
EERKTDLGKQ YWLITAFHAR GNLQEYLTRH IISWEDLWKL GGSLARGIAH LHSDHTPCGR
PKTPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPSLSV DDLANSGQVG TARYMAPEVL
ESRMNLENME SFKQTDVYSM ALVLWEMTSR CNGVGEVKEY EPPFGSKVRE HPCVESMKDN
VLRDRGRPEI PSSWLNHQGI QMVCETLIEC WDHDPEARLT AQCVAERFSE FKHHDKLSGR
SCSEEKIPED GSVTTAK


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