TGFR2_CHICK
ID TGFR2_CHICK Reviewed; 557 AA.
AC Q90999;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=TGF-beta receptor type-2;
DE Short=TGFR-2;
DE EC=2.7.11.30;
DE AltName: Full=TGF-beta type II receptor;
DE AltName: Full=Transforming growth factor-beta receptor type II;
DE Short=TGF-beta receptor type II;
DE Short=TbetaR-II;
DE Flags: Precursor;
GN Name=TGFBR2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TGF-BETA, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=8167376; DOI=10.1002/aja.1001990103;
RA Barnett J.V., Moustakas A., Lin W., Wang X.-F., Lin H.Y., Galper J.B.,
RA Maas R.L.;
RT "Cloning and developmental expression of the chick type II and type III TGF
RT beta receptors.";
RL Dev. Dyn. 199:12-27(1994).
RN [2]
RP STRUCTURE BY NMR OF 36-142, AND DISULFIDE BONDS.
RX PubMed=12589747; DOI=10.1016/s0022-2836(03)00023-8;
RA Marlow M.S., Brown C.B., Barnett J.V., Krezel A.M.;
RT "Solution structure of the chick TGFbeta type II receptor ligand-binding
RT domain.";
RL J. Mol. Biol. 326:989-997(2003).
CC -!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
CC beta type I serine/threonine kinase receptor, TGFBR1, the non-
CC promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3.
CC Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to
CC the cytoplasm and is thus regulating a plethora of physiological and
CC pathological processes including cell cycle arrest in epithelial and
CC hematopoietic cells, control of mesenchymal cell proliferation and
CC differentiation, wound healing, extracellular matrix production,
CC immunosuppression and carcinogenesis. The formation of the receptor
CC complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound
CC to the cytokine dimer results in the phosphorylation and the activation
CC of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
CC phosphorylates SMAD2 which dissociates from the receptor and interacts
CC with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the
CC nucleus where it modulates the transcription of the TGF-beta-regulated
CC genes. This constitutes the canonical SMAD-dependent TGF-beta signaling
CC cascade. Also involved in non-canonical, SMAD-independent TGF-beta
CC signaling pathways (By similarity). {ECO:0000250|UniProtKB:P37173,
CC ECO:0000269|PubMed:8167376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands
CC assemble a functional receptor composed of two TGFBR1 and TGFBR2
CC heterodimers to form a ligand-receptor heterohexamer.
CC {ECO:0000250|UniProtKB:P37173}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P37173};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P37173}.
CC Membrane raft {ECO:0000250|UniProtKB:P37173}.
CC -!- TISSUE SPECIFICITY: Detected at low levels in embryonic heart, brain
CC and lung. Detected at high levels in hatchling heart and lung.
CC {ECO:0000269|PubMed:8167376}.
CC -!- PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; L18784; AAA49091.1; -; mRNA.
DR PIR; I50429; I50429.
DR RefSeq; NP_990759.1; NM_205428.1.
DR PDB; 1KS6; NMR; -; A=36-142.
DR PDBsum; 1KS6; -.
DR AlphaFoldDB; Q90999; -.
DR BMRB; Q90999; -.
DR SMR; Q90999; -.
DR IntAct; Q90999; 1.
DR PaxDb; Q90999; -.
DR Ensembl; ENSGALT00000037691; ENSGALP00000036896; ENSGALG00000011442.
DR Ensembl; ENSGALT00000092202; ENSGALP00000074168; ENSGALG00000011442.
DR GeneID; 396399; -.
DR KEGG; gga:396399; -.
DR CTD; 7048; -.
DR VEuPathDB; HostDB:geneid_396399; -.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000157527; -.
DR HOGENOM; CLU_000288_8_3_1; -.
DR InParanoid; Q90999; -.
DR OrthoDB; 426838at2759; -.
DR PhylomeDB; Q90999; -.
DR TreeFam; TF314724; -.
DR Reactome; R-GGA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-GGA-2173789; TGF-beta receptor signaling activates SMADs.
DR EvolutionaryTrace; Q90999; -.
DR PRO; PR:Q90999; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000011442; Expressed in lung and 13 other tissues.
DR ExpressionAtlas; Q90999; baseline and differential.
DR GO; GO:0005901; C:caveola; ISA:AgBase.
DR GO; GO:0009897; C:external side of plasma membrane; ISA:AgBase.
DR GO; GO:0031012; C:extracellular matrix; ISM:AgBase.
DR GO; GO:0016021; C:integral component of membrane; ISA:AgBase.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0045121; C:membrane raft; ISA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISA:AgBase.
DR GO; GO:0043235; C:receptor complex; ISA:AgBase.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:AgBase.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; ISA:AgBase.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:InterPro.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISA:AgBase.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IDA:AgBase.
DR GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0006915; P:apoptotic process; ISA:AgBase.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IEP:AgBase.
DR GO; GO:0001775; P:cell activation; IMP:AgBase.
DR GO; GO:0016477; P:cell migration; TAS:AgBase.
DR GO; GO:0045216; P:cell-cell junction organization; ISM:AgBase.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0070483; P:detection of hypoxia; ISM:AgBase.
DR GO; GO:0048568; P:embryonic organ development; IEP:AgBase.
DR GO; GO:0001654; P:eye development; IEP:AgBase.
DR GO; GO:0060325; P:face morphogenesis; ISM:AgBase.
DR GO; GO:0007507; P:heart development; IDA:AgBase.
DR GO; GO:0030324; P:lung development; IEP:AgBase.
DR GO; GO:0048762; P:mesenchymal cell differentiation; IMP:AgBase.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISM:AgBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:AgBase.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; TAS:AgBase.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISM:AgBase.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISA:AgBase.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:AgBase.
DR GO; GO:1905075; P:positive regulation of tight junction disassembly; ISS:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; ISA:AgBase.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0070723; P:response to cholesterol; ISA:AgBase.
DR GO; GO:0001666; P:response to hypoxia; ISM:AgBase.
DR GO; GO:0032570; P:response to progesterone; ISM:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISA:AgBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISA:AgBase.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF08917; ecTbetaR2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF037393; TGFRII; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; ATP-binding; Cell membrane; Differentiation;
KW Disulfide bond; Glycoprotein; Growth regulation; Kinase; Magnesium;
KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..557
FT /note="TGF-beta receptor type-2"
FT /id="PRO_5000142219"
FT TOPO_DOM 24..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 234..537
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 240..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..74
FT /evidence="ECO:0000269|PubMed:12589747"
FT DISULFID 44..61
FT /evidence="ECO:0000269|PubMed:12589747"
FT DISULFID 51..57
FT /evidence="ECO:0000269|PubMed:12589747"
FT DISULFID 67..91
FT /evidence="ECO:0000269|PubMed:12589747"
FT DISULFID 111..126
FT /evidence="ECO:0000269|PubMed:12589747"
FT DISULFID 128..133
FT /evidence="ECO:0000269|PubMed:12589747"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1KS6"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1KS6"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1KS6"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1KS6"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1KS6"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1KS6"
FT STRAND 119..132
FT /evidence="ECO:0007829|PDB:1KS6"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1KS6"
SQ 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
