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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)

 D2JYI1_HUMAN            Unreviewed;       592 AA.
D2JYI1;
09-FEB-2010, integrated into UniProtKB/TrEMBL.
09-FEB-2010, sequence version 1.
17-JUN-2020, entry version 84.
RecName: Full=TGF-beta receptor type-2 {ECO:0000256|PIRNR:PIRNR037393};
Short=TGFR-2 {ECO:0000256|PIRNR:PIRNR037393};
EC=2.7.11.30 {ECO:0000256|PIRNR:PIRNR037393};
AltName: Full=TGF-beta type II receptor {ECO:0000256|PIRNR:PIRNR037393};
AltName: Full=Transforming growth factor-beta receptor type II {ECO:0000256|PIRNR:PIRNR037393};
Name=TGFBR2 {ECO:0000313|EMBL:ACZ58377.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606 {ECO:0000313|EMBL:ACZ58377.1};
[1] {ECO:0000313|EMBL:ACZ58377.1}
NUCLEOTIDE SEQUENCE.
Rieder M.J., Bertucci C., Stanaway I.B., Johnson E.J., Swanson J.E.,
Siegel D.L., da Ponte S.H., Igartua C., Patterson K., Nickerson D.A.;
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
-!- 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. {ECO:0000256|PIRNR:PIRNR037393}.
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.30;
Evidence={ECO:0000256|SAAS:SAAS01128400};
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-threonine + ATP = [receptor-protein]-O-
phospho-L-threonine + ADP + H(+); Xref=Rhea:RHEA:44880, Rhea:RHEA-
COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.11.30;
Evidence={ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS01128404};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037393}.
Membrane {ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane
protein {ECO:0000256|RuleBase:RU361271}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily.
{ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00595019}.
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EMBL; GU143403; ACZ58377.1; -; Genomic_DNA.
RefSeq; NP_001020018.1; NM_001024847.2.
SMR; D2JYI1; -.
PRIDE; D2JYI1; -.
Antibodypedia; 11570; 790 antibodies.
DNASU; 7048; -.
GeneID; 7048; -.
CTD; 7048; -.
EuPathDB; HostDB:ENSG00000163513.17; -.
PharmGKB; PA36486; -.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
OMA; HQGIQTV; -.
OrthoDB; 426838at2759; -.
PhylomeDB; D2JYI1; -.
SignaLink; D2JYI1; -.
BioGRID-ORCS; 7048; 17 hits in 827 CRISPR screens.
ChiTaRS; TGFBR2; human.
GenomeRNAi; 7048; -.
Bgee; ENSG00000163513; Expressed in metanephric glomerulus and 230 other tissues.
ExpressionAtlas; D2JYI1; baseline and differential.
Genevisible; D2JYI1; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:UniProtKB-UniRule.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
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:0003214; P:cardiac left ventricle morphogenesis; IEA:Ensembl.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0003274; P:endocardial cushion fusion; IEA:Ensembl.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IEA:Ensembl.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; 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:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
GO; GO:0060443; P:mammary gland morphogenesis; IEA:Ensembl.
GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
GO; GO:1990428; P:miRNA transport; IEA:Ensembl.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0003148; P:outflow tract septum morphogenesis; 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:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
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:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
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:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
GO; GO:0062009; P:secondary palate development; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0003186; P:tricuspid valve morphogenesis; IEA:Ensembl.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom_sf.
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.
3: Inferred from homology;
Apoptosis {ECO:0000256|PIRNR:PIRNR037393};
ATP-binding {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|PIRSR:PIRSR037393-
2, ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138218};
Cell membrane {ECO:0000256|PIRNR:PIRNR037393};
Differentiation {ECO:0000256|PIRNR:PIRNR037393};
Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
Growth regulation {ECO:0000256|PIRNR:PIRNR037393};
Kinase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138186};
Magnesium {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
Manganese {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
Membrane {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00488859};
Metal-binding {ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|PIRSR:PIRSR037393-2, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138218};
Receptor {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:ACZ58377.1};
Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138186};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138186};
Transmembrane {ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00488859};
Transmembrane helix {ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00488859}.
SIGNAL 1..23
/evidence="ECO:0000256|SAM:SignalP"
CHAIN 24..592
/note="TGF-beta receptor type-2"
/evidence="ECO:0000256|SAM:SignalP"
/id="PRO_5003033108"
TRANSMEM 185..214
/note="Helical"
/evidence="ECO:0000256|RuleBase:RU361271"
DOMAIN 269..569
/note="Protein kinase"
/evidence="ECO:0000259|PROSITE:PS50011"
NP_BIND 275..283
/note="ATP"
/evidence="ECO:0000256|PIRSR:PIRSR037393-2"
ACT_SITE 404
/note="Proton acceptor"
/evidence="ECO:0000256|PIRSR:PIRSR037393-1"
BINDING 302
/note="ATP"
/evidence="ECO:0000256|PIRSR:PIRSR037393-2"
DISULFID 76..109
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 79..96
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 86..92
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 102..126
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 146..161
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 163..168
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
SEQUENCE 592 AA; 67457 MW; 8ADCBA70F95E1CBB CRC64;
MGRGLLRGLW PLHIVLWTRI ASTIPPHVQK SDVEMEAQKD EIICPSCNRT AHPLRHINND
MIVTDNNGAV KFPQLCKFCD VRFSTCDNQK SCMSNCSITS ICEKPQEVCV AVWRKNDENI
TLETVCHDPK LPYHDFILED AASPKCIMKE KKKPGETFFM CSCSSDECND NIIFSEEYNT
SNPDLLLVIF QVTGISLLPP LGVAISVIII FYCYRVNRQQ KLSSTWETGK TRKLMEFSEH
CAIILEDDRS DISSTCANNI NHNTELLPIE LDTLVGKGRF AEVYKAKLKQ NTSEQFETVA
VKIFPYEEYA SWKTEKDIFS DINLKHENIL QFLTAEERKT ELGKQYWLIT AFHAKGNLQE
YLTRHVISWE DLRKLGSSLA RGIAHLHSDH TPCGRPKMPI VHRDLKSSNI LVKNDLTCCL
CDFGLSLRLD PTLSVDDLAN SGQVGTARYM APEVLESRMN LENVESFKQT DVYSMALVLW
EMTSRCNAVG EVKDYEPPFG SKVREHPCVE SMKDNVLRDR GRPEIPSFWL NHQGIQMVCE
TLTECWDHDP EARLTAQCVA ERFSELEHLD RLSGRSCSEE KIPEDGSLNT TK


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